<< Androgen >> antagonistic effect of estramustine phosphate (EMP) metabolites on wild-type and mutated [[ androgen receptor ]].


Androgen antagonistic effect of << estramustine phosphate >> (EMP) metabolites on wild-type and mutated [[ androgen receptor ]].


Androgen antagonistic effect of estramustine phosphate (<< EMP >>) metabolites on wild-type and mutated [[ androgen receptor ]].


Down-regulation of << prostate-specific antigen >> (PSA) expression, an AR-target gene, by [[ estramustine ]] and bicalutamide was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of prostate-specific antigen (<< PSA >>) expression, an AR-target gene, by [[ estramustine ]] and bicalutamide was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of prostate-specific antigen (PSA) expression, an << AR >>-target gene, by [[ estramustine ]] and bicalutamide was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of << prostate-specific antigen >> (PSA) expression, an AR-target gene, by estramustine and [[ bicalutamide ]] was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of prostate-specific antigen (<< PSA >>) expression, an AR-target gene, by estramustine and [[ bicalutamide ]] was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of prostate-specific antigen (PSA) expression, an << AR >>-target gene, by estramustine and [[ bicalutamide ]] was accompanied by the blockade of the mutated androgen receptor.


Down-regulation of prostate-specific antigen (PSA) expression, an AR-target gene, by << estramustine >> and bicalutamide was accompanied by the blockade of the mutated [[ androgen receptor ]].


Down-regulation of prostate-specific antigen (PSA) expression, an AR-target gene, by estramustine and << bicalutamide >> was accompanied by the blockade of the mutated [[ androgen receptor ]].


Exposure of LNCaP cells to << estramustine >> for 24 hr caused transcriptional inhibition of [[ PSA ]] in a concentration-dependent manner.


The levels of << PSA >> mRNA decreased 56 and 90% when LNCaP cells were treated with 5 and 10 microM of [[ estramustine ]], respectively (IC50 = 10.97 +/- 1.68 microM).


Binding of << hydroxyflutamide >> to m-AR in LNCaP cells resulted in a concentration-dependent stimulation of [[ PSA ]] expression, suggesting that hydroxyflutamide acted as an agonist of the m-AR.


Binding of hydroxyflutamide to m-AR in LNCaP cells resulted in a concentration-dependent stimulation of PSA expression, suggesting that << hydroxyflutamide >> acted as an agonist of the m-[[ AR ]].


Our data indicate that << estramustine phosphate >> metabolites perform as androgen antagonists of [[ AR ]], an additional mechanism involved in the therapeutic effect of estramustine phosphate in patients with prostate cancer.


Our data indicate that estramustine phosphate metabolites perform as << androgen >> antagonists of [[ AR ]], an additional mechanism involved in the therapeutic effect of estramustine phosphate in patients with prostate cancer.


In order to address one aspect of the feasibility of performing time-resolved studies on AChE, a data set has been collected using the Laue technique on a trigonal crystal of << Torpedo californica AChE >> soaked with the reversible inhibitor [[ edrophonium ]], using a total X-ray exposure time of 24 ms.


Selective inhibition of << cyclooxygenase 2 >> spares renal function and [[ prostaglandin ]] synthesis in cirrhotic rats with ascites.


The current study evaluates the effects of a selective << COX-2 >> inhibitor ([[ SC-236 ]]) on renal function in cirrhotic rats with ascites.


RESULTS: Administration of SC-236 to cirrhotic animals did not produce significant renal effects, whereas administration of the nonselective << COX-1 >>/COX-2 inhibitor, [[ ketorolac ]], resulted in a marked reduction in urine volume, urinary excretion of prostaglandins, and glomerular filtration rate and in a significant impairment in renal water metabolism.


RESULTS: Administration of SC-236 to cirrhotic animals did not produce significant renal effects, whereas administration of the nonselective COX-1/<< COX-2 >> inhibitor, [[ ketorolac ]], resulted in a marked reduction in urine volume, urinary excretion of prostaglandins, and glomerular filtration rate and in a significant impairment in renal water metabolism.


RESULTS: Administration of SC-236 to cirrhotic animals did not produce significant renal effects, whereas administration of the nonselective << COX-1 >>/COX-2 inhibitor, ketorolac, resulted in a marked reduction in urine volume, urinary excretion of [[ prostaglandins ]], and glomerular filtration rate and in a significant impairment in renal water metabolism.


RESULTS: Administration of SC-236 to cirrhotic animals did not produce significant renal effects, whereas administration of the nonselective COX-1/<< COX-2 >> inhibitor, ketorolac, resulted in a marked reduction in urine volume, urinary excretion of [[ prostaglandins ]], and glomerular filtration rate and in a significant impairment in renal water metabolism.


Inhibition of << cPLA2 >> translocation and leukotriene C4 secretion by [[ fluticasone propionate ]] in exogenously activated human eosinophils.


FMLP/CB-stimulated translocation of << cPLA2 >> to the nuclear envelope assessed by specific immunohistochemical staining also was blocked by [[ FP ]].


We find that << FP >> causes a decrease in stimulated eosinophil secretion of LTC4 that is regulated by [[ phospholipase A2 ]] (PLA2).


We find that FP causes a decrease in stimulated eosinophil secretion of << LTC4 >> that is regulated by [[ phospholipase A2 ]] (PLA2).


We find that FP causes a decrease in stimulated eosinophil secretion of << LTC4 >> that is regulated by phospholipase A2 ([[ PLA2 ]]).


Inhibition of LTC4 synthesis precedes the global cytotoxic effects of << FP >> as indicated by the simultaneous upregulation of [[ annexin-1 ]] expression.


<< Desipramine >> treatment decreases 3H-nisoxetine binding and [[ norepinephrine transporter ]] mRNA in SK-N-SHSY5Y cells.


The antidepressant << desipramine >> has been shown to decrease synaptic membrane concentrations of the norepinephrine re-uptake transporter ([[ NET ]]) in vivo and in vitro, on both an acute and a chronic basis.


The antidepressant << desipramine >> has been shown to decrease synaptic membrane concentrations of the [[ norepinephrine re-uptake transporter ]] (NET) in vivo and in vitro, on both an acute and a chronic basis.


We conclude that decreased NET synthesis may contribute to the chronic, but not acute, effect of << desipramine >> to downregulate the [[ NET ]].


Inhibition of the << human ether-a-go-go-related gene (HERG) potassium channel >> by [[ cisapride ]]: affinity for open and inactivated states.


2 In a chronic transfection model using CHO-K1 cells, << cisapride >> inhibited [[ HERG ]] tail currents after a step to +25 mV with similar potency at room and physiological temperatures (IC50 16. 4 nM at 20-22 degrees C and 23.6 nM at 37 degrees C).


6 In conclusion, << HERG >> channel inhibition by [[ cisapride ]] exhibits features consistent with open and inactivated state binding and is sensitive to external potassium concentration.


While it is an antagonist at these latter receptors, << ziprasidone >> behaves as a [[ 5-HT1A ]] agonist in vitro in adenylate cyclase measurements.


Pretreatment with the << 5-HT1A >> antagonist [[ WAY-100,635 ]] (10 micrograms/kg i.v.) prevented the ziprasidone-induced inhibition; the same dose of WAY-100,635 had little effect on the inhibition produced by clozapine and olanzapine.


Pretreatment with the << 5-HT1A >> antagonist WAY-100,635 (10 micrograms/kg i.v.) prevented the ziprasidone-induced inhibition; the same dose of [[ WAY-100,635 ]] had little effect on the inhibition produced by clozapine and olanzapine.


These profiles suggest a mechanism of action for each agent, << 5-HT1A >> agonism for [[ ziprasidone ]] and alpha 1 antagonism for clozapine and olanzapine.


The << 5-HT1A >> agonist activity reported here clearly distinguishes [[ ziprasidone ]] from currently available antipsychotic agents and suggests that this property may play a significant role in its pharmacologic actions.


The nonselective and irreversible << MAO >> inhibitors, [[ phenelzine ]] (3-10 mg/kg), tranylcypromine (1-3 mg/kg), and nialamide (30 mg/kg), decreased rates of responding maintained by ethanol reinforcement.


The nonselective and irreversible << MAO >> inhibitors, phenelzine (3-10 mg/kg), [[ tranylcypromine ]] (1-3 mg/kg), and nialamide (30 mg/kg), decreased rates of responding maintained by ethanol reinforcement.


The nonselective and irreversible << MAO >> inhibitors, phenelzine (3-10 mg/kg), tranylcypromine (1-3 mg/kg), and [[ nialamide ]] (30 mg/kg), decreased rates of responding maintained by ethanol reinforcement.


The reversible << MAO-A >> inhibitor, [[ befloxatone ]] (0.3-3 mg/kg), and the irreversible MAO-A inhibitor, clorgyline (10-30 mg/kg), also reduced ethanol self-administration.


The reversible MAO-A inhibitor, befloxatone (0.3-3 mg/kg), and the irreversible << MAO-A >> inhibitor, [[ clorgyline ]] (10-30 mg/kg), also reduced ethanol self-administration.


The irreversible << MAO-B >> inhibitors, [[ pargyline ]] (30 mg/kg) and l-deprenyl (3-10 mg/kg) also decreased responding maintained by ethanol reinforcement; these results are consistent with previous findings that both drugs decreased ethanol intake in mice.


The irreversible << MAO-B >> inhibitors, pargyline (30 mg/kg) and [[ l-deprenyl ]] (3-10 mg/kg) also decreased responding maintained by ethanol reinforcement; these results are consistent with previous findings that both drugs decreased ethanol intake in mice.


<< Dicumarol >>, a potent inhibitor of [[ quinone oxidoreductase ]], at high concentration (500 microm ) caused only a 72% decrease in the utilization of resorufin.


Activity of the mutant << delta-aminolevulinate synthase >> protein expressed in vitro was 15.1% compared with the normal control, but was increased up to 34.5% by the addition of [[ pyridoxal 5'-phosphate ]], consistent with the clinical response of the patient to pyridoxine treatment.


Preferential cerebrospinal fluid << acetylcholinesterase >> inhibition by [[ rivastigmine ]] in humans.


Inhibition of << AChE >> in the CSF after [[ rivastigmine ]] administration was significantly greater than after placebo for up to 8.4 hours after the dose and was maximal (40%) at 2.4 hours.


Plasma << BuChE >> activity was significantly lower after [[ rivastigmine ]] than after placebo, but this was not clinically relevant.


<< BuChE >> activity in CSF was significantly lower after [[ rivastigmine ]] than after placebo for up to 3.6 hours after dosing, but this difference was not sustained.


This study confirms the feasibility of using continuous measurement of AChE activity in CSF over prolonged periods, that << rivastigmine >> markedly inhibits CSF [[ AChE ]] after a single oral dose of 3 mg, and that the inhibition of central AChE is substantially greater than that of peripheral AChE or BuChE.


This study confirms the feasibility of using continuous measurement of AChE activity in CSF over prolonged periods, that << rivastigmine >> markedly inhibits CSF AChE after a single oral dose of 3 mg, and that the inhibition of central [[ AChE ]] is substantially greater than that of peripheral AChE or BuChE.


This study confirms the feasibility of using continuous measurement of AChE activity in CSF over prolonged periods, that << rivastigmine >> markedly inhibits CSF AChE after a single oral dose of 3 mg, and that the inhibition of central AChE is substantially greater than that of peripheral [[ AChE ]] or BuChE.


