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Journal of Andrology, Vol 2, Issue 2 94-102, Copyright © 1981 by The American Society of Andrology

Rat Testicular Phospholipase A2 Activity:

pH Optima, Its Cellular and Subcellular Distribution in the Gonad, and Some Factors That May Modulate Its Activity

LEGRANDE C. ELLIS 1, JAMES R. BOCCIO 1, MICHAEL J. CUNNINGHAM 1, MICHAEL D. GROESBECK 1, AND M. JAMES COSENTINO 1

1 Departments of Biology and Chemistry, Utah State University, Logan, Utah

A sensitive radiometric assay was developed for detecting phospholipase A1 and A2 (PLA1 and A2) activity. Four to five times more PLA2 activity was observed in rat testes than PLA1 activity. Two PLA2 were observed in the testis, one with an acid (3.5) and one with an alkaline (7.5-8.0) pH optimum. The acid pH optimal PLA2 was located in the interstitial and lysosomal fractions. The alkaline pH optimal PLA2 was localized in the germinal elements of the seminiferous tubules and in the lysosomalenriched and membrane-enriched fractions. Triton X-100 inhibited PLA2 at 10-2 M and inhibited PLA1 at 10-3 M. At 10-2 M, triton X-100 activated PLA1. EGTA inhibited PLA2 activity, whereas Ca++ at 10-2 to 10-3 M restored this activity. Corticosterone had no effect on PLA2 activity, but progesterone, dihydrotestosterone, and testosterone all stimulated the enzyme at lower concentrations (10-9-10-7 M), with testosterone giving maximum stimulation at a lower dosage (ie, 10-9 M compared to 10-7 M for dihydrotestosterone). Both androgens inhibited PLA2 activity at higher concentrations.

     Key words: rat testicular phospholipase A2 activity, pH optima, localization, control

Submitted on June 9, 1980
Revised on September 8, 1980
Accepted on October 29, 1980






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Copyright © 1981 by The American Society of Andrology.