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The Membrane-Bound Spermatozoal Adenylyl Cyclase System Does not Share Coupling Characteristics with Somatic Cell Adenylyl Cyclases^*

JOHN D. HILDEBRANDT, JUAN CODINA, JOSEPH S. TASH, HOWARD J. KIRCHICK, LAWRENCE LIPSCHULTZ, RONALD D. SEKURA and LUTZ BIRNBAUMER

Departments of Cell Biology Baylor College Medicine Houston, Texas 77030;
Urology Baylor College Medicine Houston, Texas 77030;
Laboratory of Developmental and Molecular Immunity, National Laboratory of Developmental and Molecular Immunity, National Bethesda, Maryland 20205

Address all correspondence and requests for reprints to: Dr. Lutz Birnbaumer, Department of Cell Biology, Baylor College of Medicine, Texas Medical Center, Houston, Texas 77030.

Abstract

Membrane-bound adenylyl cyclases from ram, dog, and human sperm are unresponsive to fluoride and guanylylimidodiphosphate [GMP-P(NH)P], two agents that stimulate the adenylyl cyclases of somatic cells by an action on the stimulatory guanine nucleotide-binding regulatory (iV8) component of adenylyl cyclase. We have investigated whether this is because the sperm cell catalytic unit is functionally uncoupled from Ns but, nevertheless, capable of interacting with it, or because the sperm cell adenylyl cyclase system is unique and regulated differently from that of somatic cells. Sperm cells were found to be deficient in NB, as evidenced by the inability of detergent extracts from sperm cell membranes and fractions to reconstitute JV.-mediated regulation of the adenylyl cyclase of cyc S49 cells. In addition, attempts to label Ns in sperm cell membranes by [32P]ADP ribosylation with cholera toxin revealed that, if present, N, is less than 1% of that found in human erythrocyte membranes. This, however, was not the only reason for the unresponsiveness of sperm cell adenylyl cyclase, since fluoride stimulation of the sperm cell enzyme could not be induced by reconstituting it with NB purified from human erythrocytes (hRBC). When intact hRBC membranes were added to sperm cell fractions in the presence of fluoride, the activities that resulted were greater than the sum of the individual activities. This apparent reconstitution of fluoride regulation of sperm cell adenylyl cyclase could be blocked by lima bean trypsin inhibitor and appears to have resulted from proteolytic activation of the hRBC adenylyl cyclase by sperm proteases. Sperm cell membranes also appear to lack a functional inhibitory regulatory protein of the adenylyl cyclase system (NO, since they did not contain an ADP-ribosylatable substrate for pertussis toxin action. These results suggest that the sperm cell adenylyl cyclase system is unique and different from that of somatic cells. Sperm cells appear to neither contain NB or N; nor possess the ability of their adenylyl cyclase system to interact with Na from an exogenous source. (Endocrinology 116: 1357-1366,1985)

Footnotes

^* This work was supported in part by Research Grants HD-09581 L.B.), AM-19318 (to L.B.), and GM-29476 (to J.S.T.) from the NIH, a grant from the Andrew W. Mellon Foundation (to J.S.T.), and Center Grants HD-07495 and AM-27685 from the NIH.

Present address: Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.

Supported by NIH Training Grant AM-07348 to Dr. James B. Field.

^* Present address: American Dade, P.O. Box 520672, Miami, Florida 33152. Recipient of NIH Postdoctoral Fellowship HD-05823.

Received August 6, 1984.

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