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The results showed that (1) 15mg/kg body weight PhIP induced obvious histopathological changes in gastric mucosa; (2) << PhIP >> (10 and/or 15mg/kg) significantly decreased superoxide dismutase (SOD) and glutathioneperoxidase (GPx) activities, while increased catalase ([[ CAT ]]) activity compared with the control.

The results showed that (1) 15mg/kg body weight PhIP induced obvious histopathological changes in gastric mucosa; (2) << PhIP >> (10 and/or 15mg/kg) significantly decreased [[ superoxide dismutase ]] (SOD) and glutathioneperoxidase (GPx) activities, while increased catalase (CAT) activity compared with the control.

The results showed that (1) 15mg/kg body weight PhIP induced obvious histopathological changes in gastric mucosa; (2) << PhIP >> (10 and/or 15mg/kg) significantly decreased superoxide dismutase ([[ SOD ]]) and glutathioneperoxidase (GPx) activities, while increased catalase (CAT) activity compared with the control.

The results showed that (1) 15mg/kg body weight PhIP induced obvious histopathological changes in gastric mucosa; (2) << PhIP >> (10 and/or 15mg/kg) significantly decreased superoxide dismutase (SOD) and [[ glutathioneperoxidase ]] (GPx) activities, while increased catalase (CAT) activity compared with the control.

The results showed that (1) 15mg/kg body weight PhIP induced obvious histopathological changes in gastric mucosa; (2) << PhIP >> (10 and/or 15mg/kg) significantly decreased superoxide dismutase (SOD) and glutathioneperoxidase ([[ GPx ]]) activities, while increased catalase (CAT) activity compared with the control.

With the elevated doses of PhIP, malondialdehyde (MDA) contents, protein carbonyl (PCO) contents and DNA-protein crosslinks (DPC) coefficients were significantly raised in a dose-dependent manner; (3) << PhIP >> at the doses of 10mg/kg and/or 15mg/kg significantly inhibited p16 mRNA and protein expression, whereas enhanced c-fos and [[ c-jun ]] expression relative to control.

With the elevated doses of PhIP, malondialdehyde (MDA) contents, protein carbonyl (PCO) contents and DNA-protein crosslinks (DPC) coefficients were significantly raised in a dose-dependent manner; (3) << PhIP >> at the doses of 10mg/kg and/or 15mg/kg significantly inhibited p16 mRNA and protein expression, whereas enhanced [[ c-fos ]] and c-jun expression relative to control.

With the elevated doses of PhIP, malondialdehyde (MDA) contents, protein carbonyl (PCO) contents and DNA-protein crosslinks (DPC) coefficients were significantly raised in a dose-dependent manner; (3) << PhIP >> at the doses of 10mg/kg and/or 15mg/kg significantly inhibited [[ p16 ]] mRNA and protein expression, whereas enhanced c-fos and c-jun expression relative to control.

The data indicated that << PhIP >> could cause stomach injury, oxidative stress in rat stomachs as well as the activation of [[ c-fos ]] and c-jun and inactivation of p16, which may play a role in the pathogenesis of PhIP-associated stomach cancer.

The data indicated that << PhIP >> could cause stomach injury, oxidative stress in rat stomachs as well as the activation of c-fos and [[ c-jun ]] and inactivation of p16, which may play a role in the pathogenesis of PhIP-associated stomach cancer.

The data indicated that << PhIP >> could cause stomach injury, oxidative stress in rat stomachs as well as the activation of c-fos and c-jun and inactivation of [[ p16 ]], which may play a role in the pathogenesis of PhIP-associated stomach cancer.

We also shortly discuss the ongoing debate on whether << NO >> is the actual reaction product of [[ NOS ]] catalysis, as well as the phenomenon of NO-mediated autoinhibition.

<< Prostacyclin >> analogues inhibit [[ tissue factor ]] expression in the human monocytic cell line THP-1 via a cyclic AMP-dependent mechanism.

The present studies were undertaken to determine whether stable analogues of << prostacyclin >>, a potent endothelium-derived platelet inhibitor and vasodilator, could inhibit [[ tissue factor ]] expression by human monocytic cells.

