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-Glutamyl-Transpeptidase in Sperm Maturation



From the * Departments of Human Genetics and
Molecular Medicine and
Cell and Developmental
Biology, Sackler School of Medicine, Tel-Aviv University, Tel Aviv, Israel;
and the
Department of Chemistry and
Biochemistry, University of California, San Diego, La Jolla, California.
| Correspondence to: Dr Nechama S. Kosower, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel (e-mail: nkosower{at}post.tau.ac.il). |
-glutamyl-transpeptidase
(
-GT)-dependent catabolism. Little information is available on the
dynamics of nonprotein thiols (NPSHs) and disulfides (NPSSNPs) in spermatozoa
and epididymal fluid (EF) during sperm passage in the epididymis. It is not
clear whether NPSHs and NPSSNPs are involved in sperm protein thiol (PSH)
oxidation or whether GSH catabolism in the epididymis can serve as a pathway
for sperm PSH oxidation. In the present study, we used the thiol fluorescence
labeling agent monobromobimane to analyze NPSHs and nonprotein disulfides
(NPSSRs) (R, nonprotein or protein) in spermatozoa and EF in the rat caput and
cauda epididymis. NPSH levels are shown to be significantly higher in the
caput than in the cauda (spermatozoa and fluid). GSH in the caput lumen is
subject to high
-GT activity. A marked loss of sperm GSH and a shift to
an oxidized state (resulting in a significantly higher concentration of
glutathione disulfides [GSSRs] than GSH) occur during the passage of
spermatozoa from the caput to the cauda epididymis. Caput EF and extracellular
NPSSNPs induce sperm thiol oxidation. The results suggest that epididymal
NPSH/NPSSNP participates in sperm PSH oxidation and that some reactions of GSH
in the
-GT pathway (in the epididymis) provide oxidizing power, leading
to physiologic sperm thiol oxidation.
Key words: Glutathione/glutathione disulfides, cysteine/cysteine disulfides, nonprotein mixed disulfides, nonprotein-protein mixed disulfides, sperm oxidative pathways
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