This study confirms the feasibility of using continuous measurement of AChE activity in CSF over prolonged periods, that << rivastigmine >> markedly inhibits CSF AChE after a single oral dose of 3 mg, and that the inhibition of central AChE is substantially greater than that of peripheral AChE or [[ BuChE ]].


Agonist and antagonist actions of << yohimbine >> as compared to fluparoxan at alpha(2)-adrenergic receptors [[ (AR)s ]], serotonin (5-HT)(1A), 5-HT(1B), 5-HT(1D) and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of << yohimbine >> as compared to fluparoxan at alpha(2)-adrenergic receptors (AR)s, serotonin [[ (5-HT)(1A) ]], 5-HT(1B), 5-HT(1D) and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of << yohimbine >> as compared to fluparoxan at alpha(2)-adrenergic receptors (AR)s, serotonin (5-HT)(1A), [[ 5-HT(1B) ]], 5-HT(1D) and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of << yohimbine >> as compared to fluparoxan at alpha(2)-adrenergic receptors (AR)s, serotonin (5-HT)(1A), 5-HT(1B), [[ 5-HT(1D) ]] and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of << yohimbine >> as compared to fluparoxan at [[ alpha(2)-adrenergic receptors ]] (AR)s, serotonin (5-HT)(1A), 5-HT(1B), 5-HT(1D) and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of yohimbine as compared to << fluparoxan >> at alpha(2)-adrenergic receptors [[ (AR)s ]], serotonin (5-HT)(1A), 5-HT(1B), 5-HT(1D) and dopamine D(2) and D(3) receptors.


Agonist and antagonist actions of yohimbine as compared to << fluparoxan >> at [[ alpha(2)-adrenergic receptors ]] (AR)s, serotonin (5-HT)(1A), 5-HT(1B), 5-HT(1D) and dopamine D(2) and D(3) receptors.


Herein, we evaluate the interaction of the << alpha(2)-AR antagonist >>, [[ yohimbine ]], as compared to fluparoxan, at multiple monoaminergic receptors and examine their roles in the modulation of adrenergic, dopaminergic and serotonergic transmission in freely-moving rats.


Herein, we evaluate the interaction of the << alpha(2)-AR antagonist >>, yohimbine, as compared to [[ fluparoxan ]], at multiple monoaminergic receptors and examine their roles in the modulation of adrenergic, dopaminergic and serotonergic transmission in freely-moving rats.


In [(35)S]GTPgammaS binding protocols, << yohimbine >> exerts antagonist actions at halpha(2A)-AR, h5-HT(1B), h5-HT(1D), and hD(2) sites, yet partial agonist actions at [[ h5-HT(1A) ]] sites.


In [(35)S]GTPgammaS binding protocols, << yohimbine >> exerts antagonist actions at [[ halpha(2A)-AR ]], h5-HT(1B), h5-HT(1D), and hD(2) sites, yet partial agonist actions at h5-HT(1A) sites.


In [(35)S]GTPgammaS binding protocols, << yohimbine >> exerts antagonist actions at halpha(2A)-AR, [[ h5-HT(1B) ]], h5-HT(1D), and hD(2) sites, yet partial agonist actions at h5-HT(1A) sites.


In [(35)S]GTPgammaS binding protocols, << yohimbine >> exerts antagonist actions at halpha(2A)-AR, h5-HT(1B), [[ h5-HT(1D) ]], and hD(2) sites, yet partial agonist actions at h5-HT(1A) sites.


In [(35)S]GTPgammaS binding protocols, << yohimbine >> exerts antagonist actions at halpha(2A)-AR, h5-HT(1B), h5-HT(1D), and [[ hD(2) ]] sites, yet partial agonist actions at h5-HT(1A) sites.


In vivo, agonist actions of << yohimbine >> at [[ 5-HT(1A) ]] sites are revealed by WAY100,635-reversible induction of hypothermia in the rat.


In vivo, agonist actions of yohimbine at << 5-HT(1A) >> sites are revealed by [[ WAY100,635 ]]-reversible induction of hypothermia in the rat.


In guinea pigs, antagonist actions of yohimbine at 5-HT(1B) receptors are revealed by blockade of hypothermia evoked by the << 5-HT(1B) >> agonist, [[ GR46,611 ]].


In guinea pigs, antagonist actions of << yohimbine >> at [[ 5-HT(1B) ]] receptors are revealed by blockade of hypothermia evoked by the 5-HT(1B) agonist, GR46,611.


In distinction to << yohimbine >>, fluparoxan shows only modest partial agonist actions at [[ h5-HT(1A) ]] sites versus marked antagonist actions at halpha(2)-ARs.


In distinction to yohimbine, << fluparoxan >> shows only modest partial agonist actions at [[ h5-HT(1A) ]] sites versus marked antagonist actions at halpha(2)-ARs.


In distinction to << yohimbine >>, fluparoxan shows only modest partial agonist actions at h5-HT(1A) sites versus marked antagonist actions at [[ halpha(2)-ARs ]].


In distinction to yohimbine, << fluparoxan >> shows only modest partial agonist actions at h5-HT(1A) sites versus marked antagonist actions at [[ halpha(2)-ARs ]].


In conclusion, the << alpha(2)-AR >> antagonist properties of [[ yohimbine ]] increase DA and NAD levels both alone and in association with fluoxetine.


However, in contrast to the selective alpha(2)-AR antagonist, fluparoxan, the << 5-HT(1A) >> agonist actions of [[ yohimbine ]] suppress 5-HT levels alone and underlie its inability to augment the influence of fluoxetine upon 5-HT levels.


However, in contrast to the selective << alpha(2)-AR >> antagonist, [[ fluparoxan ]], the 5-HT(1A) agonist actions of yohimbine suppress 5-HT levels alone and underlie its inability to augment the influence of fluoxetine upon 5-HT levels.


In this study, the activity of the << delta-opioid receptor >> subtype-selective agonist, [[ SB 227122 ]], was investigated in a guinea pig model of citric acid-induced cough.


Parenteral administration of selective agonists of the delta-opioid receptor (SB 227122), mu-opioid receptor (codeine and hydrocodone), and << kappa-opioid receptor >> ([[ BRL 52974 ]]) produced dose-related inhibition of citric acid-induced cough with ED(50) values of 7.3, 5.2, 5.1, and 5.3 mg/kg, respectively.


Parenteral administration of selective agonists of the << delta-opioid receptor >> ([[ SB 227122 ]]), mu-opioid receptor (codeine and hydrocodone), and kappa-opioid receptor (BRL 52974) produced dose-related inhibition of citric acid-induced cough with ED(50) values of 7.3, 5.2, 5.1, and 5.3 mg/kg, respectively.


Parenteral administration of selective agonists of the delta-opioid receptor (SB 227122), << mu-opioid receptor >> ([[ codeine ]] and hydrocodone), and kappa-opioid receptor (BRL 52974) produced dose-related inhibition of citric acid-induced cough with ED(50) values of 7.3, 5.2, 5.1, and 5.3 mg/kg, respectively.


Parenteral administration of selective agonists of the delta-opioid receptor (SB 227122), << mu-opioid receptor >> (codeine and [[ hydrocodone ]]), and kappa-opioid receptor (BRL 52974) produced dose-related inhibition of citric acid-induced cough with ED(50) values of 7.3, 5.2, 5.1, and 5.3 mg/kg, respectively.


The nonselective << opioid receptor >> antagonist, naloxone (3 mg/kg, i.m.), attenuated the antitussive effects of [[ codeine ]] or SB 227122, indicating that the antitussive activity of both compounds is opioid receptor-mediated.


The nonselective opioid receptor antagonist, naloxone (3 mg/kg, i.m.), attenuated the antitussive effects of << codeine >> or SB 227122, indicating that the antitussive activity of both compounds is [[ opioid receptor ]]-mediated.


The nonselective << opioid receptor >> antagonist, naloxone (3 mg/kg, i.m.), attenuated the antitussive effects of codeine or [[ SB 227122 ]], indicating that the antitussive activity of both compounds is opioid receptor-mediated.


The nonselective opioid receptor antagonist, naloxone (3 mg/kg, i.m.), attenuated the antitussive effects of codeine or << SB 227122 >>, indicating that the antitussive activity of both compounds is [[ opioid receptor ]]-mediated.


The nonselective << opioid receptor >> antagonist, [[ naloxone ]] (3 mg/kg, i.m.), attenuated the antitussive effects of codeine or SB 227122, indicating that the antitussive activity of both compounds is opioid receptor-mediated.


The << delta-receptor >> antagonist, SB 244525 (10 mg/kg, i.p.), inhibited the antitussive effect of [[ SB 227122 ]] (20 mg/kg, i.p.).


The << delta-receptor >> antagonist, [[ SB 244525 ]] (10 mg/kg, i.p.), inhibited the antitussive effect of SB 227122 (20 mg/kg, i.p.).


In contrast, combined pretreatment with << beta-funaltrexamine >> ([[ mu-receptor ]] antagonist; 20 mg/kg, s.c.) and norbinaltorphimine (kappa-receptor antagonist; 20 mg/kg, s.c.), at doses that inhibited the antitussive activity of mu- and kappa-receptor agonists, respectively, was without effect on the antitussive response of SB 227122 (20 mg/kg, i.p.).


In contrast, combined pretreatment with beta-funaltrexamine (mu-receptor antagonist; 20 mg/kg, s.c.) and << norbinaltorphimine >> ([[ kappa-receptor ]] antagonist; 20 mg/kg, s.c.), at doses that inhibited the antitussive activity of mu- and kappa-receptor agonists, respectively, was without effect on the antitussive response of SB 227122 (20 mg/kg, i.p.).


The << sigma-receptor >> antagonist rimcazole (3 mg/kg, i.p.) inhibited the antitussive effect of [[ dextromethorphan ]] (30 mg/kg, i.p.), a sigma-receptor agonist, but not that of SB 227122.


The << sigma-receptor >> antagonist [[ rimcazole ]] (3 mg/kg, i.p.) inhibited the antitussive effect of dextromethorphan (30 mg/kg, i.p.), a sigma-receptor agonist, but not that of SB 227122.


These studies provide compelling evidence that the antitussive effects of << SB 227122 >> in this guinea pig cough model are mediated by agonist activity at the [[ delta-opioid receptor ]].


New modes of therapy have recently been introduced, and data on the << cyclooxygenase-2 >> (COX-2)-specific inhibitors [[ celecoxib ]] and rofecoxib suggest that these agents will meet the need for safe and effective therapeutic alternatives to conventional NSAIDs.


New modes of therapy have recently been introduced, and data on the cyclooxygenase-2 (<< COX-2 >>)-specific inhibitors [[ celecoxib ]] and rofecoxib suggest that these agents will meet the need for safe and effective therapeutic alternatives to conventional NSAIDs.


New modes of therapy have recently been introduced, and data on the << cyclooxygenase-2 >> (COX-2)-specific inhibitors celecoxib and [[ rofecoxib ]] suggest that these agents will meet the need for safe and effective therapeutic alternatives to conventional NSAIDs.


New modes of therapy have recently been introduced, and data on the cyclooxygenase-2 (<< COX-2 >>)-specific inhibitors celecoxib and [[ rofecoxib ]] suggest that these agents will meet the need for safe and effective therapeutic alternatives to conventional NSAIDs.


