Journal of Clinical Endocrinology & Metabolism, Vol 74, 680-684, Copyright © 1992 by Endocrine Society

ARTICLES

Evidence for the presence of differently glycosylated forms of prorenin in the plasma of anephric man

M Hosoi, S Kim, T Tabata, H Nishitani, Y Nishizawa, H Morii, K Murakami and K Yamamoto
Department of Pharmacology, Osaka City University Medical School, Japan.

Previously, we unexpectedly observed that plasma inactive renin (trypsin-activatable renin) in bilaterally nephrectomized rats is not prorenin. To determine whether plasma inactive renin in anephric man is prorenin, we examined the immunological and biochemical properties of plasma inactive renin from five anephric patients. There were significant concentrations of inactive renin (5.33 +/- 2.08 ng/L.s) in plasma of anephric patients, while active renin was negligible (0.06 +/- 0.01 ng/L.s). The inactive renin from anephric patients could be immunoprecipitated 97 +/- 1% by specific antiserum against the prosegment portion of prorenin. Specific antimature renin serum completely inhibited the angiotensin-I-generating activity of inactive renin induced by trypsin treatment. The molecular mass of inactive renin from anephric patients (49.0 +/- 0 kDa), estimated by gel permeation high performance liquid chromatography, was similar to that of normal human plasma prorenin (48.2 +/- 0.8 kDa). These results indicate that plasma inactive renin in anephric man is prorenin, findings different from our previous observations obtained in anephric rats. Concanavalin-A chromatography separated inactive renin from anephric patients into three forms, including the column-unbound form, the loosely bound form, and the tightly bound form. Thus, in anephric man, differently glycosylated multiple forms of prorenin are released into the circulation from an extrarenal organ(s).

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