Occurrence of Big Renin in Human Plasma, Amniotic Fluid and Kidney Extracts

Abstract

Big renin, a relatively inactive renin which possesses a molecular weight larger than that of normal plasma or renal renin, has been demonstrated by gel filtration in certain human plasma, tumor extracts, and amniotic fluid. Big renin was not present in normal plasma or kidney extracts. Plasma from 3 hypertensive patients with nephropathy contained chiefly big renin. Varying proportions of both big and normal renin activity were present in plasma of other patients with hypertension and proteinuria. The renin present in amniotic fluid, which increased in activity following exposure to acid pH, was shown to be big renin in two patients. Large amounts of circulating big renin apparently can cause hypertension in patients with Wilms' tumors. Furthermore, the relatively inactive big renin may replace normal plasma renin in some patients, resulting in low plasma renin activity.

<b>INTERMEDIATE MOLECULAR WEIGHT RENIN AND RENIN-BINDING PROTEIN(S) IN THE HOG </b><b>KIDNEY </b>

“…3.0 or pH 10. 5. Confirma-tion of this speculation would be provided after further purification of the binding proteins.…”

Pathophysiological Significance of Plasma Total Renin and Prorenin in Patients with Diabetes Mellitus.

“…Plasma inactive renin, viz. prorenin, has been of interest because of its significant increase in certain pathological states including renin secreting tumors [9,10] and diabetes mellitus [11,12] has been reported to be significantly increased [11,12] and to correlate with diabetic complications [12][13][14][15][16][17] Plasma prorenin has been determined by enzyme kinetic assay after activation by various pretreatments [1][2][3][4] in which the angiotensin I generated by plasma in vitro is measured by radioimmunoassay. The plasma renin activity, however, can be affected by the amount of plasma angiotensinogen.…”

The changes in active and inactive renin induced by various maneuvers in hypertensive patients.

“…Inactive renin can be activatReceived August 24, 1984; accepted for publication April 22, 1986. 169 ed in vitro by acidification (Skinner et al 1975), low temperature (Osmond et al 1973;Sealey and Laragh 1975), or trypsin and other proteolytic enzymes (Day et al 1975;Sealey et al 1979). However, in vivo, the conversion of inactive renin to active renin is not yet proved or disproved.…”