Zygote
- Zygote / Volume 1 / Issue 02 / May 1993, pp 163-171
- Copyright © Cambridge University Press 1993
- DOI: http://dx.doi.org/10.1017/S0967199400001428 (About DOI), Published online: 26 September 2008
Article
Retention of hamster oolemma fusibility with spermatozoa after various enzyme treatments: a search for the molecules involved in sperm-egg fusion
Ruben H. Poncea11, Ryuzo Yanagimachia1 c11, Umbert A Urcha12, Tatsuya Yamagataa13 and Makoto ltoa13
a1 University of Hawaii School of Medicine and University of California, USA, and Mitsubishi Kasei Insitutie of Life Sciences, Tokyo, Japan.
Abstract
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.
Correspondence:
c1 R. Yanagimachi, Department of Anatomy and Reproductive Biology, University of Haxaii School of Medicine, Honolulu, Hawaii 96822, USA.
Footnotes
1 Department of Anatomy and Reproductive Biology, University of Hawaii School of Medicine, Honolulu, Hawaii, USA.
2 Department of Biochemistry and Biophysics, University of California, Davis, CA 95616, USA.
3 Laboratory of Glycoconjugate Research, Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo, Japan.
