| Autor: |
Linz, Wolfgang, Wiemer, Gabriele, Schaper, Jutta, Zimmermann, René, Nagasawa, Kazushige, Gohlke, Peter, Unger, Thomas, Schölkens, Bernward |
| Zdroj: |
Molecular & Cellular Biochemistry; Jun1995, Vol. 147 Issue 1/2, p89-97, 9p |
| Abstrakt: |
From pharmacological investigations and clinical studies, it is known that angiotensin converting enzyme (ACE) inhibitors exhibit additional local actions, which are not related to hemodynamic changes and which cannot be explained only by interference with the renin angiotensin system (RAS) by means of an inhibition of angiotensin II (ANG II) formation. Since ACE is identical to kininase II, which inactivates the nonapeptide bradykinin (BK) and related kinins, potentiation of kinins might be responsible for these additional effects of ACE inhibitors.These experimental findings in different models of LVH characterise ACE inhibitors as remarkable antihypertrophic and antifibrotic substances. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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