Kinetics of inhibition of << human and rat dihydroorotate dehydrogenase >> by atovaquone, lawsone derivatives, [[ brequinar sodium ]] and polyporic acid.


Kinetics of inhibition of << human and rat dihydroorotate dehydrogenase >> by atovaquone, lawsone derivatives, brequinar sodium and [[ polyporic acid ]].


Kinetics of inhibition of << human and rat dihydroorotate dehydrogenase >> by [[ atovaquone ]], lawsone derivatives, brequinar sodium and polyporic acid.


Kinetics of inhibition of << human and rat dihydroorotate dehydrogenase >> by atovaquone, [[ lawsone ]] derivatives, brequinar sodium and polyporic acid.


Mitochondrially-bound << dihydroorotate dehydrogenase >> (EC 1.3.99.11) catalyzes the fourth sequential step in the de novo synthesis of [[ uridine monophosphate ]].


Mitochondrially-bound dihydroorotate dehydrogenase (<< EC 1.3.99.11 >>) catalyzes the fourth sequential step in the de novo synthesis of [[ uridine monophosphate ]].


With respect to the quinone co-substrate of the dihydroorotate dehydrogenase, << atovaquone >> (Kic = 2.7 microM) and dichloroally-lawsone (Kic = 9.8 nM) were shown to be competitive inhibitors of [[ human dihydroorotate dehydrogenase ]].


With respect to the quinone co-substrate of the dihydroorotate dehydrogenase, atovaquone (Kic = 2.7 microM) and << dichloroally-lawsone >> (Kic = 9.8 nM) were shown to be competitive inhibitors of [[ human dihydroorotate dehydrogenase ]].


With respect to the << quinone >> co-substrate of the [[ dihydroorotate dehydrogenase ]], atovaquone (Kic = 2.7 microM) and dichloroally-lawsone (Kic = 9.8 nM) were shown to be competitive inhibitors of human dihydroorotate dehydrogenase.


<< Dichloroally]-lawsone >> was found to be a time-dependent inhibitor of the rat enzyme, with the lowest inhibition constant (Ki* = 0.77 nM) determined so far for [[ mammalian dihydroorotate dehydrogenases ]].


Another inhibitor, << brequinar >> was previously reported to be a slow-binding inhibitor of the [[ human dihydroorotate dehydrogenase ]] [W. Knecht, M. Loffler, Species-related inhibition of human and rat dihyroorotate dehydrogenase by immunosuppressive isoxazol and cinchoninic acid derivatives, Biochem. Pharmacol. 56 (1998) 1259-1264].


Another inhibitor, brequinar was previously reported to be a slow-binding inhibitor of the human dihydroorotate dehydrogenase [W. Knecht, M. Loffler, Species-related inhibition of << human and rat dihyroorotate dehydrogenase >> by immunosuppressive [[ isoxazol ]] and cinchoninic acid derivatives, Biochem. Pharmacol. 56 (1998) 1259-1264].


Another inhibitor, brequinar was previously reported to be a slow-binding inhibitor of the human dihydroorotate dehydrogenase [W. Knecht, M. Loffler, Species-related inhibition of << human and rat dihyroorotate dehydrogenase >> by immunosuppressive isoxazol and [[ cinchoninic acid ]] derivatives, Biochem. Pharmacol. 56 (1998) 1259-1264].


With respect to the substrate << dihydroorotate >>, atovaquone was an uncompetitive inhibitor of [[ human dihydroorotate dehydrogenase ]] (Kiu = 11.6 microM) and a non-competitive inhibitor of the rat enzyme (Kiu = 905/ Kic = 1,012 nM).


With respect to the substrate dihydroorotate, << atovaquone >> was an uncompetitive inhibitor of [[ human dihydroorotate dehydrogenase ]] (Kiu = 11.6 microM) and a non-competitive inhibitor of the rat enzyme (Kiu = 905/ Kic = 1,012 nM).


Determinants of voltage-dependent inactivation affect << Mibefradil >> block of [[ calcium channels ]].


<< Mibefradil >> (Ro 40-5967) belongs to a new chemical class of these molecules which differs from other Ca2+ antagonists by its ability to potently block [[ T-type Ca2+ channels ]].


Mibefradil (<< Ro 40-5967 >>) belongs to a new chemical class of these molecules which differs from other Ca2+ antagonists by its ability to potently block [[ T-type Ca2+ channels ]].


<< Mibefradil >> blocked alpha1A and alpha1E with a Kd comparable to that reported for [[ T-type channels ]], but had a lower affinity (approximately 30-fold) for alpha1C.


Postoperative concentrations of << plasminogen >> were decreased significantly in the [[ tranexamic acid ]] group (P < 0.001).


Iontophoresis of << +/- propranolol >>, whose serotonergic actions include antagonism and partial agonism at [[ 5-HT1 ]] receptors, also increased serotonin and decreased firing (n=4).


<< Methiothepin >> (intravenous, 1 mg/kg), whose serotonergic actions include [[ 5-HT1 ]] and 5-HT2 antagonism, typically raised serotonin levels (four of five cells) and always blocked inhibition by clomipramine (n = 3).


<< Methiothepin >> (intravenous, 1 mg/kg), whose serotonergic actions include 5-HT1 and [[ 5-HT2 ]] antagonism, typically raised serotonin levels (four of five cells) and always blocked inhibition by clomipramine (n = 3).


The << Hsp90 >>-specific inhibitor [[ geldanamycin ]] selectively disrupts kinase-mediated signaling events of T-lymphocyte activation.


The Hsp90-specific inhibitor << geldanamycin >> selectively disrupts [[ kinase ]]-mediated signaling events of T-lymphocyte activation.


Improper function of these proteins can be induced by selective disruption of their complexes with << Hsp90 >> using the [[ benzoquinonoid ansamycin ]] geldanamycin.


Improper function of these proteins can be induced by selective disruption of their complexes with << Hsp90 >> using the benzoquinonoid ansamycin [[ geldanamycin ]].


In this study, we demonstrate that << geldanamycin >> treatment blocks [[ interleukin (IL)-2 ]] secretion, IL-2 receptor expression, and proliferation of stimulated T-lymphocytes.


In this study, we demonstrate that << geldanamycin >> treatment blocks interleukin (IL)-2 secretion, [[ IL-2 receptor ]] expression, and proliferation of stimulated T-lymphocytes.


Moreover, << geldanamycin >> decreases the amount and phosphorylation of [[ Lck ]] and Raf-1 kinases and prevents activation of the extracellular signal regulated kinase (ERK)-2 kinase.


Moreover, << geldanamycin >> decreases the amount and phosphorylation of Lck and [[ Raf-1 ]] kinases and prevents activation of the extracellular signal regulated kinase (ERK)-2 kinase.


Moreover, << geldanamycin >> decreases the amount and phosphorylation of Lck and Raf-1 [[ kinases ]] and prevents activation of the extracellular signal regulated kinase (ERK)-2 kinase.


Moreover, << geldanamycin >> decreases the amount and phosphorylation of Lck and Raf-1 kinases and prevents activation of the [[ extracellular signal regulated kinase (ERK)-2 ]] kinase.


Moreover, << geldanamycin >> decreases the amount and phosphorylation of Lck and Raf-1 kinases and prevents activation of the extracellular signal regulated kinase (ERK)-2 [[ kinase ]].


<< Geldanamycin >> also disrupts the [[ T-cell receptor ]]-mediated activation of nuclear factor of activated T-cells (NF-AT).


<< Geldanamycin >> also disrupts the T-cell receptor-mediated activation of [[ nuclear factor of activated T-cells ]] (NF-AT).


<< Geldanamycin >> also disrupts the T-cell receptor-mediated activation of nuclear factor of activated T-cells ([[ NF-AT ]]).


Through demonstrating the selective inhibition of << kinase >>-related T-lymphocyte responses by [[ geldanamycin ]], our results emphasize the substantial role of Hsp90-kinase complexes in T-cell activation.


<< gamma-Butyrobetaine hydroxylase >> catalyse the last step in [[ carnitine ]] biosynthesis, the formation of L-carnitine from gamma-butyrobetaine, a reaction dependent on Fe2+, alpha-ketoglutarate, ascorbate and oxygen.


<< gamma-Butyrobetaine hydroxylase >> catalyse the last step in carnitine biosynthesis, the formation of [[ L-carnitine ]] from gamma-butyrobetaine, a reaction dependent on Fe2+, alpha-ketoglutarate, ascorbate and oxygen.


<< gamma-Butyrobetaine hydroxylase >> catalyse the last step in carnitine biosynthesis, the formation of L-carnitine from [[ gamma-butyrobetaine ]], a reaction dependent on Fe2+, alpha-ketoglutarate, ascorbate and oxygen.


Inhibition of the actions of << ET-1 >> by [[ salicylates ]] is apparently competitive.


A unique cytosolic activity related but distinct from << NQO1 >> catalyses metabolic activation of [[ mitomycin C ]].


Among the various enzymes, << dicoumarol >> inhibitable cytosolic [[ NAD(P)H:quinone oxidoreductase1 ]] (NQO1) was shown to catalyse bioreductive activation of MMC leading to cross-linking of the DNA and cytotoxicity.


Among the various enzymes, << dicoumarol >> inhibitable cytosolic NAD(P)H:quinone oxidoreductase1 ([[ NQO1 ]]) was shown to catalyse bioreductive activation of MMC leading to cross-linking of the DNA and cytotoxicity.


Among the various enzymes, dicoumarol inhibitable cytosolic << NAD(P)H:quinone oxidoreductase1 >> (NQO1) was shown to catalyse bioreductive activation of [[ MMC ]] leading to cross-linking of the DNA and cytotoxicity.


Among the various enzymes, dicoumarol inhibitable cytosolic NAD(P)H:quinone oxidoreductase1 (<< NQO1 >>) was shown to catalyse bioreductive activation of [[ MMC ]] leading to cross-linking of the DNA and cytotoxicity.


However, the role of << NQO1 >> in metabolic activation of [[ MMC ]] has been disputed.


In this report, we present cellular and animal models to demonstrate that << NQO1 >> may play only a minor role in metabolic activation of [[ MMC ]].


This activity, like << NQO1 >>, was inhibited by [[ dicoumarol ]] and immunologically related to NQO1.


<< Troglitazone >> reduces [[ plasminogen activator inhibitor-1 ]] expression and secretion in cultured human adipocytes.


RESULTS: Exposure of in vitro differentiated subcutaneous adipocytes from young normal-weight females to 1 microgram/ml << troglitazone >> for 72 h caused a reduction of both [[ PAI-1 ]] secretion (by 29 +/- 5%; p < 0.01) and PAI-1 mRNA expression (by 26 +/- 3%; p < 0.05).


RESULTS: Exposure of in vitro differentiated subcutaneous adipocytes from young normal-weight females to 1 microgram/ml << troglitazone >> for 72 h caused a reduction of both PAI-1 secretion (by 29 +/- 5%; p < 0.01) and [[ PAI-1 ]] mRNA expression (by 26 +/- 3%; p < 0.05).


In cultures from severely obese subjects, << troglitazone >> induced a decrease of [[ PAI-1 ]] antigen secretion from newly differentiated omental adipocytes by 49 +/- 8% (p < 0.01) and from subcutaneous adipocytes by 30 +/- 7% (p < 0.05).


Exposure of freshly isolated subcutaneous and omental adipocytes in suspension culture to << troglitazone >> induced a similar reduction of [[ PAI-1 ]] concentration in the culture medium (by 35 +/- 11%, p < 0.05, and 33 +/- 8%, p < 0.05 compared with control, respectively).


