Rearrangement of sperm surface antigens prior to fertilization.
During spermiogenesis and epididymal transit, proteins on the sperm surface become localized to specific domains. In at least one case (PH-20), the protein is initially inserted throughout the membrane and subsequently becomes restricted to a domain by some mechanism that has not yet been determined. Other proteins could become localized through localized insertion. The sperm surface is a dynamic structure that is altered even after the spermatozoon leaves the male. In the female reproductive tract the spermatozoa undergo capacitation and the acrosome reaction that enables them to fertilize the egg. Both of these processes are accompanied by alterations in protein localization: the PT-1 protein migrates during capacitation, and the PH-20 protein migrates after the acrosome reaction. In addition, an upregulation of the surface expression of PH-20 occurs during the acrosome reaction. This additional PH-20 is incorporated into the plasma membrane by the irreversible fusion of the acrosomal membrane with the plasma membrane. The acrosomal membrane contains PH-20 protein that has been stored there since the formation of the acrosome at the spermatid stage of spermiogenesis. Proteins that are freely diffusing must be maintained in a domain by a mechanism that does not involve immobilization or slowing of protein diffusion. We have suggested that barriers to membrane protein diffusion exist at the equatorial region, the posterior ring, and the annulus and that they are responsible for maintaining a localized distribution of at least some of the surface proteins. The migration of surface proteins could result from an alteration of these barriers, a change in the protein structure so that it can pass through the barrier, or active transport across the barrier. These observed changes in surface expression (localization and the level of expression) may be acting to control surface function post-testicularly.
Myles
D G
DG
Department of Physiology and Biochemistry, University of Connecticut Health Center, Farmington 06032.
Koppel
D E
DE
Cowan
A E
AE
Phelps
B M
BM
Primakoff
P
P
D000177:Acrosome / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000954:Antigens, Surface / Q000502:physiology*; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D004058:Diffusion; D004822:Epididymis / Q000502:physiology; D008297:Male; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000502:physiology*; D013075:Sperm Capacitation; D013094:Spermatozoa / Q000276:immunology / Q000648:ultrastructure*
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D008565:Membrane Proteins