Preincubation for 30 minutes with << iloprost >>, ciprostene, and carbacyclin led to a dose-dependent inhibition of [[ tissue factor ]] expression induced by all three challenging agents.

Preincubation for 30 minutes with iloprost, << ciprostene >>, and carbacyclin led to a dose-dependent inhibition of [[ tissue factor ]] expression induced by all three challenging agents.

Preincubation for 30 minutes with iloprost, ciprostene, and << carbacyclin >> led to a dose-dependent inhibition of [[ tissue factor ]] expression induced by all three challenging agents.

This effect was potentiated by << isobutylmethylxanthine >>, an inhibitor of [[ phosphodiesterase ]].

The inhibitory effects of iloprost on << tissue factor >> expression were also potentiated by [[ isobutylmethylxanthine ]] and mimicked by forskolin and dibutyryl cyclic AMP but not dibutyryl cyclic GMP.

The inhibitory effects of iloprost on << tissue factor >> expression were also potentiated by isobutylmethylxanthine and mimicked by [[ forskolin ]] and dibutyryl cyclic AMP but not dibutyryl cyclic GMP.

The inhibitory effects of iloprost on << tissue factor >> expression were also potentiated by isobutylmethylxanthine and mimicked by forskolin and d[[ ibutyryl cyclic AMP ]] but not dibutyryl cyclic GMP.

These results suggest that prostacyclin may play a role in downregulating << tissue factor >> expression in monocytes, at least in part via elevation of intracellular levels of [[ cyclic AMP ]].

These results suggest that << prostacyclin >> may play a role in downregulating [[ tissue factor ]] expression in monocytes, at least in part via elevation of intracellular levels of cyclic AMP.

PURPOSE: The fluoropyrimidine carbamate (capecitabine) is converted to << 5-fluorouracil >> (5-FU) by thymidine phosphorylase ([[ TP ]]) inside target tissues.

PURPOSE: The fluoropyrimidine carbamate (capecitabine) is converted to << 5-fluorouracil >> (5-FU) by [[ thymidine phosphorylase ]] (TP) inside target tissues.

PURPOSE: The fluoropyrimidine carbamate (capecitabine) is converted to 5-fluorouracil (<< 5-FU >>) by thymidine phosphorylase ([[ TP ]]) inside target tissues.

PURPOSE: The fluoropyrimidine carbamate (capecitabine) is converted to 5-fluorouracil (<< 5-FU >>) by [[ thymidine phosphorylase ]] (TP) inside target tissues.

PURPOSE: The << fluoropyrimidine carbamate >> (capecitabine) is converted to 5-fluorouracil (5-FU) by thymidine phosphorylase ([[ TP ]]) inside target tissues.

PURPOSE: The << fluoropyrimidine carbamate >> (capecitabine) is converted to 5-fluorouracil (5-FU) by [[ thymidine phosphorylase ]] (TP) inside target tissues.

PURPOSE: The fluoropyrimidine carbamate (<< capecitabine >>) is converted to 5-fluorouracil (5-FU) by thymidine phosphorylase ([[ TP ]]) inside target tissues.

PURPOSE: The fluoropyrimidine carbamate (<< capecitabine >>) is converted to 5-fluorouracil (5-FU) by [[ thymidine phosphorylase ]] (TP) inside target tissues.

<< 5-FU >> interferes with DNA synthesis by blocking [[ thymidylate synthase ]] (TS) but is inactivated by dihydropyrimidine dehydrogenase (DPD).

<< 5-FU >> interferes with DNA synthesis by blocking thymidylate synthase ([[ TS ]]) but is inactivated by dihydropyrimidine dehydrogenase (DPD).

Favorable enzyme profiles (high << TP >> and low DPD) generate high intratumor levels of [[ 5-FU ]] that are effective against many tumors, especially those with low TS.

Favorable enzyme profiles (high TP and low << DPD >>) generate high intratumor levels of [[ 5-FU ]] that are effective against many tumors, especially those with low TS.