CONCLUSION/INTERPRETATION: This study provides evidence that << troglitazone >> reduces [[ PAI-1 ]] production in human adipocytes, probably at the transcriptional level.


We examined the effect of JTH-601 (3- inverted question mark<< N-[2-(4-hydroxy-2-isopropyl-5-methylphenoxy)ethyl]-N-methylaminom >> ethyl inverted question mark-4-methoxy-2,5,6-trimethylphenol hemifumarate), a new [[ alpha(1L)-adrenoceptor ]] antagonist, on prostatic function in isolated canine prostate and in anesthetized dogs.


We examined the effect of JTH-601 (3- inverted question markN-[2-(4-hydroxy-2-isopropyl-5-methylphenoxy)ethyl]-N-methylaminom << ethyl >> inverted question mark-4-methoxy-2,5,6-trimethylphenol hemifumarate), a new [[ alpha(1L)-adrenoceptor ]] antagonist, on prostatic function in isolated canine prostate and in anesthetized dogs.


We examined the effect of JTH-601 (3- inverted question markN-[2-(4-hydroxy-2-isopropyl-5-methylphenoxy)ethyl]-N-methylaminom ethyl inverted question mark-<< 4-methoxy-2,5,6-trimethylphenol hemifumarate >>), a new [[ alpha(1L)-adrenoceptor ]] antagonist, on prostatic function in isolated canine prostate and in anesthetized dogs.


We examined the effect of << JTH-601 >> (3- inverted question markN-[2-(4-hydroxy-2-isopropyl-5-methylphenoxy)ethyl]-N-methylaminom ethyl inverted question mark-4-methoxy-2,5,6-trimethylphenol hemifumarate), a new [[ alpha(1L)-adrenoceptor ]] antagonist, on prostatic function in isolated canine prostate and in anesthetized dogs.


In these tissues, << JTH-601 >>, prazosin (a non-selective [[ alpha(1)-adrenoceptor ]] antagonist), and tamsulosin (an alpha(1A)-adrenoceptor antagonist) competitively antagonized contraction in a concentration-dependent manner.


In these tissues, JTH-601, << prazosin >> (a non-selective [[ alpha(1)-adrenoceptor ]] antagonist), and tamsulosin (an alpha(1A)-adrenoceptor antagonist) competitively antagonized contraction in a concentration-dependent manner.


In these tissues, JTH-601, prazosin (a non-selective alpha(1)-adrenoceptor antagonist), and << tamsulosin >> (an [[ alpha(1A)-adrenoceptor ]] antagonist) competitively antagonized contraction in a concentration-dependent manner.


<< JTH-601 >> is expected to be an effective [[ alpha(1)-adrenoceptor ]] antagonist for the treatment of urinary outlet obstruction by benign prostatic hypertrophy with a minimum effect on the cardiovascular system.


The salivary fluid secretory mechanism is thought to require << Na(+)/K(+)/2Cl(-) cotransporter >>-mediated [[ Cl(-) ]] uptake.


These data directly demonstrate that << NKCC1 >> is the major [[ Cl(-) ]] uptake mechanism across the basolateral membrane of acinar cells and is critical for driving saliva secretion in vivo.


UNLABELLED: Apparent << muscarinic acetylcholine (mAch) receptor >> occupancy in mouse cerebral cortex, hippocampus, and striatum by [[ scopolamine ]], an antagonist, and biperiden, a relatively selective M1 antagonist, was estimated with competitive binding studies using two different radioligands: 3H-N-methyl piperidyl benzilate (3H-NMPB) and 3H-quinuclidinyl benzilate (3H-QNB).


UNLABELLED: Apparent muscarinic acetylcholine (mAch) receptor occupancy in mouse cerebral cortex, hippocampus, and striatum by scopolamine, an antagonist, and << biperiden >>, a relatively selective [[ M1 ]] antagonist, was estimated with competitive binding studies using two different radioligands: 3H-N-methyl piperidyl benzilate (3H-NMPB) and 3H-quinuclidinyl benzilate (3H-QNB).


Impaired expression of the uncoupling protein-3 gene in skeletal muscle during lactation: fibrates and << troglitazone >> reverse lactation-induced downregulation of the [[ uncoupling protein-3 ]] gene.


Treatment of lactating mice with a single injection of << bezafibrate >>, an activator of the [[ peroxisome proliferator-activated receptor ]] (PPAR), raises UCP-3 mRNA in skeletal muscle to levels similar to those in virgin mice.


Treatment of lactating mice with a single injection of << bezafibrate >>, an activator of the peroxisome proliferator-activated receptor ([[ PPAR ]]), raises UCP-3 mRNA in skeletal muscle to levels similar to those in virgin mice.


Treatment of lactating mice with a single injection of << bezafibrate >>, an activator of the peroxisome proliferator-activated receptor (PPAR), raises [[ UCP-3 ]] mRNA in skeletal muscle to levels similar to those in virgin mice.


4-chloro-6-[(2,3-xylidine)-pirimidinylthio] acetic acid (WY-14,643), a specific ligand of the PPAR-alpha subtype, causes the most dramatic increase in UCP-3 mRNA, whereas << troglitazone >>, a specific activator of [[ PPAR-gamma ]], also significantly increases UCP-3 mRNA abundance in skeletal muscle of lactating mice.


<< 4-chloro-6-[(2,3-xylidine)-pirimidinylthio] acetic acid >> (WY-14,643), a specific ligand of the PPAR-alpha subtype, causes the most dramatic increase in [[ UCP-3 ]] mRNA, whereas troglitazone, a specific activator of PPAR-gamma, also significantly increases UCP-3 mRNA abundance in skeletal muscle of lactating mice.


4-chloro-6-[(2,3-xylidine)-pirimidinylthio] acetic acid (<< WY-14,643 >>), a specific ligand of the PPAR-alpha subtype, causes the most dramatic increase in [[ UCP-3 ]] mRNA, whereas troglitazone, a specific activator of PPAR-gamma, also significantly increases UCP-3 mRNA abundance in skeletal muscle of lactating mice.


4-chloro-6-[(2,3-xylidine)-pirimidinylthio] acetic acid (WY-14,643), a specific ligand of the PPAR-alpha subtype, causes the most dramatic increase in UCP-3 mRNA, whereas << troglitazone >>, a specific activator of PPAR-gamma, also significantly increases [[ UCP-3 ]] mRNA abundance in skeletal muscle of lactating mice.


It is proposed that the UCP-3 gene is regulated in skeletal muscle during lactation in response to changes in circulating free << fatty acids >> by mechanisms involving activation of [[ PPARs ]].


<< Retigabine >>, a novel anti-convulsant, enhances activation of KCNQ2/Q3 [[ potassium channels ]].


Suppression of << NF-kappaB >> activity by [[ sulfasalazine ]] is mediated by direct inhibition of IkappaB kinases alpha and beta.


The aim of this study was to define the molecular mechanism by which << sulfasalazine >> inhibits [[ NF-kappaB ]] activation.


RESULTS: << NF-kappaB >>/Rel activity induced by tumor necrosis factor alpha, [[ 12-O-tetradecanoylphorbol-13-acetate ]], or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by sulfasalazine.


RESULTS: NF-kappaB/<< Rel >> activity induced by tumor necrosis factor alpha, [[ 12-O-tetradecanoylphorbol-13-acetate ]], or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by sulfasalazine.


RESULTS: << NF-kappaB >>/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/<< Rel >> activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of << NF-kappaB-inducing kinase >>, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, << IKK-alpha >>, IKK-beta, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, IKK-alpha, << IKK-beta >>, or constitutively active IKK-alpha and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active << IKK-alpha >> and IKK-beta mutants was inhibited dose dependently by [[ sulfasalazine ]].


RESULTS: NF-kappaB/Rel activity induced by tumor necrosis factor alpha, 12-O-tetradecanoylphorbol-13-acetate, or overexpression of NF-kappaB-inducing kinase, IKK-alpha, IKK-beta, or constitutively active IKK-alpha and << IKK-beta >> mutants was inhibited dose dependently by [[ sulfasalazine ]].


<< Sulfasalazine >> inhibited [[ tumor necrosis factor alpha ]]-induced activation of endogenous IKK in Jurkat T cells and SW620 colon cells, as well as the catalytic activity of purified IKK-alpha and IKK-beta in vitro.


<< Sulfasalazine >> inhibited tumor necrosis factor alpha-induced activation of endogenous [[ IKK ]] in Jurkat T cells and SW620 colon cells, as well as the catalytic activity of purified IKK-alpha and IKK-beta in vitro.


<< Sulfasalazine >> inhibited tumor necrosis factor alpha-induced activation of endogenous IKK in Jurkat T cells and SW620 colon cells, as well as the catalytic activity of purified [[ IKK-alpha ]] and IKK-beta in vitro.


<< Sulfasalazine >> inhibited tumor necrosis factor alpha-induced activation of endogenous IKK in Jurkat T cells and SW620 colon cells, as well as the catalytic activity of purified IKK-alpha and [[ IKK-beta ]] in vitro.


The decrease in substrate phosphorylation by IKK-alpha and -beta is associated with a decrease in autophosphorylation of << IKKs >> and can be antagonized by excess [[ adenosine triphosphate ]].


The suppression of << NF-kappaB >> activation by inhibition of the IKKs contributes to the well-known anti-inflammatory and immunosuppressive effects of [[ sulfasalazine ]].


The suppression of NF-kappaB activation by inhibition of the << IKKs >> contributes to the well-known anti-inflammatory and immunosuppressive effects of [[ sulfasalazine ]].


<< COX-2 >> produces [[ prostaglandins ]] that inhibit apoptosis and stimulate angiogenesis and invasiveness.


In contrast, aspirin-like nonselective NSAIDs such as sulindac and << indomethacin >> inhibit not only the enzymatic action of the highly inducible, proinflammatory [[ COX-2 ]] but the constitutively expressed, cytoprotective COX-1 as well.


In contrast, aspirin-like nonselective NSAIDs such as sulindac and << indomethacin >> inhibit not only the enzymatic action of the highly inducible, proinflammatory COX-2 but the constitutively expressed, cytoprotective [[ COX-1 ]] as well.


In contrast, << aspirin >>-like nonselective NSAIDs such as sulindac and indomethacin inhibit not only the enzymatic action of the highly inducible, proinflammatory [[ COX-2 ]] but the constitutively expressed, cytoprotective COX-1 as well.


In contrast, << aspirin >>-like nonselective NSAIDs such as sulindac and indomethacin inhibit not only the enzymatic action of the highly inducible, proinflammatory COX-2 but the constitutively expressed, cytoprotective [[ COX-1 ]] as well.


In contrast, aspirin-like nonselective NSAIDs such as << sulindac >> and indomethacin inhibit not only the enzymatic action of the highly inducible, proinflammatory [[ COX-2 ]] but the constitutively expressed, cytoprotective COX-1 as well.


In contrast, aspirin-like nonselective NSAIDs such as << sulindac >> and indomethacin inhibit not only the enzymatic action of the highly inducible, proinflammatory COX-2 but the constitutively expressed, cytoprotective [[ COX-1 ]] as well.


Selective COX-2 inhibitors, such as << meloxicam >>, celecoxib (SC-58635), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit [[ COX-2 ]] but not COX-1.


