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From the Department of Biological Sciences, Kent State University, Kent, Ohio.
| Correspondence to: Dr Srinivasan Vijayaraghavan, Department of Biological Sciences, Kent State University, Kent, OH 44242 (e-mail: svijayar{at}kent.edu). |
(GSK-3), is
present in spermatozoa. In somatic cells, GSK-3 is regulated by serine and
tyrosine phosphorylation. In this report, we document that both GSK-3
and GSK-ß isoforms are present in spermatozoa, with GSK-3 being
the predominant isoform. The relationship between GSK-3 serine phosphorylation
and motility was investigated. Serine phosphorylation of GSK-3 increases
significantly in spermatozoa during their passage through the epididymis.
Initiation and stimulation of motility in vitro by isobutyl-methyl-xanthine,
2-chloro-2'-deoxy-adenosine, and calyculin A lead to a dramatic increase
in GSK-3 serine phosphorylation. The concentration-dependent induction of
motility by calyculin A is closely associated with GSK-3 serine
phosphorylation. Immunoprecipitation of GSK-3 and GSK-3ß shows
that both of the GSK-3 isoforms are more active in caput than in caudal
spermatozoa. Calyculin A treatment decreased the activity of both isoforms.
Column chromatography was used to purify inactive GSK-3 from the caudal
sperm extracts. This GSK-3 species was phosphorylated at amino acid
residues serine 21 and tyrosine 214. Inactive GSK-3 is present in
caudal but not in caput epididymal spermatozoa. The enzymes protein kinase B
(PKB; also known as cAkt) and phosphoinositide 3-kinase (PI3-kinase), the
upstream signaling proteins involved in GSK-3 phosphorylation, are both
present in spermatozoa. Fluorescence immunocytochemistry showed that GSK-3 is
present in the head and tail regions of sperm. Our work suggests a novel role
for the signaling system involving GSK-3 in the regulation of sperm
motility.
Key words: Epididymis, protein kinase B, phosphoinositide 3-kinase
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