Previous studies by this research team proved that vasodilating << prostaglandins >> (PGs) E1, E2 and I2 inhibit [[ carbonic anhydrase ]] (CA) in vitro and in vivo, which suggested involvement of CA in gastric acid secretion inhibition and the increase of gastric mucosa blood flow produced by this group of PGs.

Previous studies by this research team proved that vasodilating << prostaglandins >> (PGs) E1, E2 and I2 inhibit carbonic anhydrase ([[ CA ]]) in vitro and in vivo, which suggested involvement of CA in gastric acid secretion inhibition and the increase of gastric mucosa blood flow produced by this group of PGs.

Previous studies by this research team proved that vasodilating prostaglandins (<< PGs >>) E1, E2 and I2 inhibit [[ carbonic anhydrase ]] (CA) in vitro and in vivo, which suggested involvement of CA in gastric acid secretion inhibition and the increase of gastric mucosa blood flow produced by this group of PGs.

Previous studies by this research team proved that vasodilating prostaglandins (<< PGs >>) E1, E2 and I2 inhibit carbonic anhydrase ([[ CA ]]) in vitro and in vivo, which suggested involvement of CA in gastric acid secretion inhibition and the increase of gastric mucosa blood flow produced by this group of PGs.

Histamine and << Ca >> added to NSAIDs amplified the activating effect of the latter on [[ CA II ]].

Association of PGE2 or << acetazolamide >> to NSAIDs reduced NSAID-induced activation of [[ CA I ]] and CA II.

Association of PGE2 or << acetazolamide >> to NSAIDs reduced NSAID-induced activation of CA I and [[ CA II ]].

<< Indomethacin >> abolished the inhibitory effect of acetazolamide on [[ CA I ]] and CA II.

<< Indomethacin >> abolished the inhibitory effect of acetazolamide on CA I and [[ CA II ]].

Indomethacin abolished the inhibitory effect of << acetazolamide >> on [[ CA I ]] and CA II.

Indomethacin abolished the inhibitory effect of << acetazolamide >> on CA I and [[ CA II ]].

<< COX-1 >> inhibition was measured as percentage inhibition of serum [[ TXB2 ]] generation in clotting whole blood, and as closure time with use of the platelet function analyser PFA-100.

CONCLUSIONS: In the maximum registered dosage, << nabumetone >> inhibits thromboxane production much more than meloxicam, signifying less [[ COX-2 ]] selectivity of the former.

Treatment with << diclofenac >> resulted in nuclear condensation (a morphological change due to apoptosis of NSCs) 24hr after the treatment and activated [[ caspase-3 ]] after 6 hr, indicating that diclofenac may cause apoptosis of neuronal cells via activation of the caspase cascade.

Treatment with diclofenac resulted in nuclear condensation (a morphological change due to apoptosis of NSCs) 24hr after the treatment and activated caspase-3 after 6 hr, indicating that << diclofenac >> may cause apoptosis of neuronal cells via activation of the [[ caspase ]] cascade.

Correlation between activation of << PPARγ >> and resistin downregulation in a mouse adipocyte cell line by a series of [[ thiazolidinediones ]].

Correlation between activation of PPARγ and << resistin >> downregulation in a mouse adipocyte cell line by a series of [[ thiazolidinediones ]].

