AJP - Endocrinology and Metabolism, Vol 248, Issue 6 694-E698, Copyright © 1985 by American Physiological Society
Modification of renin isoelectric heterogeneity in Goldblatt hypertensive rat
F. M. Sessler and R. L. Malvin
Six forms of renin have been described in rat kidney. Different stimuli
resulted in secretion of unique profiles of those forms. We studied their
storage and secretion in the two-kidney, one-clip Goldblatt hypertensive
rat (GHR). Renal venous blood, kidney homogenates, and incubation media
from cortical slices were subjected to isoelectric focusing. In all samples
tested, six peaks of renin activity were found with isoelectric points at
pH 5.90, 5.70, 5.40, 5.20, 5.00, and 4.80. The quantity of renin activity
for each form was expressed as a percentage of the total recovered from the
gel. In control kidneys the profile of renin stored and that released by in
vitro slices were similar. However, in plasma, the percentage of renin
focusing at the more basic pH was decreased. This is in agreement with
other work showing that the liver removes the more basic forms more rapidly
than the acidic forms. The clipped kidney of GHR secreted, both in vivo and
in vitro, a profile of renin forms that was significantly different from
the control kidney. The difference was expressed by an increase in the
secretion of the more acidic forms by the clipped kidney. It is
hypothesized that changes in the secretory profile of renin may reflect
changes in storage and synthesis of those forms.
