Plasma renin activity and changes in tissue angiotensin converting enzyme.
OBJECTIVE
Recent evidence suggests that tissue generation of angiotensins I and II depends on the level of the plasma components of the renin-angiotensin system and on tissue-specific processes. The present study was undertaken to clarify the possible relationship between plasma renin activity (PRA) and tissue angiotensin converting enzyme (ACE) activity in the heart, lung, kidney cortex and kidney medulla of Wistar-Kyoto rats. In the kidney cortex particular attention was focused on renal brush-border ACE.


METHODS
Different experimental models known to have opposite effects on PRA were used: changes in salt intake, deoxycorticosterone acetate (DOCA) with or without salt supplements, and the Goldblatt two-kidney, one clip (2-K,1C) model. Two weeks after the start of the experiments the rats were killed, and PRA, and plasma and tissue ACE activity, were measured.


RESULTS
At the end of the study the blood pressure in the treated rats was not significantly different from control. As expected, the PRA were highest in the 2-K,1C and depleted-salt groups and lowest in the DOCA, DOCA-salt and high-salt groups. ACE responses were different in different types of tissue, with no relationship between PRA and plasma or tissue ACE activity. For example, DOCA treatment led to increased ACE activity in the heart and the kidney only if the rats were maintained on a high salt intake. DOCA or salt alone failed to have this effect. In the 2-K,1C model the unclipped kidneys did not show any significant variation in ACE activity, but the clipped kidneys exhibited increased ACE activity compared with sham-operated rats. This increase, coupled with increased renal renin secretion, could play a role in the acceleration of local angiotensin II formation, and could thus initiate and sustain the development of hypertension in this model.


CONCLUSIONS
The present results show that variations in ACE activity were organ-specific and were not linked either to hypertension or to changes in PRA.
Michel
B
B
Institut de Pharmacologie (URA D0589 CNRS), Université Louis Pasteur, Strasbourg, France.
Grima
M
M
Stephan
D
D
Coquard
C
C
Welsch
C
C
Barthelmebs
M
M
Imbs
J L
JL
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000378:metabolism; D000818:Animals; D003900:Desoxycorticosterone / Q000494:pharmacology; D006978:Hypertension, Renovascular / Q000378:metabolism; D007668:Kidney / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008297:Male; D008871:Microvilli / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology; D007703:Peptidyl-Dipeptidase A / Q000097:blood / Q000378:metabolism*; D017257:Ramipril / Q000031:analogs & derivatives / Q000378:metabolism; D051381:Rats; D011921:Rats, Inbred WKY; D012083:Renin / Q000097:blood*; D012965:Sodium Chloride / Q000494:pharmacology
D000806:Angiotensin-Converting Enzyme Inhibitors; D003900:Desoxycorticosterone; D012965:Sodium Chloride; C052549:ramiprilat; D007703:Peptidyl-Dipeptidase A; D012083:Renin; D017257:Ramipril