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Retention of hamster oolemma fusibility with spermatozoa after various enzyme treatments: a search for the molecules involved in sperm-egg fusion

Published online by Cambridge University Press:  26 September 2008

Ruben H. Ponce ,
Ryuzo Yanagimachi ,
Umbert A Urch ,
Tatsuya Yamagata  and
Makoto lto
Ruben H. Ponce
Affiliation:
University of Hawaii School of Medicine and University of California, USA, and Mitsubishi KaseiInsitutie of Life Sciences, Tokyo, Japan.
Ryuzo Yanagimachi*
Affiliation:
University of Hawaii School of Medicine and University of California, USA, and Mitsubishi KaseiInsitutie of Life Sciences, Tokyo, Japan.
Umbert A Urch
Affiliation:
University of Hawaii School of Medicine and University of California, USA, and Mitsubishi KaseiInsitutie of Life Sciences, Tokyo, Japan.
Tatsuya Yamagata
Affiliation:
University of Hawaii School of Medicine and University of California, USA, and Mitsubishi KaseiInsitutie of Life Sciences, Tokyo, Japan.
Makoto lto
Affiliation:
University of Hawaii School of Medicine and University of California, USA, and Mitsubishi KaseiInsitutie of Life Sciences, Tokyo, Japan.
*
R. Yanagimachi, Department of Anatomy and Reproductive Biology, University of Haxaii School of Medicine, Honolulu, Hawaii 96822, USA.
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Summary

The plasma membrane (oolemma) of the hamster egg retains the ability to fuse with spermatozoa even after exhaustive treatment with proteases and glycosidases. In contrast, when mouse oolemma is treated with proteases, the ability of eggs to fuse with spermatozoa is reduced. In the present study, similar treatments effective in reducing fusibility in the mouse were reexamined in the hamster. Of the several enzymes and treatments tested, only trypsin in Ca2+-free medium significantly reduced the hamster oolemma's ability to fuse with spermatozoa. This is suggestive of a cadherin-like system of binding and fusion. When hamster oolemmae were treated with the same protease regimen that reduced fusibility of mouse oolemma for mouse spermatozoa, heterologous fusion of hamster oolemmae with mouse spermatozoa was reduced, without affecting the fusion of these oolemmae with hamster spermatozoa. These data suggest that a protease-sensitive oolemma molecule is of critical importance for mouse sperm-oolemma fusion but not for hamster sperm-oolemma fusion.

Keywords

EggFusionHamsterMouseSperm
Type
Article
Information
Zygote , Volume 1 , Issue 2 , May 1993 , pp. 163 - 171
Copyright
Copyright © Cambridge University Press 1993

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