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A unique expression pattern for a sperm membrane protein during sea urchin spermatogenesis

Published online by Cambridge University Press:  26 September 2008

Rita D. Ward ,
Lisa M. Mendoza ,
Gary W. Moy ,
Victor D. Vacquier  and
David Nishioka
Rita D. Ward
Affiliation:
Department of Biology, Georgetown University, Washington, DC and Scripps Institution of Oceanography, La Jolla, California, USA
Lisa M. Mendoza
Affiliation:
Department of Biology, Georgetown University, Washington, DC and Scripps Institution of Oceanography, La Jolla, California, USA
Gary W. Moy
Affiliation:
Department of Biology, Georgetown University, Washington, DC and Scripps Institution of Oceanography, La Jolla, California, USA
Victor D. Vacquier
Affiliation:
Department of Biology, Georgetown University, Washington, DC and Scripps Institution of Oceanography, La Jolla, California, USA
David Nishioka*
Affiliation:
Department of Biology, Georgetown University, Washington, DC and Scripps Institution of Oceanography, La Jolla, California, USA
*
Dr David Nishioka, Department of Biology, Georgetown University, Washington, DC 20057-1028, USA. Tel: 202/687-5888. Fax: 202/687-5662.
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Summary

Specific mRNAs coding for a 63 kDa sperm membrane protein (63-SMP) were localised in Strongylocentrotus purpuratus testis sections using in situ hybridisation techniques. 35S-labelled antisense RNA probes transcribed from a 766 base pair fragment of the gene coding for the 63-SMP hybridised to all spermatogenic cells in the basal germinal epithelia of testicular acini, except the most peripherally located (least differentiated) spermatogonia. No hybridisation to the luminally located mature spermatozoa or somatic cells of the testis was observed. Using monoclonal antibody J17/30 and indirect immunofluorescence techniques, the 63-SMP was localised to the same subset of spermatogenic cells that contain the 63-SMP mRNA, suggesting that expression of this gene is transcriptionally controlled. In combination with previous studies on the expression of sperm histones and sperm bindin, these results show that multiple, perhaps sequential, classes of gene activity contribute to the differentiation of sea urchin sperm.

Keywords

Gene expressionIn situ hybridisationSea urchinSpermatogenesisSperm proteins
Type
Article
Information
Zygote , Volume 2 , Issue 2 , May 1994 , pp. 159 - 165
Copyright
Copyright © Cambridge University Press 1994

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References

Belvé, A.R. & ÓBrien, D.A. (1983). The mammalian spermatozoon: structure and temporal assembly. In: Mechanisms and Control of Animal Fertilization, ed. J.E., Hartman, pp. 55–137. New York: Academic Press.Google Scholar
Cameron, R.A., Minor, J.E., Nishioka, D., Britten, R.J. & Davidson, E.H. (1990). Locale and level of bindin mRNA in maturing testis of the sea urchin, Strongylocentrotus purpuratus. Dev. Biol. 142, 44–9.CrossRefGoogle ScholarPubMed
Cox, K.H., DeLeon, D.V., Angerer, L.M. & Angerer, R.C. (1984). Detection of mRNAs in sea urchin embryos by in situ hybridization using asymmetric RNA probes. Dev. Biol. 101, 485–502.CrossRefGoogle ScholarPubMed
Harvey, E.B. (1956). The American Arbacia and Other Sea Urchins. Princeton: Princeton University Press.CrossRefGoogle Scholar
Holland, N. & Giese, A. (1965). An autoradiographic investigation of the gonads of the purple sea urchin, Strongylocentrotus purpuratus. Biol. Bull. 128, 241–58.CrossRefGoogle Scholar
Longo, F.J. & Anderson, E. (1969). Sperm differentiation in the sea urchins Arbacia punctulata and Strongylocentrotus purpuratus. J. Ultrastruct.Res. 27, 486–98.CrossRefGoogle ScholarPubMed
Mallory, F.B. (1944). Pathological Technique. Philadelphia: W.B. Saunders.Google Scholar
Mendoza, L.M. (1993). Primary structure of two sea urchin sperm membrane proteins implicated in induction of the acrosome reaction. PhD dissertation, University of California, San Diego.Google Scholar
Mendoza, L.M., Nishioka, D. & Vacquier, V.D. (1993). A GPI-anchored sea urchin sperm membrane protein containing EGF domains is related to human uromodulin. J. Cell Biol. 121, 1291–7.CrossRefGoogle ScholarPubMed
Nishioka, D., Trimmer, J.S., Poccia, D. & Vacquier, V.D. (1987). Changing localizations of site-specific surface antigens during sea urchin spermiogenesis. Exp. Cell Res. 173, 606–16.CrossRefGoogle ScholarPubMed
Nishioka, D., Ward, R.D., Poccia, D., Kostacos, C. & Minor, J.E. (1990). Localization of bindin expression during sea urchin spermatogenesis. Mol. Reprod. Dev. 27, 181–90;CrossRefGoogle ScholarPubMed
Osborn, M. & Weber, K. (1982). Immunofluorescence and immunocytochemical procedures with affinity purified antibodies: Tubulin-containing structures. In: Methods in Cell Biology, 24, ed. Wilson, L., pp. 97–132. New York: Academic Press.Google Scholar
Poccia, D., Lieber, T. & Childs, G. (1989). Histone gene expression during sea urchin spermatogenesis: an in situ hybridization study. Mol. Reprod. Dev. 1, 219–29.CrossRefGoogle ScholarPubMed
Podell, S.B., Moy, G.W. & Vacquier, V.D. (1984). Isolation and characterization of a plasma membrane fraction from sea urchin sperm exhibiting species specific recognition of the egg surface. Biochim. Biophys. Acta. 778, 25–37.CrossRefGoogle ScholarPubMed
Sambrook, J., Fritsch, E.F. & Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.Google Scholar
Trimmer, J.S., Trowbridge, I.S. & Vacquier, V.D. (1985). Monoclonal antibody to a membrane glycoprotein inhibits the acrosome reaction and associated Ca2+ and H+ fluxes of sea urchin sperm. Cell 40, 697–703.CrossRefGoogle Scholar
Trimmer, J.S., Schackmann, R.W. & Vacquier, V.D. (1986). Monoclonal antibodies increase intracellular Ca2+ in sea urchin spermatozoa. Proc. Natl. Acad. Sci. USA 83, 9055–9.CrossRefGoogle ScholarPubMed
Trimmer, J.S., Ebina, Y., Schackmann, R.W., Meinhof, C.-G. & Vacquier, V.D. (1987). Characterization of a monoclonal antibody that induces the acrosome reaction of sea urchin sperm. J. Cell Biol. 105, 1121–8.CrossRefGoogle ScholarPubMed
Ward, R.D. & Nishioka, D. (1993). Seasonal changes in testicular structure and localization of a sperm surface glycoprotein during spermatogenesis in sea urchins. J. Histochem. Cytochem. 41, 423–31.CrossRefGoogle ScholarPubMed
Wilson, L.P. (1940). Histology of the gonad wall of Arbacia punctulata. J. Morphol. 66, 463–79.CrossRefGoogle Scholar