| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Regular Article |
in Bovine Sperm Motility Regulation1
a Department of Biological Sciences, Kent State University, Kent, Ohio 44240
b State University of California, Long Beach, California 90840
c Veterans Affairs Medical Center, Oregon Health Sciences University, Portland, Oregon 97201
ABSTRACT
The long-term goal of our work is to understand biochemical mechanisms underlying sperm motility and fertility. In a recent study we showed that tyrosine phosphorylation of a 55-kDa protein varied in direct proportion to motility. Tyrosine phosphorylation of the protein was low in immotile compared to motile epididymal sperm. Inhibition or stimulation of motility by high calcium levels or cAMP, respectively, results in a corresponding decrease or increase in tyrosine phosphorylation of the 55-kDa protein. Here we report purification and identification of this motility-associated protein. Soluble extracts from bovine caudal epididymal sperm were subjected to DEAE-cellulose, Affi-Gel blue, and cellulose phosphate chromatography. Tyrosine phosphate immunoreactive fractions contained glycogen synthase kinase-3 (GSK-3) activity, suggesting a possible correspondence between these proteins. This suggestion was verified by Western blot analyses following one-dimensional and two-dimensional gel electrophoresis of the purified protein using monoclonal and affinity-purified polyclonal antibodies against the catalytic amino-terminus and carboxy-terminus regions of GSK-3. Further confirmation of the identity of these proteins came from Western blot analysis using antibodies specific to the tyrosine phosphorylated GSK-3. Using this antibody, we also showed that GSK-3 tyrosine phosphorylation was high in motile compared to immotile sperm. Immunocytochemistry revealed that GSK-3 is present in the flagellum and the anterior portion of the sperm head. These data suggest that GSK-3, regulated by phosphorylation, could be a key element underlying motility initiation in the epididymis and regulation of mature sperm function.
First decision: 16 August 1999.
1 This research was supported by funds from Kent State University and NIH Grants HD36408.
2 Correspondence. FAX: 330 672 3713; svijayar{at}kent.edu
This article has been cited by other articles:
|
|
 |
|
  P. Puri, K. Myers, D. Kline, and S. Vijayaraghavan Proteomic Analysis of Bovine Sperm YWHA Binding Partners Identify Proteins Involved in Signaling and Metabolism Biol Reprod, December 1, 2008; 79(6): 1183 - 1191. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I M Aparicio, M J Bragado, M C Gil, M Garcia-Herreros, L Gonzalez-Fernandez, J A Tapia, and L J Garcia-Marin Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3{alpha} Reproduction, September 1, 2007; 134(3): 435 - 444. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I M Aparicio, M C Gil, M Garcia-Herreros, F J Pena, and L J Garcia-Marin Inhibition of phosphatidylinositol 3-kinase modifies boar sperm motion parameters Reproduction, March 1, 2005; 129(3): 283 - 289. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Huang, P. R. Somanath, R. Chakrabarti, E. M. Eddy, and S. Vijayaraghavan Changes in Intracellular Distribution and Activity of Protein Phosphatase PP1{gamma}2 and Its Regulating Proteins in Spermatozoa Lacking AKAP4 Biol Reprod, February 1, 2005; 72(2): 384 - 392. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. R. Somanath, S. L. Jack, and S. Vijayaraghavan Changes in Sperm Glycogen Synthase Kinase-3 Serine Phosphorylation and Activity Accompany Motility Initiation and Stimulation J Androl, July 1, 2004; 25(4): 605 - 617. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Willipinski-Stapelfeldt, J. Lubberstedt, S. Stelter, K. Vogt, A. K. Mukhopadhyay, and D. Muller Comparative analysis between cyclic GMP and cyclic AMP signalling in human sperm Mol. Hum. Reprod., July 1, 2004; 10(7): 543 - 552. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. M. Turner Tales From the Tail: What Do We Really Know About Sperm Motility? J Androl, November 1, 2003; 24(6): 790 - 803. [Full Text] [PDF]
|
|
|
|
|
|
Z. Huang, B. Khatra, M. Bollen, D. W. Carr, and S. Vijayaraghavan Sperm PP1{gamma}2 Is Regulated by a Homologue of the Yeast Protein Phosphatase Binding Protein sds221 Biol Reprod, December 1, 2002; 67(6): 1936 - 1942. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Vernet, N. Fulton, C. Wallace, and R. J. Aitken Analysis of Reactive Oxygen Species Generating Systems in Rat Epididymal Spermatozoa Biol Reprod, October 1, 2001; 65(4): 1102 - 1113. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Luconi, F. Marra, L. Gandini, E. Filimberti, A. Lenzi, G. Forti, and E. Baldi Phosphatidylinositol 3-kinase inhibition enhances human sperm motility Hum. Reprod., September 1, 2001; 16(9): 1931 - 1937. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
