The histochemical localization of acrosin in guinea-pig sperm after the acrosome reaction.
The protease acrosin is widely considered to be an essential component of a zona lysin which enables sperm to penetrate the zona pellucida of the egg. Sperm form a characteristic penetration slit little wider than the sperm head itself and this has long suggested that any zona lysin is attached to the sperm surface after an acrosome reaction. This paper provides the first ultrastructural evidence that this is the case. The protein acrosin inhibitor, Kunitz soybean trypsin inhibitor, has been covalently attached to the electron-dense marker, ferritin, and the conjugate incubated with guinea-pig sperm which have undergone an A23187-induced acrosome reaction. Electron microscopy shows that ferritin is distributed unevenly over the outer surface of the newly exposed inner acrosomal membrane but does not extend to the equatorial segment. This is further evidence that acrosin can be considered as a candidate for the role of zona lysin. The mechanism of sperm penetration of the zona is discussed in the light of these observations.
D000176:Acrosin / Q000032:analysis*; D000177:Acrosome / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D000818:Animals; D000001:Calcimycin / Q000494:pharmacology; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure; D010450:Endopeptidases / Q000032:analysis*; D006168:Guinea Pigs; D006651:Histocytochemistry; D008297:Male; D008854:Microscopy, Electron; D013094:Spermatozoa / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology* / Q000648:ultrastructure
D000001:Calcimycin; D010450:Endopeptidases; D000176:Acrosin