Electrophoretic characterization of the human sperm-specific enolase at different stages of maturation.
The presence of a sperm-specific enolase isoform (ENO-S) in human ejaculated spermatozoa was previously demonstrated. The objective of this study was to characterize this ENO-S in spermatozoa at different steps of maturation. Sperm ENO-S was characterized in testicular, epididymal, and ejaculated spermatozoa to determine whether any change occurred in the isoform patterns of this enzyme during epididymal maturation. In testicular sperm, ENO-S was present under 2 main bands named S1 and S3. In epididymal sperm, S1 and S3 bands and a prominent additional S2 band, with the same electrophoretic properties as the S isoform of ejaculated sperm, were visualized. In the testicular extracts obtained from testes in which no spermatozoa were visualized by histologic analysis, none of the 3 ENO-S bands was found. ENO-S exists as different isoforms (electrophoretic variants) in the different stages of sperm maturation. Passage through the epididymis seems to play a major role in the maturational process of this sperm-specific enolase.
Service de Biologie du Développement et de la Reproduction, CHU Hôtel-Dieu, Boulevard Léon Malfreyt, 63003 Clermont-Ferrand, France. andre.force@wanadoo.fr
Andre
A
Force
Jean-Louis
JL
Viallard
Fabrice
F
Saez
Genevieve
G
Grizard
Daniel
D
Boucher
D015415:Biomarkers / Q000032:analysis; D004586:Electrophoresis; D004822:Epididymis / Q000166:cytology / Q000201:enzymology; D006801:Humans; D008297:Male; D010751:Phosphopyruvate Hydratase / Q000032:analysis / Q000378:metabolism*; D020033:Protein Isoforms / Q000032:analysis / Q000378:metabolism*; D013079:Sperm Maturation / Q000502:physiology*; D013094:Spermatozoa / Q000166:cytology* / Q000201:enzymology*; D013737:Testis / Q000166:cytology / Q000201:enzymology
D015415:Biomarkers; D020033:Protein Isoforms; D010751:Phosphopyruvate Hydratase