This Article Full Text (PDF) Submit a related Letter to the Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via Google Scholar Google Scholar Articles by ZIPSER, R. D. Articles by HORTON, R. Search for Related Content PubMed PubMed Citation Articles by ZIPSER, R. D. Articles by HORTON, R.

Deoxycorticosterone and Aldosterone Clearance and Binding in Normal and Hypertensive Man^*

Section of Endocrinology, University of Southern California-Los Angeles County Medical Center Los Angeles, California 90033

Address requests for reprints to: Dr. Zipser, USC School of Medicine, Room 18-632, 2025 Zonal Avenue, Los Angeles, California 90033.

Deoxycorticosterone (DOC) may play a role in several hypertensive disorders in man, but the dynamics of DOC metabolism are unclear. To characterize DOC binding to plasma proteins and its MCR, 12 patients with essential hypertension and 10 age-matched controls were studied. In control subjects, the DOC MCR was nearly identical to the simultaneously measured aldosterone MCR (719 ± 32 vs. 734 ± 61 liters%m² • day, respectively), and the MCRs of both steroids were not significantly different in essential hypertension (682 ± 49 and 672 ± 50 liters%m²-day, respectively). Whole blood MCR was also unaltered by hypertension. The DOC whole blood MCRs were 1056 ± 85 and 1040 ± 69 liters%m² • day for control and hypertensive subjects, respectively. The aldosterone whole blood MCRs were 916 ± 96 and 941 ± 67 liters%m² • min. The similarity of the DOC MCR to the aldosterone MCR suggested minimal binding of DOC to high affinity carrier proteins, and this was confirmed by equilibrium dialysis with [³H]D0C at 37 C. In plasma, 6 ± 1% of DOC is unbound, 84 ± 3% is bound to albumin, and only 10 ± 4% is bound to nonalbumin proteins. We conclude that the dynamics of DOC closely resemble those of aldosterone, with minimal plasma binding to specific binding proteins and high MCR that are unaltered in essential hypertension.

^* This work was supported by grants from the NIH (HL-21112 and RR-43) and a Research Award from the American Heart Association-Greater Los Angeles Affiliate (567-Cl).

Received March 14, 1980.