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported << NRF2 >> target genes in response to NRF2 inducers ([[ sulforaphane ]], tert-butylhydroquinone, cinnamic aldehyde, and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to << NRF2 >> inducers ([[ sulforaphane ]], tert-butylhydroquinone, cinnamic aldehyde, and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported << NRF2 >> target genes in response to NRF2 inducers (sulforaphane, [[ tert-butylhydroquinone ]], cinnamic aldehyde, and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to << NRF2 >> inducers (sulforaphane, [[ tert-butylhydroquinone ]], cinnamic aldehyde, and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported << NRF2 >> target genes in response to NRF2 inducers (sulforaphane, tert-butylhydroquinone, [[ cinnamic aldehyde ]], and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to << NRF2 >> inducers (sulforaphane, tert-butylhydroquinone, [[ cinnamic aldehyde ]], and hydrogen peroxide) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported << NRF2 >> target genes in response to NRF2 inducers (sulforaphane, tert-butylhydroquinone, cinnamic aldehyde, and [[ hydrogen peroxide ]]) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to << NRF2 >> inducers (sulforaphane, tert-butylhydroquinone, cinnamic aldehyde, and [[ hydrogen peroxide ]]) showed that the aldo-keto reductase (AKR) 1C1 is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to NRF2 inducers (<< sulforaphane >>, tert-butylhydroquinone, cinnamic aldehyde, and hydrogen peroxide) showed that the [[ aldo-keto reductase (AKR) 1C1 ]] is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to NRF2 inducers (sulforaphane, << tert-butylhydroquinone >>, cinnamic aldehyde, and hydrogen peroxide) showed that the [[ aldo-keto reductase (AKR) 1C1 ]] is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to NRF2 inducers (sulforaphane, tert-butylhydroquinone, << cinnamic aldehyde >>, and hydrogen peroxide) showed that the [[ aldo-keto reductase (AKR) 1C1 ]] is highly inducible by all treatments.

Firstly, in the normal human renal epithelial HK-2 cells, the measurement of the expression of 30 previously reported NRF2 target genes in response to NRF2 inducers (sulforaphane, tert-butylhydroquinone, cinnamic aldehyde, and << hydrogen peroxide >>) showed that the [[ aldo-keto reductase (AKR) 1C1 ]] is highly inducible by all treatments.

The treatment of U937 cells with << NRF2 >> inducers including [[ sulforaphane ]] effectively elevated the expression of AKR1B1, 1B10, 1C1, 1C2, and 1C3.

The treatment of U937 cells with NRF2 inducers including << sulforaphane >> effectively elevated the expression of [[ AKR1B1, 1B10, 1C1, 1C2, and 1C3 ]].

Whereas, the levels of both the basal and << sulforaphane >>-inducible expression of [[ AKR1C1 ]] were significantly reduced in NRF2-silenced stable U937 cells compared to the control cells.

<< Human and rat renin >> and angiotensinogen genes were downregulated in dTGR and were increased by [[ losartan ]] and cilazapril treatments, whereas no changes in the expression of rat ACE and AT1A receptor genes were observed.

Human and rat renin and << angiotensinogen >> genes were downregulated in dTGR and were increased by [[ losartan ]] and cilazapril treatments, whereas no changes in the expression of rat ACE and AT1A receptor genes were observed.

<< Human and rat renin >> and angiotensinogen genes were downregulated in dTGR and were increased by losartan and [[ cilazapril ]] treatments, whereas no changes in the expression of rat ACE and AT1A receptor genes were observed.

Human and rat renin and << angiotensinogen >> genes were downregulated in dTGR and were increased by losartan and [[ cilazapril ]] treatments, whereas no changes in the expression of rat ACE and AT1A receptor genes were observed.

<< Endothelial NO synthase >> expression was increased by [[ cilazapril ]] but not by losartan.

In addition to this pronounced loss of function, << M1766L >> also showed a 10-fold increase in the persistent late [[ sodium ]] current.

Western blot analysis revealed that << OMT >> decreased the expression of [[ Bax ]] and repaired the balance of pro- and anti-apoptotic proteins.

Furthermore, << OMT >> significantly reversed the up-regulation of [[ NR2B ]] and inhibited the calcium overload in the cultured neurons after challenging the NMDA.

<< OMT >> showed partial protection in the cortical neurons via down-regulation of NR2B containing NMDA receptors and up-regulation of [[ Bcl-2 ]] family.

<< OMT >> showed partial protection in the cortical neurons via down-regulation of NR2B containing [[ NMDA receptors ]] and up-regulation of Bcl-2 family.

<< OMT >> showed partial protection in the cortical neurons via down-regulation of [[ NR2B ]] containing NMDA receptors and up-regulation of Bcl-2 family.

<< Emodin-6-O-β-D-glucoside >> inhibits [[ HMGB1 ]]-induced inflammatory responses in vitro and in vivo.

Pharmacology of << ramelteon >>, a selective [[ MT1 ]]/MT2 receptor agonist: a novel therapeutic drug for sleep disorders.

