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Tryptic activation of plasma renin activity
The Journal of Clinical Endocrinology and Metabolism
|June 1, 1980
Summary
Trypsin activation of human plasma reveals an inactive renin precursor. This finding supports the existence of a previously unknown form of renin in circulation, crucial for understanding renin regulation.
Area of Science:
- Biochemistry
- Endocrinology
- Physiology
Background:
- Renin activity in human plasma can be increased by various activation methods, including acid and cryoactivation.
- Understanding the mechanisms of renin activation is essential for studying the renin-angiotensin-aldosterone system (RAAS).
Purpose of the Study:
- To investigate the effect of trypsinization on human plasma renin activity.
- To determine the optimal conditions for tryptic activation of plasma renin.
- To explore the implications of tryptic activation for the existence of inactive renin precursors.
Main Methods:
- Human plasma samples were treated with varying concentrations of trypsin.
- Renin activity was measured using enzymatic assays.
- Plasma renin reactivity and substrate levels were assessed after trypsin treatment.
Main Results:
- Trypsinization significantly increased plasma renin activity (PRA), with maximal activation observed at 500 micrograms/ml trypsin within 2 minutes.
- Prolonged incubation or temperature variations (0°C or 37°C) did not affect tryptic activation.
- Plasma renin reactivity and substrate remained unaltered at optimal trypsin concentrations, suggesting activation of a precursor rather than alteration of existing components.
Conclusions:
- The data strongly support the existence of an inactive renin precursor in human plasma.
- Trypsin effectively activates this precursor, leading to increased measurable renin activity.
- Careful optimization of trypsin concentration is necessary to avoid degradation of the renin assay system and maximize activation.