About: Inhibition of aminopeptidases N, A and W A re-evaluation of the actions of bestatin and inhibitors of angiotensin converting enzyme

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About: Inhibition of aminopeptidases N, A and W A re-evaluation of the actions of bestatin and inhibitors of angiotensin converting enzyme Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Inhibition of aminopeptidases N, A and W A re-evaluation of the actions of bestatin and inhibitors of angiotensin converting enzyme
Creator	Tieku, Stephen Hooper, Nigel
source	Elsevier; Medline; PMC
abstract	Abstract The effects of a range of metallopeptidase inhibitors on the activities of the porcine kidney cell surface zinc aminopeptidases, aminopeptidase A (AP-A; EC 3.4.11.2), aminopeptidase N (AP-N; EC 3.4.11.7) and aminopeptidase W (AP-W; EC 3.4.11.16), have been directly compared. Amastatin and probestin were effective against all three aminopeptidases, with the concentration of inhibitor required to cause 50% inhibition (I50) in the low micromolar range (I50 = 1.5–20 μM), except for probestin with AP-N which displayed an I50 of 50 nM. Actinonin failed to inhibit significantly either AP-A or AP-W, and thus can be considered a relatively selective inhibitor (I50 = 2.0 μM of AP-N. In contrast, bestatin was a relatively poor inhibitor of AP-N (I50 = 89 μm) and failed to inhibit AP-A, but was more potent towards AP-W (I50 = 7.9 μM). Thus, some of the observed chemotherapeutic actions of bestatin may be due to inhibition of cell-surface AP-W. A number of other metallopeptidase inhibitors, including inhibitors of endopeptidase-24.11 (EC 3.4.24.11) and membrane dipeptidase (EC 3.4.13.11), and the carboxylalkyl and phosphoryl inhibitors of angiotensin converting enzyme (EC 3.4.15.1) failed to inhibit significantly AP-A, AP-N or AP-W. However, AP-W was inhibited with I50 values in the micromolar range by the sulphydryl converting enzyme inhibitors rentiapril (I50 = 1.6 μM), zofenoprilat (I50 = 7.0 μM) and YS 980 (I50 = 17.7 μM). Neither AP-A nor AP-N were affected by these sulphydryl compounds. Inhibition of AP-W may account for some of the side effects noted with the clinical use of the sulphydryl converting enzyme inhibitors. The availability of compounds which are totally selective for AP-W over any of the other mammalian cell surface zinc aminopeptidases may aid in identifying endogenous substrates, and thus physiological or pathophysiological role(s) of AP-W.
has issue date	1992-11-03(xsd:dateTime)
bibo:doi	10.1016/0006-2952(92)90065-q
bibo:pmid	1360211
has license	els-covid
sha1sum (hex)	3843020862eda73775740154e71c3e991ebaaf8f
schema:url	https://doi.org/10.1016/0006-2952%2892%2990065-q
resource representing a document's title	Inhibition of aminopeptidases N, A and W A re-evaluation of the actions of bestatin and inhibitors of angiotensin converting enzyme
has PubMed Central identifier	PMC7111144
has PubMed identifier	1360211
schema:publication	Biochemical Pharmacology
resource representing a document's body	covid:3843020862eda73775740154e71c3e991ebaaf8f#body_text
is schema:about of	named entity 'metallopeptidase' named entity 'inhibit' named entity 'THE' named entity 'RE-EVALUATION' named entity 'ENZYME' named entity 'DUE TO' named entity 'EFFECTIVE' named entity 'MICROMOLAR' named entity 'BUT' named entity 'EITHER' named entity 'AMINOPEPTIDASE N' named entity 'ZINC' named entity 'AMASTATIN' named entity 'EC 3' named entity 'AMINOPEPTIDASE W' named entity '50%' named entity 'ACTIONS' named entity 'METALLOPEPTIDASE' named entity '1.5' named entity 'ANGIOTENSIN CONVERTING ENZYME' named entity 'BESTATIN' covid:arg/3843020862eda73775740154e71c3e991ebaaf8f named entity 'AMINOPEPTIDASE A' named entity 'RENTIAPRIL' named entity '3.4' named entity 'KIDNEY CELL' named entity 'INHIBITED' named entity 'ACTINONIN' named entity 'ACTIONS' named entity 'INHIBITORS' named entity 'EON' named entity 'FAILED' named entity 'NUMBER OF' named entity 'CONTRAST' named entity 'VALUES' named entity 'INHIBITORS' named entity 'CONVERTING' named entity 'POOR' named entity 'AP-N' named entity 'ACTIVITIES' named entity 'LOW' named entity 'SULPHYDRYL' named entity 'MEMBRANE DIPEPTIDASE' named entity 'PORCINE' named entity 'AMINOPEPTIDASES' named entity '3.4.24.11' named entity 'OBSERVED' named entity 'BESTATIN' named entity 'ENDOPEPTIDASE' named entity 'PEPTIDASES' named entity 'INHIBITION' named entity 'DISPLAYED' named entity 'DIRECTLY' named entity 'CELL SURFACE' named entity '3.4.15.1' named entity 'INCLUDING' named entity 'REQUIRED' named entity 'CONSIDERED' named entity '28I' named entity 'WAS A' named entity 'PROBESTIN' named entity 'TO INHIBIT' named entity 'SELECTIVE' named entity 'PHOSPHO' named entity 'CAUSE' named entity 'CELL' named entity 'MAY BE' named entity '1.6' named entity 'RANGE' named entity 'HAVE' named entity 'INHIBITOR' named entity 'COMPARED' named entity 'EFFECTS' named entity 'ENZYME INHIBITORS' named entity 'INHIBITION' named entity 'SURFACE' named entity 'EC 3.4.11.2' named entity 'EXCEPT FOR' named entity 'range' named entity 'zinc'

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