Potentiation by aminopeptidase P of blood pressure response to bradykinin
Open Access
- 1 January 1995
- journal article
- Published by Wiley in British Journal of Pharmacology
- Vol. 114 (1) , 6-7
- https://doi.org/10.1111/j.1476-5381.1995.tb14897.x
Abstract
We examined whether a specific aminopeptidase P (APP) inhibitor, apstatin, increases vasodepressor responses to bradykinin in anaesthetized rats, and whether it would augment blood pressure responses further after treatment with the angiotensin-converting enzyme inhibitor (ACEi), lisinopril. Apstatin doubled the maximum blood pressure response to bradykinin. The area under the curve (AUC), which incorporates both peak blood pressure changes and duration of response, was doubled in apstatin-treated rats vs controls and in the apstatin + lisinopril group vs lisinopril alone. These data demonstrate that APP is an important kininase in vivo.Keywords
This publication has 6 references indexed in Scilit:
- Endothelial protection by converting enzyme inhibitorsCardiovascular Research, 1994
- Membrane-bound aminopeptidase P from bovine lung. Its purification, properties, and degradation of bradykinin.Journal of Biological Chemistry, 1992
- Inhibition by converting enzyme inhibitors of pig kidney aminopeptidase P.Hypertension, 1992
- Metabolism of bradykinin agonists and antagonists by plasma aminopeptidase PBiochemical Pharmacology, 1991
- Role of angiotensin converting enzyme and other peptidases in in vivo metabolism of kinins.Hypertension, 1989
- Aminopeptidase P activity in rat organs and human serumAnalytical Biochemistry, 1987