Changes in the plasma membrane proteins of stallion spermatozoa during maturation in the epididymis.
The present paper reports modifications in the electrophoretic and cytochemical characteristics of mature and immature stallion spermatozoa. Some sperm surface glycoproteins (36, 32, 29, 21, 20, 18 kDa) detected in cauda epididymidis spermatozoa, were either absent or present in a very low relative concentration in immature sperm cells. A major 14 kDa protein band, observed in sperm extracts obtained from ductus efferentes, progressively decreased along the epididymal ductus. The nature and distribution of carbohydrate residues on the sperm membrane, during epididymal maturation, was also studied by use of lectin probes. Some protein bands bound concanavalin A while others, as the 36, 32 and 20 kDa proteins, exhibited higher affinity for WGA lectin. The distribution and relative density of mannose-, galactose-, N-acetylglucosamine-, N-acetylgalactosamine-, fucose- and sialic acid-containing macromolecules showed a characteristic pattern depending on the sperm membrane domain and on its origin. Some sperm surface domains displayed affinity for more than one lectin, indicating a diversity in their exposed carbohydrate residues, whereas others bound only one or no lectin. The passage of spermatozoa through the epididymidis was accompanied by changes in the accessibility or abundance of lectin ligands. Some lectins (UEA, WGA, LPA) gave stronger reaction in mature spermatozoa, while others (RCA, WFH, PNA) stained better immature spermatozoa. This remodeling of sperm surface molecules is probably a consequence of interactions between spermatozoa and the epididymal secretions, and may reflect addition or adsorption of new molecules, space configurations changes or biochemical modifications of pre-existing compounds. Our results suggest that the distribution and density of terminal oligosaccharidic residues on the sperm plasma membrane have species-specific characteristics. These post testicular developmental changes may be of significance in the overall understanding of the stallion fertility.
Retamal
C
C
Faculty of Medicine, University of Chile, Santiago.
Urzúa
J
J
Lorca
C
C
López
M L
ML
Alves
E W
EW
D000818:Animals; D002454:Cell Differentiation; D004822:Epididymis / Q000166:cytology / Q000378:metabolism; D006736:Horses; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D013091:Spermatogenesis; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism*
D008565:Membrane Proteins