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Abstract
Potent and specific aminopeptidase A (APA; glutamylaminopeptidase, EC 3.4.11.7) inhibitors could be useful as powerful tools in the study of the physiological involvement of this enzyme in the metabolism of various peptides. Thus, using newly designed selective APA inhibitors, APA has been shown to participate in the metabolism of cholecystokinin and to be responsible for the conversion of angiotensin II (Ang II), a peripheral vasoconstrictor peptide, into Ang III, which has been recently shown to induce an increase in blood pressure and in vasopressin release in rat brain. Moreover, APA was shown to be overexpressed in several types of malignant tumours, probably by inducing the formation of as yet unidentified cell proliferating active peptide(s). This review highlights advances in the structure and functions of APA and in the design of very potent and selective inhibitors of this zinc metallopeptidase. These compounds could have interesting applications in the treatment of essential hypertension and their usefulness in cancer chemotherapy warrants further investigations.
