Abstract
Pretreatment of hog high molecular weight renin for 30 min at 37 degrees C with 0.12 unit of either kallikrein or thrombin significantly increased (p less than 0.001) the amount of angiotensin I formed during subsequent incubations with homologous angiotensinogen. However, the thrombin-treated hog renin had 13 times more activity than the kallikrein-treated enzyme. Aprotinin did not inhibit the kallikrein-mediated activation of renin; the results indicated that aprotinin inhibited renin preferentially. Plasmin (0.25 unit) had little effect on the activity of high molecular weight renin. The molecular weight of hog renin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was not altered after exposure to either kallikrein, thrombin, or plasmin. These results do not exclude the occurrence of a limited proteolytic event or a conformational change beyond the detection of the current method. The data show that the activation of hog high molecular weight renin by thrombin and kallikrein was not associated with the conversion of renin to Mr = 43,000.
Highlights
Pretreatment of hog high molecular weight renin for 30 min at 37°C with 0.12 unit of either kallikrein or thrombin significantly increased (p < 0.001) the amount of angiotensin I formed during subsequent incubations with homologous angiotensinogen
The molecular weight of hog renin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was not altered after exposure to either kallikrein, thrombin, or plasmin
The data show that the activation of hog high molecular weight renin by thrombin and kallikrein was not associated with the conversion of renin to lI2, = 43,000
Summary
Pretreatment of hog high molecular weight renin for 30 min at 37°C with 0.12 unit of either kallikrein or thrombin significantly increased (p < 0.001) the amount of angiotensin I formed during subsequent incubations with homologous angiotensinogen. The molecular weight of hog renin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was not altered after exposure to either kallikrein, thrombin, or plasmin. These results do not exclude the occurrence of a limited proteolytic event or a conformational change beyond the detection of the current method. The addition of serine protease inhibitors to plasma prior to cold exposure has been found to prevent most of the anticipated cryoactivation of renin [12, 13]. These reports suggest that proteases are involved in renin activation
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