Expression and topographical localization of cell surface fucosyltransferase activity during epididymal sperm maturation in the mouse.
We have demonstrated previously that spermatogenic cells in the mouse testis have high levels of fucosyltransferase activity. Furthermore, a significant portion of this activity has been localized to the cell surface (Millette et al.: Cell Biology of the Testis and Epididymis, 1987). Differential expression of fucosyltransferases and their function as ecto-enzymes may be important in the processes of sperm maturation and fertilization in mammals. Accordingly, here we report the activity levels of fucosyltransferase (FT) in spermatozoa isolated from the mouse caput and cauda epididymides. Calculated on a per cell basis, spermatozoa from the caput epididymis have significantly more FT activity than do spermatozoa from the cauda epididymis (18.07 +/- 2.2 pmol/million cells compared with 2.8 +/- 0.09 pmol/million cells). Furthermore, caput sperm exhibit a more significant increase in FT activity when assayed in the presence of Nonidet P-40. Calculated on the basis of cell surface area, however, FT activity remains constant on the head portion of spermatozoa isolated from all portions of the male reproductive tract and from capacitated spermatozoa. Measurements of FT activity in extracts of isolated sperm tails from cells at different stages of maturation indicate a greatly diminished activity in tails from sperm in the cauda epididymis. The total sperm surface area is composed predominantly of the plasma membrane surrounding the flagellar apparatus. Therefore, our data demonstrate that FT activity is retained selectively on the different topological regions of sperm, with losses during sperm maturation in the epididymis being restricted to the tail segment. Maintenance of high levels of FT activity of the plasma membranes of the mouse sperm head raise the possibility that FT is indeed involved in some aspects of sperm-egg recognition.
Ram
P A
PA
Department of Anatomy & Cellular Biology, Harvard Medical School, Boston, Massachusetts 02115.
Cardullo
R A
RA
Millette
C F
CF
D000818:Animals; D002462:Cell Membrane / Q000032:analysis / Q000201:enzymology; D004822:Epididymis; D005647:Fucosyltransferases / Q000378:metabolism*; D006602:Hexosyltransferases / Q000378:metabolism*; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D051379:Mice; D008815:Mice, Inbred Strains; D008854:Microscopy, Electron; D013079:Sperm Maturation; D013091:Spermatogenesis; D013094:Spermatozoa / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure
D008565:Membrane Proteins; D005647:Fucosyltransferases; D006602:Hexosyltransferases