Pharmacology of << ramelteon >>, a selective MT1/[[ MT2 ]] receptor agonist: a novel therapeutic drug for sleep disorders.

<< Ramelteon >> (Rozerem; Takeda Pharmaceutical Company Limited, Osaka, Japan) is an orally active, highly selective melatonin [[ MT(1) ]]/MT(2) receptor agonist.

<< Ramelteon >> (Rozerem; Takeda Pharmaceutical Company Limited, Osaka, Japan) is an orally active, highly selective melatonin MT(1)/[[ MT(2) ]] receptor agonist.

Unlike the sedative hypnotics that target GABA(A) receptor complexes, << ramelteon >> is a chronohypnotic that acts on the melatonin [[ MT(1) ]] and MT(2) receptors, which are primarily located in the suprachiasmatic nucleus, the body's "master clock." As such, ramelteon possesses the first new therapeutic mechanism of action for a prescription insomnia medication in over three decades.

Unlike the sedative hypnotics that target GABA(A) receptor complexes, << ramelteon >> is a chronohypnotic that acts on the melatonin MT(1) and [[ MT(2) ]] receptors, which are primarily located in the suprachiasmatic nucleus, the body's "master clock." As such, ramelteon possesses the first new therapeutic mechanism of action for a prescription insomnia medication in over three decades.

<< Am80 >> slightly inhibited the growth of both myeloma cells and HUVECs, and remarkably inhibited the growth of HUVECs stimulated by [[ VEGF ]].

<< Am80 >> inhibited VEGF-induced phosphorylation of [[ VEGF receptor ]].

<< Am80 >> inhibited [[ VEGF ]]-induced phosphorylation of VEGF receptor.

In addition, << VEGF >>-induced formation of tube-like structures in vitro and neovascularization in mouse corneas were significantly inhibited by [[ Am80 ]].

We have examined the effect of dihydropyridine << Ca2+-channel >> blockers [[ felodipine ]] and nicardipine on CaMPDE.

We have examined the effect of dihydropyridine << Ca2+-channel >> blockers felodipine and [[ nicardipine ]] on CaMPDE.

We have examined the effect of << dihydropyridine >> [[ Ca2+-channel ]] blockers felodipine and nicardipine on CaMPDE.

The results suggest that the 63-kDa (<< PDE 1B1 >>) and 60-kDa (PDE 1A2) CaMPDE isozymes are inhibited by [[ felodipine ]] and nicardipine by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

The results suggest that the 63-kDa (PDE 1B1) and 60-kDa (<< PDE 1A2 >>) CaMPDE isozymes are inhibited by [[ felodipine ]] and nicardipine by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

The results suggest that the 63-kDa (PDE 1B1) and 60-kDa (PDE 1A2) << CaMPDE >> isozymes are inhibited by [[ felodipine ]] and nicardipine by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

The results suggest that the 63-kDa (<< PDE 1B1 >>) and 60-kDa (PDE 1A2) CaMPDE isozymes are inhibited by felodipine and [[ nicardipine ]] by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

The results suggest that the 63-kDa (PDE 1B1) and 60-kDa (<< PDE 1A2 >>) CaMPDE isozymes are inhibited by felodipine and [[ nicardipine ]] by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

The results suggest that the 63-kDa (PDE 1B1) and 60-kDa (PDE 1A2) << CaMPDE >> isozymes are inhibited by felodipine and [[ nicardipine ]] by partial competitive inhibition and that these two Ca2+ antagonists appear to counteract each other.

Felodipine and nicardipine have similar affinities for 60-kDa << CaMPDE >> isozymes but bring about different levels of enzyme inhibition, suggesting the possibility of designing specific drugs that can protect the enzyme from inhibition by [[ dihydropyridine ]] Ca2+-channel blockers.

Felodipine and nicardipine have similar affinities for 60-kDa CaMPDE isozymes but bring about different levels of enzyme inhibition, suggesting the possibility of designing specific drugs that can protect the enzyme from inhibition by << dihydropyridine >> [[ Ca2+-channel ]] blockers.