Biol Reprod Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by WELLS, J. N.
Right arrow Articles by GARBERS, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by WELLS, J. N.
Right arrow Articles by GARBERS, D. L.
Agricola
Right arrow Articles by WELLS, J. N.
Right arrow Articles by GARBERS, D. L.

Biology of Reproduction, Vol 15, 46-53, Copyright © 1976 by Society for the Study of Reproduction

Nucleoside 3',5'-Monophosphate Phosphodiesterases in Sea Urchin Sperm

JACK N. WELLS 1, and DAVID L. GARBERS 1

1 Department of Physiology, Vanderbilt University Medical School, Nashville, Tennessee 37232


In sea urchin sperm, the hydrolysis of adenosine 3',5'-monophosphate (cyclic AMP) appears to be predominantly catalyzed by a protein different from that which catalyzes the hydrolysis of guanosine 3',5'-monophosphate (cyclic GMP). The cyclic GMP phosphodiesterase is located primarily in the particulate fraction, whereas the cyclic AMP phosphodiesterase is found mainly in the soluble fraction of the sperm cell homogenate. The cyclic AMP and cyclic GMP phosphodiesterases are inactivated at different rates by N-ethylmaleimide and are inhibited to different degrees by various phosphodiesterase inhibitors. Three fractions (A, B, C) of cyclic nucleotide phosphodiesterase activity (as measured at 1 µM substrate) can be separated by DEAE-cellulose chromatography of the supernatant fraction. The bulk of the recovered cyclic AMP phosphodiesterase activity is found in fraction C while most of the recovered cyclic GMP phosphodiesterase activity is contained in fraction B.

With either cyclic nucleotide as substrate, Mn2+ is a more effective activator of the sperm homogenate phosphodiesterase activity at low concentrations (10-6 to 10-4M) than is Mg2+, but these metals are equally effective at 10-3M. Kinetic behavior of the phosphodiesterase activities in particulate and supernatant fractions are anomalous with either cyclic AMP or cyclic GMP as the substrate.

A heat stable, nondialyzable material that is capable of increasing the activity of partially purified (activator-deficient) coronary artery phosphodiesterase can be isolated by DEAE-cellulose chromatography of the supernatant fraction of a sperm homogenate. This material, however, does not affect the rates of hydrolysis of either cyclic AMP or cyclic GMP by fractions A, B, or C obtained by DEAE-cellulose chromatography of sperm supernatant fractions.

Note:
ACKNOWLEDGMENTS The authors wish to thank Dr. Joel G. Hardman for his advice during the course of these experiments and Y. J. Wu and Janice L. Suddath for expert technical assistance.

Submitted on January 7, 1976
Accepted on March 12, 1976




This article has been cited by other articles:


Home page
 J AndrolHome page
J. Glogowski, D. R. Danforth, and A. Ciereszko
Inhibition of Alkaline Phosphatase Activity of Boar Semen by Pentoxifylline, Caffeine, and Theophylline
J Androl, November 1, 2002; 23(6): 783 - 792.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
L. Lefievre, E. de Lamirande, and C. Gagnon
Presence of Cyclic Nucleotide Phosphodiesterases PDE1A, Existing as a Stable Complex with Calmodulin, and PDE3A in Human Spermatozoa
Biol Reprod, August 1, 2002; 67(2): 423 - 430.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1976 by the Society for the Study of Reproduction.