Selective << COX-2 >> inhibitors, such as [[ meloxicam ]], celecoxib (SC-58635), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit COX-2 but not COX-1.


Selective COX-2 inhibitors, such as meloxicam, << celecoxib >> (SC-58635), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit [[ COX-2 ]] but not COX-1.


Selective << COX-2 >> inhibitors, such as meloxicam, [[ celecoxib ]] (SC-58635), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit COX-2 but not COX-1.


Selective COX-2 inhibitors, such as meloxicam, celecoxib (<< SC-58635 >>), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit [[ COX-2 ]] but not COX-1.


Selective << COX-2 >> inhibitors, such as meloxicam, celecoxib ([[ SC-58635 ]]), and rofecoxib (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit COX-2 but not COX-1.


Selective COX-2 inhibitors, such as meloxicam, celecoxib (SC-58635), and << rofecoxib >> (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit [[ COX-2 ]] but not COX-1.


Selective << COX-2 >> inhibitors, such as meloxicam, celecoxib (SC-58635), and [[ rofecoxib ]] (MK-0966), are NSAIDs that have been modified chemically to preferentially inhibit COX-2 but not COX-1.


Selective COX-2 inhibitors, such as meloxicam, celecoxib (SC-58635), and rofecoxib (<< MK-0966 >>), are NSAIDs that have been modified chemically to preferentially inhibit [[ COX-2 ]] but not COX-1.


Selective << COX-2 >> inhibitors, such as meloxicam, celecoxib (SC-58635), and rofecoxib ([[ MK-0966 ]]), are NSAIDs that have been modified chemically to preferentially inhibit COX-2 but not COX-1.


For instance, << meloxicam >> inhibits the growth of cultured colon cancer cells (HCA-7 and Moser-S) that express [[ COX-2 ]] but has no effect on HCT-116 tumor cells that do not express COX-2.


This effect may due to induction of apoptosis through uncoupling of oxidative phosphorylation and down-regulation of << Bcl-2 >>, as has been demonstrated for some nonselective NSAIDs, for instance, [[ flurbiprofen ]].


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors [[ carbidopa ]] (alpha-methyl-dopahydrazine), alpha-monofluoromethyldopa (MFMD), and 3-hydroxybenzylhydrazine (NSD-1015) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors carbidopa ([[ alpha-methyl-dopahydrazine ]]), alpha-monofluoromethyldopa (MFMD), and 3-hydroxybenzylhydrazine (NSD-1015) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors carbidopa (alpha-methyl-dopahydrazine), [[ alpha-monofluoromethyldopa ]] (MFMD), and 3-hydroxybenzylhydrazine (NSD-1015) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors carbidopa (alpha-methyl-dopahydrazine), alpha-monofluoromethyldopa ([[ MFMD ]]), and 3-hydroxybenzylhydrazine (NSD-1015) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors carbidopa (alpha-methyl-dopahydrazine), alpha-monofluoromethyldopa (MFMD), and [[ 3-hydroxybenzylhydrazine ]] (NSD-1015) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


To assess the feasibility of targeting these high AAAD levels for chemotherapy, << AAAD >> inhibitors carbidopa (alpha-methyl-dopahydrazine), alpha-monofluoromethyldopa (MFMD), and 3-hydroxybenzylhydrazine ([[ NSD-1015 ]]) were incubated (72 h) with NCI-H727 human lung carcinoid cells.


<< Hexahydrochromeno[4,3-b]pyrrole >> derivatives as [[ acetylcholinesterase ]] inhibitors.


Since this compound retains good << AChE >> inhibitory activity and its [[ hexahydrochromeno[4,3-b]pyrrole ]] moiety is reminiscent of the hexahydropyrrolo[2,3-b]indole of physostigmine (3), we have designed and synthesized carbamates 4-6, and their biological evaluation has been assessed in vitro against human AChE and BChE.


Since this compound retains good << AChE >> inhibitory activity and its hexahydrochromeno[4,3-b]pyrrole moiety is reminiscent of the [[ hexahydropyrrolo[2,3-b]indole of physostigmine ]] (3), we have designed and synthesized carbamates 4-6, and their biological evaluation has been assessed in vitro against human AChE and BChE.


When the anti-corticosterone drug << aminoglutethimide >> (CYP11A1 inhibitor) was administered to B16F10 mice, corticosterone levels in splenic tissue or serum and [[ CYP11A1 ]] mRNA expression were decreased at 14 days after tumor inoculation.


When the anti-corticosterone drug << aminoglutethimide >> ([[ CYP11A1 ]] inhibitor) was administered to B16F10 mice, corticosterone levels in splenic tissue or serum and CYP11A1 mRNA expression were decreased at 14 days after tumor inoculation.


We report here that a human degradation-resistant GLP-2 analogue, h[Gly2]-GLP-2 significantly improves survival, reduces bacteremia, attenuates epithelial injury, and inhibits crypt apoptosis in the murine gastrointestinal tract after administration of << topoisomerase I >> inhibitor [[ irinotecan hydrochloride ]] or the antimetabolite 5-fluorouracil.


Furthermore, h[<< Gly2 >>]-GLP-2 reduced chemotherapy-induced apoptosis, decreased activation of caspase-8 and -3, and inhibited [[ poly(ADP-ribose) polymerase ]] cleavage in heterologous cells transfected with the GLP-2 receptor.


OBJECTIVES: The hypothesis of the present study was that differences among << dopamine transporter >> (DAT) ligands in potency and effectiveness as a positive reinforcers were related to potency and effectiveness as [[ DA ]] uptake inhibitors.


OBJECTIVES: The hypothesis of the present study was that differences among dopamine transporter (<< DAT >>) ligands in potency and effectiveness as a positive reinforcers were related to potency and effectiveness as [[ DA ]] uptake inhibitors.


Accordingly, self-administration of a group of local anesthetics that are << DAT >> ligands was compared to their effects as [[ DA ]] uptake blockers in vitro in brain tissue.


Contribution of the << Na+-K+-2Cl- cotransporter >> NKCC1 to [[ Cl- ]] secretion in rat OMCD.


Contribution of the Na+-K+-2Cl- cotransporter << NKCC1 >> to [[ Cl- ]] secretion in rat OMCD.


The purpose of this study was to determine whether rat outer medullary collecting duct (OMCD) secretes Cl- and whether transepithelial Cl- transport occurs, in part, through << Cl- >> uptake across the basolateral membrane mediated by [[ NKCC1 ]] in series with Cl- efflux across the apical membrane.


The purpose of this study was to determine whether rat outer medullary collecting duct (OMCD) secretes Cl- and whether transepithelial Cl- transport occurs, in part, through Cl- uptake across the basolateral membrane mediated by << NKCC1 >> in series with [[ Cl- ]] efflux across the apical membrane.


Bumetanide-sensitive Cl- secretion was dependent on extracellular Na+ and either K+ or NH, consistent with the ion dependency of << NKCC1 >>-mediated [[ Cl- ]] transport.


In conclusion, OMCD tubules from deoxycorticosterone pivalate-treated rats secrete << Cl- >> into the luminal fluid through [[ NKCC1 ]]-mediated Cl- uptake across the basolateral membrane in series with Cl- efflux across the apical membrane.


In conclusion, OMCD tubules from deoxycorticosterone pivalate-treated rats secrete Cl- into the luminal fluid through << NKCC1 >>-mediated [[ Cl- ]] uptake across the basolateral membrane in series with Cl- efflux across the apical membrane.


In conclusion, OMCD tubules from deoxycorticosterone pivalate-treated rats secrete Cl- into the luminal fluid through << NKCC1 >>-mediated Cl- uptake across the basolateral membrane in series with [[ Cl- ]] efflux across the apical membrane.


The physiological role of << NKCC1 >>-mediated [[ Cl- ]] uptake remains to be determined.


The broad-spectrum anti-emetic activity of << AS-8112 >>, a novel dopamine D2, D3 and [[ 5-HT3 receptors ]] antagonist.


In guinea-pig isolated colon, AS-8112 produced a rightward shift of the concentration-response curves of << 2-methyl-5HT >>, a [[ 5-HT3 receptor ]] agonist (pA2 value of 7.04).


In guinea-pig isolated colon, << AS-8112 >> produced a rightward shift of the concentration-response curves of 2-methyl-5HT, a [[ 5-HT3 receptor ]] agonist (pA2 value of 7.04).


Other << 5-HT3 receptor >> antagonists also produced such a shift in the following antagonistic-potency order: [[ granisetron ]]> ondansetron=AS-8112>>metoclopramide.


Other << 5-HT3 receptor >> antagonists also produced such a shift in the following antagonistic-potency order: granisetron> [[ ondansetron ]]=AS-8112>>metoclopramide.


Other << 5-HT3 receptor >> antagonists also produced such a shift in the following antagonistic-potency order: granisetron> ondansetron=[[ AS-8112 ]]>>metoclopramide.


Other << 5-HT3 receptor >> antagonists also produced such a shift in the following antagonistic-potency order: granisetron> ondansetron=AS-8112>>[[ metoclopramide ]].


In mice, << AS-8112 >> (1.0 - 3.0 mg kg(-1) s.c.) potently inhibited hypothermia induced by the [[ dopamine D3 receptor ]] agonist; R(+)-7-OH-DPAT (R(+)-7-hydroxy-2-(N,N-di-n-propylamino)tetraline) (0.3 mg kg(-1) s.c.).


In mice, AS-8112 (1.0 - 3.0 mg kg(-1) s.c.) potently inhibited hypothermia induced by the << dopamine D3 receptor >> agonist; [[ R(+)-7-OH-DPAT ]] (R(+)-7-hydroxy-2-(N,N-di-n-propylamino)tetraline) (0.3 mg kg(-1) s.c.).


In mice, AS-8112 (1.0 - 3.0 mg kg(-1) s.c.) potently inhibited hypothermia induced by the << dopamine D3 receptor >> agonist; R(+)-7-OH-DPAT ([[ R(+)-7-hydroxy-2-(N,N-di-n-propylamino)tetraline ]]) (0.3 mg kg(-1) s.c.).


In conclusion, << AS-8112 >> is a potent dopamine D2, D3 and [[ 5-HT3 receptors ]] antagonist, and a novel anti-emetic agent with a broad-spectrum of anti-emetic activity.


<< Rofecoxib >> is a selective [[ cyclo-oxygenase (COX)-2 ]] inhibitor which has little or no effect on the COX-1 isoenzyme at doses up to 1000 mg/day.


<< Rofecoxib >> has greater selectivity for [[ COX-2 ]] than celecoxib, meloxicam, diclofenac and indomethacin.


<< Fenofibrate >> and GW2331 induced expression of [[ acyl-coenzyme A (CoA) oxidase ]] and enoyl-CoA hydratase and reduced apolipoprotein C-III and phosphoenolpyruvate carboxykinase mRNAs.


<< Fenofibrate >> and GW2331 induced expression of acyl-coenzyme A (CoA) oxidase and [[ enoyl-CoA hydratase ]] and reduced apolipoprotein C-III and phosphoenolpyruvate carboxykinase mRNAs.


Fenofibrate and << GW2331 >> induced expression of [[ acyl-coenzyme A (CoA) oxidase ]] and enoyl-CoA hydratase and reduced apolipoprotein C-III and phosphoenolpyruvate carboxykinase mRNAs.


