amastatin and zincov

amastatin has been researched along with zincov* in 2 studies

Other Studies

2 other study(ies) available for amastatin and zincov

Article	Year
Intracisternal neutral endopeptidase-24.11 inhibitors produce inhibition in gastric acid output: independence from opiate, bombesin, or neurotensin-mediated mechanisms. Regulatory peptides, 1993, Jul-23, Volume: 46, Issue:3 Intracisternal (ic) injection of the neutral endopeptidase-24.11 inhibitor phosphoramidon (1-100 nmol) produced a dose-dependent inhibition of gastric acid secretion in 2-h pylorus-ligated rats. The response resulted from a reduction in acid concentration and volume. Likewise, ic injection of another neutral endopeptidase-24.11 inhibitor Zincov (200 nmol) produced a 63% inhibition in gastric acid output. In contrast, neither intravenous injection of phosphoramidon (100 nmol) nor ic injection of the aminopeptidase inhibitor amastatin (100 nmol) produced any change in gastric acid secretion. The inhibitory effect of ic phosphoramidon (10 nmol) was not reversed by a dose of naloxone sufficient to antagonize the acid inhibitory effects of ic [D-Ala2-D-met5]enkephalinamide (8.5 nmol). Moreover, phosphoramidon-induced inhibition of acid was not reduced by the centrally effective bombesin antagonist N-acetyl-GRP(20-26)-O-CH3 or by reserpine pretreatment at a dose effective to antagonize ic neurotensin-induced inhibition in acid secretion. These results suggest that an endogenous neutral endopeptidase-24.11 sensitive substrate may act in the brain to inhibit gastric acid output by mechanisms independent of CNS opiate, bombesin or neurotensin activity. Topics: Animals; Anti-Bacterial Agents; Drug Interactions; Gastric Acid; Gastrointestinal Hormones; Glycopeptides; Hydroxamic Acids; Injections, Intravenous; Injections, Intraventricular; Male; Naloxone; Neprilysin; Oligopeptides; Peptides; Rats; Rats, Sprague-Dawley; Reserpine	1993
Peptide hydroxamic acids inhibit skin collagenase. Biochemical and biophysical research communications, 1986, Apr-14, Volume: 136, Issue:1 A number of peptide hydroxamic acids have been synthesized and have been shown to be inhibitors of human skin collagenase. One of these, Z-Pro-Leu-Gly-NHOH, has an IC50 value of 4 X 10(-5)M. Corresponding peptides with different C-terminal functional groups, such as amide, carboxylate and aldehyde, showed little or no inhibition, indicating the importance of the hydroxamate functional group. In addition, the peptide sequence of this effective inhibitor corresponds closely to that of the cleavage site of native collagen, the substrate for the enzyme. Thus, substrate analogs incorporating a suitable metal coordinating group serve as potential inhibitors of human collagenase. Topics: Anti-Bacterial Agents; Captopril; Endopeptidases; Fibroblasts; Humans; Hydroxamic Acids; Metalloendopeptidases; Microbial Collagenase; Oligopeptides; Peptides; Protease Inhibitors; Skin	1986

Article

Year

Intracisternal neutral endopeptidase-24.11 inhibitors produce inhibition in gastric acid output: independence from opiate, bombesin, or neurotensin-mediated mechanisms.

Regulatory peptides, 1993, Jul-23, Volume: 46, Issue:3

Intracisternal (ic) injection of the neutral endopeptidase-24.11 inhibitor phosphoramidon (1-100 nmol) produced a dose-dependent inhibition of gastric acid secretion in 2-h pylorus-ligated rats. The response resulted from a reduction in acid concentration and volume. Likewise, ic injection of another neutral endopeptidase-24.11 inhibitor Zincov (200 nmol) produced a 63% inhibition in gastric acid output. In contrast, neither intravenous injection of phosphoramidon (100 nmol) nor ic injection of the aminopeptidase inhibitor amastatin (100 nmol) produced any change in gastric acid secretion. The inhibitory effect of ic phosphoramidon (10 nmol) was not reversed by a dose of naloxone sufficient to antagonize the acid inhibitory effects of ic [D-Ala2-D-met5]enkephalinamide (8.5 nmol). Moreover, phosphoramidon-induced inhibition of acid was not reduced by the centrally effective bombesin antagonist N-acetyl-GRP(20-26)-O-CH3 or by reserpine pretreatment at a dose effective to antagonize ic neurotensin-induced inhibition in acid secretion. These results suggest that an endogenous neutral endopeptidase-24.11 sensitive substrate may act in the brain to inhibit gastric acid output by mechanisms independent of CNS opiate, bombesin or neurotensin activity.

Topics: Animals; Anti-Bacterial Agents; Drug Interactions; Gastric Acid; Gastrointestinal Hormones; Glycopeptides; Hydroxamic Acids; Injections, Intravenous; Injections, Intraventricular; Male; Naloxone; Neprilysin; Oligopeptides; Peptides; Rats; Rats, Sprague-Dawley; Reserpine

1993

Peptide hydroxamic acids inhibit skin collagenase.

Biochemical and biophysical research communications, 1986, Apr-14, Volume: 136, Issue:1

A number of peptide hydroxamic acids have been synthesized and have been shown to be inhibitors of human skin collagenase. One of these, Z-Pro-Leu-Gly-NHOH, has an IC50 value of 4 X 10(-5)M. Corresponding peptides with different C-terminal functional groups, such as amide, carboxylate and aldehyde, showed little or no inhibition, indicating the importance of the hydroxamate functional group. In addition, the peptide sequence of this effective inhibitor corresponds closely to that of the cleavage site of native collagen, the substrate for the enzyme. Thus, substrate analogs incorporating a suitable metal coordinating group serve as potential inhibitors of human collagenase.

Topics: Anti-Bacterial Agents; Captopril; Endopeptidases; Fibroblasts; Humans; Hydroxamic Acids; Metalloendopeptidases; Microbial Collagenase; Oligopeptides; Peptides; Protease Inhibitors; Skin

1986