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Hypertension. 1999;34:520-524

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(Hypertension. 1999;34:520-524.)
© 1999 American Heart Association, Inc.


Scientific Contributions

Rat Renal and Plasma Prorenin Are Activated In Vitro by Different Mechanisms

Paula A. Vincent; Eduardo De Vito

From the Instituto Superior de Investigaciones Biológicas (INSIBIO), Universidad Nacional de Tucumán and Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), San Miguel de Tucumán (E.D.V., P.A.V.), Argentina.

Abstract—The aim of the present study was to purify and identify a plasma protein fraction (PreR-Co) involved in renal prorenin activation and to explore its capacity to process plasma prorenin. PreR-Co was obtained from plasma as a single electrophoretic band by (NH4)2SO4 precipitation, Sephacryl S-200 HR gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. The amidase, esterase, and kallikrein activities of PreR-Co were studied, as was its N-terminal amino acid sequence. Rat kidney extract or plasma (normal or previously treated with acid to pH 2.8) were incubated with PreR-Co for 15 minutes at 37°C. Renin concentration was measured by incubation with homologous angiotensinogen. The same protocol was repeated with samples activated by trypsin. The N-terminal amino acid sequence was IIGGSMDAKGSFP, which had a homology of 90% with the ß-chain of haptoglobin, 69% with serine-proteases, and 65% with kallikreins. The renin concentration in rat kidney extract was 34±4 ng of angiotensin I (Ang I) · mg of tissue-1 · h-1. After PreR-Co or trypsin treatments, renin concentrations were 211±7 and 110±11 ng of Ang I · mg of tissue-1 · h-1, respectively. The plasma renin concentration in normal plasma was 67.6±13.3 ng of Ang I · mL-1 · h-1, and no significant difference was observed after PreR-Co treatment. However, a significant increase (202.8±7.8 ng of Ang I · mL-1 · h-1; P<0.01) was found after trypsin treatment. The isolated PreR-Co acts on renal prorenin but not on plasma prorenin. These results suggest that active renin is processed in the kidney by a circulating enzyme that may have a role in the regulation of circulating renin.


Key Words: kidney • renin • renin-angiotensin system




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The novel serine protease PreR-Co promotes endothelium-independent vasorelaxation in rabbit aortic rings
Am J Physiol Heart Circ Physiol, February 1, 2003; 284(2): H704 - H710.
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