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Lipid raft on gametic cells as a functional domain for sperm–egg interaction coupled with signal transduction

Published online by Cambridge University Press:  16 July 2018

Kaoru Ohta ,
Chihiro Sato ,
Tsukasa Matsuda ,
Masaru Toriyama ,
Victor D. Vacquier ,
Noritaka Hirohashi ,
William J. Lennarz  and
Ken Kitajima
Kaoru Ohta
Affiliation:
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Chihiro Sato
Affiliation:
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Tsukasa Matsuda
Affiliation:
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Masaru Toriyama
Affiliation:
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Ohya, Shizuoka 422-8529, Japan
Victor D. Vacquier
Affiliation:
Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093-0202, USA
Noritaka Hirohashi
Affiliation:
Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, NY 11794-5215, USA
William J. Lennarz
Affiliation:
Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, NY 11794-5215, USA
Ken Kitajima
Affiliation:
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
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Extract

It has been shown that lipid raft, a microdomain of plasma membrane, is a hot spot of signal transduction in somatic cells, because it contains several transducer proteins as well as various receptor molecules. The lipid raft is characterised by its low-density detergent-insoluble nature and by enrichment of glycosphingolipids (GSLs). We hypothesised that lipid raft was also on the gamete surface, and might function as a sperm–egg adhesion site as well as in signal transduction during fertilisation. To test this hypothesis, we have initiated studies using sea urchin gametes. Recently we have demonstrated the presence of the lipid raft in sperm of three sea urchin species as the first example in gametic cells (Ohta et al., 1999). Here we show several lines of evidence for the functional importance of the lipid raft in sperm–egg interaction as well as in subsequent signal transduction.

In sea urchin sperm, lipid rafts were able to be prepared as a low-density detergent-insoluble membrane (LD-DIM) fraction and were rich in GSLs including gangliosides and sulphatide, containing more than 50% of the total amount of GSL present in sperm. On the other hand, cholesterol and sphingomyelin were not so enriched, which contrasted with the LD-DIM from MDCK cells, where these lipids were reported to be abundant (Brown & Rose, 1992).

Type
Special Lecture for Citizens
Information
Zygote , Volume 8 , supplement S1: Proceedings of the International Symposium on Fertilization and Development of Sea Urchin and Marine Invertebrates , December 1999 , pp. S63
Copyright
Copyright © Cambridge University Press 1999

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References

Bookbinder, L.H., et al. (1990). J. Cell Biol. 111, 1859–66.CrossRefGoogle Scholar
Brown, D.A. & Rose, J.K. (1992). Cell 68, 533–44.CrossRefGoogle ScholarPubMed
Dangott, L.J., et al. (1984). J. Biol. Chem. 259, 13712–16.CrossRefGoogle Scholar
Garbers, D.L., et al. (1980). Biol. Reprod. 22, 526–32.CrossRefGoogle Scholar
Garbers, D.L. & Lowe, D.G. (1994). J. Biol. Chem. 269, 30741–4.CrossRefGoogle Scholar
Mata, P.C., et al. (1995). Dev. Growth Differ. 37, 173–81.CrossRefGoogle Scholar
Mendoza, L.M., et al. (1993). J. Cell Biol. 121, 1291–7.CrossRefGoogle Scholar
Ohlendieck, K., et al. (1993). J. Cell Biol. 122, 887–95.CrossRefGoogle Scholar
Ohta, K., et al. (1999). Biochem. Biophys. Res. Commun. 258, 616–23.CrossRefGoogle Scholar
Stears, R.L. & Lennarz, W.J. (1997). Dev. Biol. 187, 200–8.CrossRefGoogle Scholar
Vacquier, V.D. & Moy, G.W. (1997). Dev. Biol. 192, 125–35.CrossRefGoogle Scholar