Fenofibrate and << GW2331 >> induced expression of acyl-coenzyme A (CoA) oxidase and [[ enoyl-CoA hydratase ]] and reduced apolipoprotein C-III and phosphoenolpyruvate carboxykinase mRNAs.


<< Fenofibrate >> and GW2331 induced expression of acyl-coenzyme A (CoA) oxidase and enoyl-CoA hydratase and reduced [[ apolipoprotein C-III ]] and phosphoenolpyruvate carboxykinase mRNAs.


<< Fenofibrate >> and GW2331 induced expression of acyl-coenzyme A (CoA) oxidase and enoyl-CoA hydratase and reduced apolipoprotein C-III and [[ phosphoenolpyruvate carboxykinase ]] mRNAs.


Fenofibrate and << GW2331 >> induced expression of acyl-coenzyme A (CoA) oxidase and enoyl-CoA hydratase and reduced [[ apolipoprotein C-III ]] and phosphoenolpyruvate carboxykinase mRNAs.


Fenofibrate and << GW2331 >> induced expression of acyl-coenzyme A (CoA) oxidase and enoyl-CoA hydratase and reduced apolipoprotein C-III and [[ phosphoenolpyruvate carboxykinase ]] mRNAs.


<< Rosiglitazone >> modestly increased apolipoprotein C-III mRNA and had no effect on expression of the other 2 genes in the liver but increased the expression of [[ glucose transporter 4 ]] and phosphoenolpyruvate carboxykinase in adipose tissue.


<< Rosiglitazone >> modestly increased apolipoprotein C-III mRNA and had no effect on expression of the other 2 genes in the liver but increased the expression of glucose transporter 4 and [[ phosphoenolpyruvate carboxykinase ]] in adipose tissue.


<< Rosiglitazone >> modestly increased [[ apolipoprotein C-III ]] mRNA and had no effect on expression of the other 2 genes in the liver but increased the expression of glucose transporter 4 and phosphoenolpyruvate carboxykinase in adipose tissue.


<< Long-chain alkanols >> are general anesthetics which can also act as uncharged noncompetitive inhibitors of the peripheral [[ nicotinic acetylcholine receptor ]] (AChR) by binding to one or more specific sites on the AChR.


<< Cembranoids >> are naturally occurring, uncharged noncompetitive inhibitors of peripheral and neuronal [[ AChRs ]], which have no demonstrable general anesthetic activity in vivo.


<< Sulfasalazine >>, a potent suppressor of lymphoma growth by inhibition of the [[ x(c)- cystine transporter ]]: a new action for an old drug.


<< Sulfasalazine >> was fortuitously found to be a novel, potent inhibitor of the [[ x(c)- transporter ]].


It showed high rat lymphoma growth-inhibitory and lytic activity in vitro (IC50 = 0.16 mM), based specifically on inhibition of << x(c) >>--mediated cystine uptake, in contrast to its colonic metabolites, [[ sulfapyridine ]] and 5-aminosalicylic acid.


It showed high rat lymphoma growth-inhibitory and lytic activity in vitro (IC50 = 0.16 mM), based specifically on inhibition of << x(c) >>--mediated cystine uptake, in contrast to its colonic metabolites, sulfapyridine and [[ 5-aminosalicylic acid ]].


It showed high rat lymphoma growth-inhibitory and lytic activity in vitro (IC50 = 0.16 mM), based specifically on inhibition of << x(c) >>--mediated [[ cystine ]] uptake, in contrast to its colonic metabolites, sulfapyridine and 5-aminosalicylic acid.


The << x(c)- cystine transporter >> represents a novel target for sulfasalazine-like drugs with high potential for application in therapy of lymphoblastic and other malignancies dependent on extracellular [[ cyst(e)ine ]].


Advances in antihypertensive combination therapy: benefits of low-dose thiazide diuretics in conjunction with << omapatrilat >>, a [[ vasopeptidase ]] inhibitor.


<< Omapatrilat >>, the prototypical [[ vasopeptidase ]] inhibitor, inhibits not only ACE but also neutral endopeptidase.


<< Omapatrilat >>, the prototypical vasopeptidase inhibitor, inhibits not only [[ ACE ]] but also neutral endopeptidase.


<< Omapatrilat >>, the prototypical vasopeptidase inhibitor, inhibits not only ACE but also [[ neutral endopeptidase ]].


Like conventional ACE inhibitors, << omapatrilat >> causes extracellular volume reduction and vasodilatation; moreover, it increases levels of [[ atrial and brain natriuretic peptides ]] and bradykinin.


Like conventional ACE inhibitors, << omapatrilat >> causes extracellular volume reduction and vasodilatation; moreover, it increases levels of atrial and brain natriuretic peptides and [[ bradykinin ]].


Like conventional << ACE >> inhibitors, [[ omapatrilat ]] causes extracellular volume reduction and vasodilatation; moreover, it increases levels of atrial and brain natriuretic peptides and bradykinin.


The transport amiloride-sensitive mechanism, that decreased the acidic intracellular pH change occurring in this medium, would correspond to << Na+ >>-H+ exchange ([[ NHE1 ]] isoform).


The transport amiloride-sensitive mechanism, that decreased the acidic intracellular pH change occurring in this medium, would correspond to Na+-<< H+ >> exchange ([[ NHE1 ]] isoform).


<< Aspirin >> and salicylate bind to immunoglobulin heavy chain binding protein (BiP) and inhibit its [[ ATPase ]] activity in human fibroblasts.


Aspirin and << salicylate >> bind to immunoglobulin heavy chain binding protein (BiP) and inhibit its [[ ATPase ]] activity in human fibroblasts.


<< Salicylates >> inhibited [[ ATPase ]] activity stimulated by this specific heptapeptide but did not block ATP binding or induce BiP expression.


The specific activity of only << ornithine aminotransferase >> (OAT), the rate-limiting enzyme in the conversion of ornithine to [[ proline ]], increased in 2 weeks of hypertrophy.


The specific activity of only ornithine aminotransferase (<< OAT >>), the rate-limiting enzyme in the conversion of ornithine to [[ proline ]], increased in 2 weeks of hypertrophy.


The specific activity of only << ornithine aminotransferase >> (OAT), the rate-limiting enzyme in the conversion of [[ ornithine ]] to proline, increased in 2 weeks of hypertrophy.


The specific activity of only ornithine aminotransferase (<< OAT >>), the rate-limiting enzyme in the conversion of [[ ornithine ]] to proline, increased in 2 weeks of hypertrophy.


A series of studies is reviewed that assesses the relationship between cytokines released at the site of tissue injury and NSAID analgesia, and the in vivo selectivity of a selective << cyclooxygenase (COX)-2 >> inhibitor ([[ celecoxib ]]) in comparison to a dual COX-1/COX-2 inhibitor (ketorolac).


A series of studies is reviewed that assesses the relationship between cytokines released at the site of tissue injury and NSAID analgesia, and the in vivo selectivity of a selective cyclooxygenase (COX)-2 inhibitor (celecoxib) in comparison to a dual << COX-1 >>/COX-2 inhibitor ([[ ketorolac ]]).


A series of studies is reviewed that assesses the relationship between cytokines released at the site of tissue injury and NSAID analgesia, and the in vivo selectivity of a selective cyclooxygenase (COX)-2 inhibitor (celecoxib) in comparison to a dual COX-1/<< COX-2 >> inhibitor ([[ ketorolac ]]).


Three replicate studies in the oral surgery model of acute pain used submucosal microdialysis sample collection for the measurement of << prostaglandin E2 >> (PGE2; a product of both [[ COX-1 ]] and COX-2) and thromboxane B2 (as a biomarker for COX-1 activity) with parallel assessments of pain.


Three replicate studies in the oral surgery model of acute pain used submucosal microdialysis sample collection for the measurement of << prostaglandin E2 >> (PGE2; a product of both COX-1 and [[ COX-2 ]]) and thromboxane B2 (as a biomarker for COX-1 activity) with parallel assessments of pain.


Three replicate studies in the oral surgery model of acute pain used submucosal microdialysis sample collection for the measurement of prostaglandin E2 (<< PGE2 >>; a product of both [[ COX-1 ]] and COX-2) and thromboxane B2 (as a biomarker for COX-1 activity) with parallel assessments of pain.


Three replicate studies in the oral surgery model of acute pain used submucosal microdialysis sample collection for the measurement of prostaglandin E2 (<< PGE2 >>; a product of both COX-1 and [[ COX-2 ]]) and thromboxane B2 (as a biomarker for COX-1 activity) with parallel assessments of pain.


The time course of << PGE2 >> production was consistent with early release due to [[ COX-1 ]] activity followed by increased production 2-3 hours after surgery, consistent with COX-2 expression.


The time course of << PGE2 >> production was consistent with early release due to COX-1 activity followed by increased production 2-3 hours after surgery, consistent with [[ COX-2 ]] expression.


<< Celecoxib >> selectively suppressed PGE2 but not TxB2 at time points consistent with [[ COX-2 ]] activity, while producing analgesia.


Celecoxib selectively suppressed << PGE2 >> but not TxB2 at time points consistent with [[ COX-2 ]] activity, while producing analgesia.


These studies demonstrate the ability to assess the time course and selective effects of COX-2 inhibitors in vivo and suggest that suppression of << COX-2 >> mediated [[ PGE2 ]] is temporally related to NSAID analgesia.


Acute and chronic << PLZ >> administration increase brain GABA levels, an effect due, at least in part, to an inhibition of the activity of the GABA metabolizing enzyme, [[ GABA transaminase ]] (GABA-T).


Acute and chronic << PLZ >> administration increase brain GABA levels, an effect due, at least in part, to an inhibition of the activity of the GABA metabolizing enzyme, GABA transaminase ([[ GABA-T ]]).


Acute and chronic PLZ administration increase brain GABA levels, an effect due, at least in part, to an inhibition of the activity of the << GABA >> metabolizing enzyme, [[ GABA transaminase ]] (GABA-T).


Acute and chronic PLZ administration increase brain GABA levels, an effect due, at least in part, to an inhibition of the activity of the << GABA >> metabolizing enzyme, GABA transaminase ([[ GABA-T ]]).


As with GABA, the metabolism of << alanine >> involves a [[ pyridoxal phosphate-dependent transaminase ]].


In the study reported here, the effects of acute PLZ treatment on the levels of various << amino acids >>, some of which are also metabolized by [[ pyridoxal phosphate-dependent transaminases ]] were compared in rat whole brain.


The elevation in brain alanine levels could be explained, at least in part, by a time- and dose-dependent inhibitory effect of << PLZ >> on [[ alanine transaminase ]] (ALA-T), although as with GABA the increases are higher than expected from the degree of enzyme inhibition produced.


The elevation in brain alanine levels could be explained, at least in part, by a time- and dose-dependent inhibitory effect of << PLZ >> on alanine transaminase ([[ ALA-T ]]), although as with GABA the increases are higher than expected from the degree of enzyme inhibition produced.


The elevation in brain << alanine >> levels could be explained, at least in part, by a time- and dose-dependent inhibitory effect of PLZ on [[ alanine transaminase ]] (ALA-T), although as with GABA the increases are higher than expected from the degree of enzyme inhibition produced.


The elevation in brain << alanine >> levels could be explained, at least in part, by a time- and dose-dependent inhibitory effect of PLZ on alanine transaminase ([[ ALA-T ]]), although as with GABA the increases are higher than expected from the degree of enzyme inhibition produced.


