Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.16.2 (PCP)
 3,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antibodies raised in rabbits to detergent-solubilized pig kidney microvillar proteins have been used to investigate the membrane hydrolases by crossed immunoelectrophoresis. Eight enzymes were detected by specific staining methods: aminopeptidase M, dipeptidylpeptidase IV, neutral endopeptidase, aminopeptidase A, carboxypeptidase P, gamma-glutamyltransferase, trehalase and phosphodiesterase I. The mobility of all these enzymes, with the exception of trehalase and neutral endopeptidase, was increased by treatment of the detergent-solubilized preparation with papain. The difference between the detergent and proteinase forms of these enzymes is attributed to the removal of a small, non-antigenic peptide to which detergent is bound in significant quantities. This interpretation was further supported by experiments in which the microvillus fraction was labelled with an intramembrane photolabelling reagent, 1-azido-4-[125I]iodobenzene. After photolysis, the radioactivity in the membrane could be solubilized by detergent treatment but not by papain treatment. Radioautography after crossed charge-shift immunoelectrophoresis showed a good correlation between charge-shift (signifying the presence of detergent bound to a hydrophobic domain) and the presence of the label.
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PMID:Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolases: identification and resolution of the detergent- and proteinase-solubilized forms. 48 90

Two intestinal brush border membrane carboxypeptidases were found to participate in the sequential digestion of proline-containing peptides representing a novel mechanism of hydrolysis from the COOH terminus. NH2-blocked prolyl tripeptides were rapidly hydrolyzed by either brush border membrane angiotensin converting enzyme (ACE, dipeptidyl carboxypeptidase, E.C. 3.4.15.1) or carboxypeptidase P (E.C.3.4.12-) depending on the position of the proline residue. Furthermore, these two enzymes were found to participate in a concerted manner to sequentially degrade larger proline-containing pentapeptides from the COOH terminus. A brush border membrane associated neutral endopeptidase also participated in the hydrolysis of the prolyl pentapeptides. During in vivo intestinal perfusion, the NH2-blocked prolyl peptides were degraded and their constituent amino acids efficiently absorbed by the intestine. Furthermore, hydrolysis and absorption of these peptides could be dramatically suppressed by low concentrations of captopril, a specific inhibitor of ACE. These studies show that prolyl peptides are efficiently and sequentially hydrolyzed from the COOH terminus by the combined action of ACE and carboxypeptidase P, and that these enzymes may play an important role in the digestion and assimilation of proline-containing peptides.
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PMID:Digestion and assimilation of proline-containing peptides by rat intestinal brush border membrane carboxypeptidases. Role of the combined action of angiotensin-converting enzyme and carboxypeptidase P. 283 43

We investigated the effects of thiorphan, a specific inhibitor of enkephalinase A and bestatin, a specific inhibitor of aminopeptidase, on the stereotyped behaviors induced by phencyclidine (PCP) in cannulated rats. The PCP-induced turning was significantly potentiated when thiorphan (50 micrograms) and bestatin (50 micrograms) were injected simultaneously into the rat lateral ventricle. The increase of PCP-induced turning was completely antagonized by the pretreatment with naloxone. Thiorphan (50 micrograms) or bestatin (50 micrograms) alone failed to potentiate PCP-induced turning. Thiorphan and/or bestatin did not affect significantly the PCP-induced head weaving and back-pedalling except that thiorphan (50 micrograms) potentiated the PCP-induced head weaving 15-18 min after the PCP injection. The combination of thiorphan and bestatin alone did not induce any behavioral change. These results suggest that thiorphan and bestatin produce an increase of endogenous enkephalins and that as a result, PCP-induced turning may be enhanced.
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PMID:Potentiation of phencyclidine-induced stereotyped behaviors in rats by thiorphan and bestatin. 345 6

Ang-(1-7) [angiotensin-(1-7)] constitutes an important functional end-product of the RAS (renin-angiotensin system) endogenously formed from AngI (angiotensin I) or AngII (angiotensin II) through the catalytic activity of ACE2 (angiotensin-converting enzyme 2), prolyl carboxypeptidase, neutral endopeptidase or other endopeptidases. Ang-(1-7) lacks the pressor, dipsogenic or stimulatory effect on aldosterone release characteristic of AngII. In contrast, it produces vasodilation, natriuresis and diuresis, and inhibits angiogenesis and cell growth. At the central level, Ang-(1-7) acts at sites involved in the control of cardiovascular function, thus contributing to blood pressure regulation. This action may result from its inhibitory neuromodulatory action on NE [noradrenaline (norepinephrine)] levels at the synaptic cleft, i.e. Ang-(1-7) reduces NE release and synthesis, whereas it causes an increase in NE transporter expression, contributing in this way to central NE neuromodulation. Thus, by selective neurotransmitter release, Ang-(1-7) may contribute to the overall central cardiovascular effects. In the present review, we summarize the central effects of Ang-(1-7) and the mechanism by which the peptide modulates NE levels in the synaptic cleft. We also provide new evidences of its cerebroprotective role.
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PMID:Neuromodulatory role of angiotensin-(1-7) in the central nervous system. 2353 Jun 69