In addition, we also showed that the elevation in alanine levels and the inhibition of << alanine transaminase >> in the brain are retained after 14 days of [[ PLZ ]] treatment, and that PLZ produces a marked increase in extracellular levels of alanine.


In addition, we also showed that the elevation in << alanine >> levels and the inhibition of [[ alanine transaminase ]] in the brain are retained after 14 days of PLZ treatment, and that PLZ produces a marked increase in extracellular levels of alanine.


<< Cyclooxygenase-1 >> (COX-1) inhibitors ([[ flurbiprofen ]], ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (<< COX-1 >>) inhibitors ([[ flurbiprofen ]], ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


<< Cyclooxygenase-1 >> (COX-1) inhibitors (flurbiprofen, [[ ketoprofen ]] and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (<< COX-1 >>) inhibitors (flurbiprofen, [[ ketoprofen ]] and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


<< Cyclooxygenase-1 >> (COX-1) inhibitors (flurbiprofen, ketoprofen and [[ ketrolack ]]) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (<< COX-1 >>) inhibitors (flurbiprofen, ketoprofen and [[ ketrolack ]]) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (COX-2) inhibitors at high concentrations (nimesulide and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (COX-1) inhibitors (flurbiprofen, ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and << cyclooxygenase-2 >> (COX-2) inhibitors at high concentrations ([[ nimesulide ]] and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (COX-1) inhibitors (flurbiprofen, ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (<< COX-2 >>) inhibitors at high concentrations ([[ nimesulide ]] and NS-389) slightly attenuated the contraction.


Cyclooxygenase-1 (COX-1) inhibitors (flurbiprofen, ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and << cyclooxygenase-2 >> (COX-2) inhibitors at high concentrations (nimesulide and [[ NS-389 ]]) slightly attenuated the contraction.


Cyclooxygenase-1 (COX-1) inhibitors (flurbiprofen, ketoprofen and ketrolack) attenuated the nicotine-induced contraction in a concentration-dependent manner, and cyclooxygenase-2 (<< COX-2 >>) inhibitors at high concentrations (nimesulide and [[ NS-389 ]]) slightly attenuated the contraction.


A << TXA2 synthetase >> inhibitor ([[ OKY-046 ]]) attenuated the contraction to a small extent only at high concentrations.


A << TXA2 receptor >> antagonist ([[ S-1452 ]]) attenuated the contraction in a concentration-dependent manner.


A << nicotinic receptor >> antagonist ([[ hexamethonium ]]) attenuated the contraction in part and an alpha-adrenoceptor antagonist (prazosin) nearly abolished the contraction.


A nicotinic receptor antagonist (hexamethonium) attenuated the contraction in part and an << alpha-adrenoceptor >> antagonist ([[ prazosin ]]) nearly abolished the contraction.


Non-<< steroidal >> anti-inflammatory drugs (NSAIDs) are competitive inhibitors of [[ cyclooxygenase ]] (COX), the enzyme that mediates biosynthesis of prostaglandins and thromboxanes from arachidonic acid.


Non-<< steroidal >> anti-inflammatory drugs (NSAIDs) are competitive inhibitors of cyclooxygenase ([[ COX ]]), the enzyme that mediates biosynthesis of prostaglandins and thromboxanes from arachidonic acid.


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of << cyclooxygenase >> (COX), the enzyme that mediates biosynthesis of [[ prostaglandins ]] and thromboxanes from arachidonic acid.


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of cyclooxygenase (<< COX >>), the enzyme that mediates biosynthesis of [[ prostaglandins ]] and thromboxanes from arachidonic acid.


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of << cyclooxygenase >> (COX), the enzyme that mediates biosynthesis of prostaglandins and [[ thromboxanes ]] from arachidonic acid.


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of cyclooxygenase (<< COX >>), the enzyme that mediates biosynthesis of prostaglandins and [[ thromboxanes ]] from arachidonic acid.


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of << cyclooxygenase >> (COX), the enzyme that mediates biosynthesis of prostaglandins and thromboxanes from [[ arachidonic acid ]].


Non-steroidal anti-inflammatory drugs (NSAIDs) are competitive inhibitors of cyclooxygenase (<< COX >>), the enzyme that mediates biosynthesis of prostaglandins and thromboxanes from [[ arachidonic acid ]].


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, suprofen, carprofen, [[ zomepirac ]], indomethacin, diclofenac and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, suprofen, carprofen, zomepirac, [[ indomethacin ]], diclofenac and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, suprofen, carprofen, zomepirac, indomethacin, [[ diclofenac ]] and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, suprofen, carprofen, zomepirac, indomethacin, diclofenac and [[ meclofenamic acid ]] were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: [[ rofecoxib ]], ketoprofen, suprofen, carprofen, zomepirac, indomethacin, diclofenac and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, [[ ketoprofen ]], suprofen, carprofen, zomepirac, indomethacin, diclofenac and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, [[ suprofen ]], carprofen, zomepirac, indomethacin, diclofenac and meclofenamic acid were undertaken using the AMBER program.


Accordingly, docking of different << COX >> inhibitors, including selective and non-selective ligands: rofecoxib, ketoprofen, suprofen, [[ carprofen ]], zomepirac, indomethacin, diclofenac and meclofenamic acid were undertaken using the AMBER program.


Olopatadine hydrochloride (<< olopatadine >>, 11-[(Z)-3-(dimethylamino)propylidene]-6,11-dihydrodibenz[b,e]oxepin-2-acetic acid monohydrochloride) is a novel antiallergic/[[ histamine H1-receptor ]] antagonistic drug that was synthesized and evaluated in our laboratories.


Olopatadine hydrochloride (olopatadine, << 11-[(Z)-3-(dimethylamino)propylidene]-6,11-dihydrodibenz[b,e]oxepin-2-acetic acid monohydrochloride >>) is a novel antiallergic/[[ histamine H1-receptor ]] antagonistic drug that was synthesized and evaluated in our laboratories.


<< Olopatadine hydrochloride >> (olopatadine, 11-[(Z)-3-(dimethylamino)propylidene]-6,11-dihydrodibenz[b,e]oxepin-2-acetic acid monohydrochloride) is a novel antiallergic/[[ histamine H1-receptor ]] antagonistic drug that was synthesized and evaluated in our laboratories.


<< Olopatadine >> is a selective [[ histamine H1-receptor ]] antagonist possessing inhibitory effects on the release of inflammatory lipid mediators such as leukotriene and thromboxane from human polymorphonuclear leukocytes and eosinophils.


A molecular mechanism of action of << theophylline >>: Induction of [[ histone deacetylase ]] activity to decrease inflammatory gene expression.


We show both in vitro and in vivo that low-dose << theophylline >> enhances [[ HDAC ]] activity in epithelial cells and macrophages.


Thus we have shown that low-dose << theophylline >> exerts an anti-asthma effect through increasing activation of [[ HDAC ]] which is subsequently recruited by corticosteroids to suppress inflammatory genes.


In rats, << rifamycin SV >> and rifampicin were shown to interfere with hepatic organic anion uptake by inhibition of the [[ organic anion transporting polypeptides ]] Oatp1 and Oatp2.


In rats, << rifamycin SV >> and rifampicin were shown to interfere with hepatic organic anion uptake by inhibition of the organic anion transporting polypeptides [[ Oatp1 ]] and Oatp2.


In rats, << rifamycin SV >> and rifampicin were shown to interfere with hepatic organic anion uptake by inhibition of the organic anion transporting polypeptides Oatp1 and [[ Oatp2 ]].


In rats, rifamycin SV and << rifampicin >> were shown to interfere with hepatic organic anion uptake by inhibition of the [[ organic anion transporting polypeptides ]] Oatp1 and Oatp2.


In rats, rifamycin SV and << rifampicin >> were shown to interfere with hepatic organic anion uptake by inhibition of the organic anion transporting polypeptides [[ Oatp1 ]] and Oatp2.


In rats, rifamycin SV and << rifampicin >> were shown to interfere with hepatic organic anion uptake by inhibition of the organic anion transporting polypeptides Oatp1 and [[ Oatp2 ]].


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited [[ human organic anion transporting polypeptide C ]] (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C ([[ SLC21A6 ]]) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) ([[ OATP-C ]]), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), [[ human organic anion transporting polypeptide 8 ]] (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 ([[ SLC21A8 ]]) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) ([[ OATP8 ]]), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), [[ human organic anion transporting polypeptide B ]] (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B ([[ SLC21A9 ]]) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) ([[ OATP-B ]]), and human organic anion transporting polypeptide A (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and [[ human organic anion transporting polypeptide A ]] (SLC21A3) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A ([[ SLC21A3 ]]) (OATP-A) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


In complementary RNA (cRNA)-injected Xenopus laevis oocytes, << rifamycin SV >> (10 micromol/L) cis-inhibited human organic anion transporting polypeptide C (SLC21A6) (OATP-C), human organic anion transporting polypeptide 8 (SLC21A8) (OATP8), human organic anion transporting polypeptide B (SLC21A9) (OATP-B), and human organic anion transporting polypeptide A (SLC21A3) ([[ OATP-A ]]) mediated BSP uptake by 69%, 79%, 89%, and 57%, respectively, as compared with uptake into control oocytes.


<< Rifampicin >> (10 micromol/L) inhibited [[ OATP8 ]]-mediated BSP uptake by 50%, whereas inhibition of OATP-C-, OATP-B-, and OATP-A-mediated BSP transport was below 15%.


<< Rifampicin >> (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of [[ OATP-C ]]-, OATP-B-, and OATP-A-mediated BSP transport was below 15%.


<< Rifampicin >> (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of OATP-C-, [[ OATP-B ]]-, and OATP-A-mediated BSP transport was below 15%.


<< Rifampicin >> (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of OATP-C-, OATP-B-, and [[ OATP-A ]]-mediated BSP transport was below 15%.


Rifampicin (10 micromol/L) inhibited << OATP8 >>-mediated [[ BSP ]] uptake by 50%, whereas inhibition of OATP-C-, OATP-B-, and OATP-A-mediated BSP transport was below 15%.


Rifampicin (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of << OATP-C >>-, OATP-B-, and OATP-A-mediated [[ BSP ]] transport was below 15%.


Rifampicin (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of OATP-C-, << OATP-B >>-, and OATP-A-mediated [[ BSP ]] transport was below 15%.


Rifampicin (10 micromol/L) inhibited OATP8-mediated BSP uptake by 50%, whereas inhibition of OATP-C-, OATP-B-, and << OATP-A >>-mediated [[ BSP ]] transport was below 15%.


100 micromol/L << rifampicin >> inhibited [[ OATP-C ]]- and OATP8-, OATP-B- and OATP-A-mediated BSP uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L << rifampicin >> inhibited OATP-C- and [[ OATP8 ]]-, OATP-B- and OATP-A-mediated BSP uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L << rifampicin >> inhibited OATP-C- and OATP8-, [[ OATP-B ]]- and OATP-A-mediated BSP uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L << rifampicin >> inhibited OATP-C- and OATP8-, OATP-B- and [[ OATP-A ]]-mediated BSP uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L rifampicin inhibited << OATP-C >>- and OATP8-, OATP-B- and OATP-A-mediated [[ BSP ]] uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L rifampicin inhibited OATP-C- and << OATP8 >>-, OATP-B- and OATP-A-mediated [[ BSP ]] uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L rifampicin inhibited OATP-C- and OATP8-, << OATP-B >>- and OATP-A-mediated [[ BSP ]] uptake by 66%, 96%, 25%, and 49%, respectively.


100 micromol/L rifampicin inhibited OATP-C- and OATP8-, OATP-B- and << OATP-A >>-mediated [[ BSP ]] uptake by 66%, 96%, 25%, and 49%, respectively.


Direct transport of << rifampicin >> could be shown for [[ OATP-C ]] (apparent K(m) value 13 micromol/L) and OATP8 (2.3 micromol/L).


Direct transport of << rifampicin >> could be shown for OATP-C (apparent K(m) value 13 micromol/L) and [[ OATP8 ]] (2.3 micromol/L).


Inhibition of << human liver OATPs >> can explain the previously observed effects of [[ rifamycin SV ]] and rifampicin on hepatic organic anion elimination.


Inhibition of << human liver OATPs >> can explain the previously observed effects of rifamycin SV and [[ rifampicin ]] on hepatic organic anion elimination.


<< Metformin >> increases [[ AMP-activated protein kinase ]] activity in skeletal muscle of subjects with type 2 diabetes.


<< AMP-activated protein kinase >> (AMPK) activity increases in response to depletion of cellular energy stores, and this enzyme has been implicated in the stimulation of [[ glucose ]] uptake into skeletal muscle and the inhibition of liver gluconeogenesis.


AMP-activated protein kinase (<< AMPK >>) activity increases in response to depletion of cellular energy stores, and this enzyme has been implicated in the stimulation of [[ glucose ]] uptake into skeletal muscle and the inhibition of liver gluconeogenesis.


We recently reported that << AMPK >> is activated by [[ metformin ]] in cultured rat hepatocytes, mediating the inhibitory effects of the drug on hepatic glucose production.


In the present study, we evaluated whether therapeutic doses of << metformin >> increase [[ AMPK ]] activity in vivo in subjects with type 2 diabetes.


<< Metformin >> treatment for 10 weeks significantly increased [[ AMPK alpha2 ]] activity in the skeletal muscle, and this was associated with increased phosphorylation of AMPK on Thr172 and decreased acetyl-CoA carboxylase-2 activity.


<< Metformin >> treatment for 10 weeks significantly increased AMPK alpha2 activity in the skeletal muscle, and this was associated with increased phosphorylation of [[ AMPK ]] on Thr172 and decreased acetyl-CoA carboxylase-2 activity.


<< Metformin >> treatment for 10 weeks significantly increased AMPK alpha2 activity in the skeletal muscle, and this was associated with increased phosphorylation of AMPK on Thr172 and decreased [[ acetyl-CoA carboxylase-2 ]] activity.


The increase in << AMPK alpha2 >> activity was likely due to a change in muscle energy status because ATP and phosphocreatine concentrations were lower after [[ metformin ]] treatment.


<< Metformin >>-induced increases in [[ AMPK ]] activity were associated with higher rates of glucose disposal and muscle glycogen concentrations.


<< Thalidomide >> prevents alcoholic liver injury in rats through suppression of Kupffer cell sensitization and [[ TNF-alpha ]] production.


<< Thalidomide >> has been shown to suppress [[ TNF-alpha ]] production from macrophages.


Furthermore, << thalidomide >> abolished the LPS-induced increase in [[ CD14 ]] expression and [Ca2+]i elevation in KCs.


Moreover, << thalidomide >> reduced the LPS-induced [[ TNF-alpha ]] production by KCs by decreasing TNF-alpha messenger RNA.


Moreover, << thalidomide >> reduced the LPS-induced TNF-alpha production by KCs by decreasing [[ TNF-alpha ]] messenger RNA.


CONCLUSIONS: These results collectively indicate that << thalidomide >> prevents alcoholic liver injury through suppression of [[ TNF-alpha ]] production and abolishment of KC sensitization.


During polyamine catabolism, spermine and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase (SSAT) and subsequently oxidized by << polyamine oxidase >> (PAO) to produce [[ spermidine ]] and putrescine, respectively.


During polyamine catabolism, spermine and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase (SSAT) and subsequently oxidized by polyamine oxidase (<< PAO >>) to produce [[ spermidine ]] and putrescine, respectively.


During polyamine catabolism, spermine and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase (SSAT) and subsequently oxidized by << polyamine oxidase >> (PAO) to produce spermidine and [[ putrescine ]], respectively.


During polyamine catabolism, spermine and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase (SSAT) and subsequently oxidized by polyamine oxidase (<< PAO >>) to produce spermidine and [[ putrescine ]], respectively.


During polyamine catabolism, << spermine >> and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase ([[ SSAT ]]) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


During polyamine catabolism, << spermine >> and spermidine are first acetylated by [[ spermidine/spermine N(1)-acetyltransferase ]] (SSAT) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


During polyamine catabolism, spermine and << spermidine >> are first acetylated by spermidine/spermine N(1)-acetyltransferase ([[ SSAT ]]) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


During polyamine catabolism, spermine and << spermidine >> are first acetylated by [[ spermidine/spermine N(1)-acetyltransferase ]] (SSAT) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


During << polyamine >> catabolism, spermine and spermidine are first acetylated by spermidine/spermine N(1)-acetyltransferase ([[ SSAT ]]) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


During << polyamine >> catabolism, spermine and spermidine are first acetylated by [[ spermidine/spermine N(1)-acetyltransferase ]] (SSAT) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively.


In attempting to clone the PAO involved in this back-conversion pathway, we encountered an oxidase that preferentially cleaves << spermine >> in the absence of prior acetylation by [[ SSAT ]].


Substrate specificity using lysates of oxidase-transfected HEK-293 cells revealed that the newly identified << oxidase >> strongly favoured [[ spermine ]] over N (1)-acetylspermine and that it failed to act on N (1)-acetylspermidine, spermidine or the preferred PAO substrate, N (1), N (12)-diacetylspermine.


Substrate specificity using lysates of oxidase-transfected HEK-293 cells revealed that the newly identified << oxidase >> strongly favoured spermine over [[ N (1)-acetylspermine ]] and that it failed to act on N (1)-acetylspermidine, spermidine or the preferred PAO substrate, N (1), N (12)-diacetylspermine.


Substrate specificity using lysates of oxidase-transfected HEK-293 cells revealed that the newly identified oxidase strongly favoured spermine over N (1)-acetylspermine and that it failed to act on N (1)-acetylspermidine, spermidine or the preferred << PAO >> substrate, [[ N (1), N (12)-diacetylspermine ]].


The << PAO >> inhibitor, [[ MDL-72,527 ]], only partially blocked oxidation of spermine while a previously reported PAO substrate, N (1)-( n -octanesulphonyl)spermine, potently inhibited the reaction.


The PAO inhibitor, MDL-72,527, only partially blocked oxidation of spermine while a previously reported << PAO >> substrate, [[ N (1)-( n -octanesulphonyl)spermine ]], potently inhibited the reaction.


Although a significant platelet hyperreactivity was observed in the patients, the HPA-1 genotype did not influence basal or << ADP >>-induced [[ CD62P ]] expression.


In no other subject any activation of platelets by GP IIb/IIIa inhibitors was observed and there were no statistically significant differences between HPA-1 genotypes with respect to the effects of GP IIb/IIIa inhibitors on basal or << ADP >>-stimulated [[ CD62P ]] expression.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to [[ pyruvate ]], ammonia, and an alpha-chloroenethiolate (with DCVC) or an alpha-difluoroalkylthiolate (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to pyruvate, [[ ammonia ]], and an alpha-chloroenethiolate (with DCVC) or an alpha-difluoroalkylthiolate (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to pyruvate, ammonia, and an [[ alpha-chloroenethiolate ]] (with DCVC) or an alpha-difluoroalkylthiolate (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to pyruvate, ammonia, and an alpha-chloroenethiolate (with [[ DCVC ]]) or an alpha-difluoroalkylthiolate (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to pyruvate, ammonia, and an alpha-chloroenethiolate (with DCVC) or an [[ alpha-difluoroalkylthiolate ]] (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated cysteine S-conjugates are metabolized by cysteine S-conjugate << beta-lyases >> to pyruvate, ammonia, and an alpha-chloroenethiolate (with DCVC) or an alpha-difluoroalkylthiolate (with [[ TFEC ]]) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


Most halogenated << cysteine S-conjugates >> are metabolized by cysteine S-conjugate [[ beta-lyases ]] to pyruvate, ammonia, and an alpha-chloroenethiolate (with DCVC) or an alpha-difluoroalkylthiolate (with TFEC) that may eliminate halide to give a thioacyl halide, which reacts with epsilon-amino groups of lysine residues in proteins.


The juvenile visceral steatosis (jvs) mouse, having a mutation in the << carnitine >> transporter gene [[ Octn2 ]], is a model of primary systemic carnitine deficiency in humans (SCD, OMIM 212140).


Reuptake of extracellular << noradrenaline >> (NA) into superior cervical ganglion (SCG) neurones is mediated by means of the [[ noradrenaline transporter ]] (NAT, uptake 1).


Reuptake of extracellular << noradrenaline >> (NA) into superior cervical ganglion (SCG) neurones is mediated by means of the noradrenaline transporter ([[ NAT ]], uptake 1).


Reuptake of extracellular noradrenaline (<< NA >>) into superior cervical ganglion (SCG) neurones is mediated by means of the [[ noradrenaline transporter ]] (NAT, uptake 1).


Reuptake of extracellular noradrenaline (<< NA >>) into superior cervical ganglion (SCG) neurones is mediated by means of the noradrenaline transporter ([[ NAT ]], uptake 1).


The ensuing radioactive outflow from these cultures was enhanced by desipramine and reserpine, but reduced (in the presence of desipramine) by the << OCT3 >> inhibitors cyanine 863, [[ oestradiol ]] and corticosterone.


The ensuing radioactive outflow from these cultures was enhanced by desipramine and reserpine, but reduced (in the presence of desipramine) by the << OCT3 >> inhibitors cyanine 863, oestradiol and [[ corticosterone ]].


The outflow of << [3H]-MPP+ >> was significantly enhanced by MPP+, guanidine, choline and amantadine as potential substrates for [[ OCT ]]-related transmembrane transporters.


The outflow of << [3H]-MPP+ >> was significantly enhanced by MPP+, guanidine, choline and amantadine as potential substrates for OCT-related [[ transmembrane transporters ]].


The outflow of [3H]-MPP+ was significantly enhanced by << MPP+ >>, guanidine, choline and amantadine as potential substrates for [[ OCT ]]-related transmembrane transporters.


The outflow of [3H]-MPP+ was significantly enhanced by << MPP+ >>, guanidine, choline and amantadine as potential substrates for OCT-related [[ transmembrane transporters ]].


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, << guanidine >>, choline and amantadine as potential substrates for [[ OCT ]]-related transmembrane transporters.


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, << guanidine >>, choline and amantadine as potential substrates for OCT-related [[ transmembrane transporters ]].


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, guanidine, << choline >> and amantadine as potential substrates for [[ OCT ]]-related transmembrane transporters.


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, guanidine, << choline >> and amantadine as potential substrates for OCT-related [[ transmembrane transporters ]].


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, guanidine, choline and << amantadine >> as potential substrates for [[ OCT ]]-related transmembrane transporters.


The outflow of [3H]-MPP+ was significantly enhanced by MPP+, guanidine, choline and << amantadine >> as potential substrates for OCT-related [[ transmembrane transporters ]].