Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-13T07:24:00.722Z Has data issue: false hasContentIssue false
  • English
  • Français

Non-plasmalemmal localisation of the major ganglioside in sea urchin eggs

Published online by Cambridge University Press:  26 September 2008

Hidehiko Shogomori ,
Kazuyoshi Chiba ,
Hideo Kubo  and
Motonori Hoshi
Hidehiko Shogomori
Affiliation:
Tokyo Institute of Technology, Yokohama and Tokyo Metropolitian Insitute of Medical Science, Tokyo, Japan
Kazuyoshi Chiba
Affiliation:
Tokyo Institute of Technology, Yokohama and Tokyo Metropolitian Insitute of Medical Science, Tokyo, Japan
Hideo Kubo
Affiliation:
Tokyo Institute of Technology, Yokohama and Tokyo Metropolitian Insitute of Medical Science, Tokyo, Japan
Motonori Hoshi*
Affiliation:
Tokyo Institute of Technology, Yokohama and Tokyo Metropolitian Insitute of Medical Science, Tokyo, Japan
*
Motonori Hoshi, Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Midoriku, Yokohama 227, Japan. Fax: 81-45-923-0368.
Get access Rights & Permissions [Opens in a new window]

Summary

M5 ganglioside (NeuGcα2–6Glcβl-' Cer) is the predominant glycosphingolipid in sea urchin eggs. Distribution of M5 ganglioside was studied in unfertilised and fertilised eggs of the sea urchin Hemicentrotus pulcherrimus by indirect immunofluorescence microscopy. In the cortices of unfertilised eggs, anti-M5 antibody strongly stained the submembranous, polygonal and tubular network of endoplasmic reticulum that was revealed by a membrane-staining dye, DiIC18(3). In addition to the cortical network of endoplasmic reticulum, at least two morphologically distinct vesicles were positive to the antibody. In the cortices isolated from fertilised eggs 30 min after insemination, the antibody stained only a similar network of endoplasmic reticulum, presumably the one reconstructed 5–10 min after fertilisation. During mitosis the endoplasmic reticulum is known to aggregate within the asters of the mitotic apparatus. Indeed, the antibody stained the asters and (more strongly) the vesicular components attaching to the periphery of the mitotic apparatus.

Keywords

Anti-ganglioside antibodyEndoplasmic reticulumGangliosideMitotic apparatusSeaurchin egg
Type
Review Article
Information
Zygote , Volume 1 , Issue 3 , August 1993 , pp. 215 - 223
Copyright
Copyright © Cambridge University Press 1993

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Allemand, D., DeRenzis, G., Girard, J.P. (1987). Activation of amino acid uptake at fertilization in the sea urchin egg. Exp. Cell Res. 169, 169–77.CrossRefGoogle ScholarPubMed
Christen, R. (1983). Acidic vesicles and the uptake of amines by sea urchin eggs. Exp. Cell Res. 143, 319–25.CrossRefGoogle ScholarPubMed
Fenderson, B.A., Eddy, E.M. & Hakomori, S. (1990). Glycoconjugate expression during embryogenesis and its biological significance. Bio Essays 12, 173–9.Google ScholarPubMed
Gillard, B.K., Heath, J.P., Thurmon, L.T. & Marcus, D.M. (1991). Association of glycosphingolipids with intermediate filaments of human umbilical vein endothelial cells. Exp. Cell Res. 192, 433–44.CrossRefGoogle ScholarPubMed
Gillard, B.K., Thurmon, L.T. & Marcus, D.M. (1992). Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, glial, and muscle cells. Cell Motil. Cytoskeleton 21,255–71.CrossRefGoogle ScholarPubMed
Gillard, B.K., Thumon, L.T. & Marcus, D.M. (1993). Variable subcellular localization of glycosphingolipids. Glycobiolgy 3, 57–67.CrossRefGoogle ScholarPubMed
Hakomori, S. (1981). Glycosphingolipids in cellular interaction, differentiation, and oncogenesis. Annu. Rev. Biochem. 50, 733–64.CrossRefGoogle ScholarPubMed
Henson, J.H. & Begg, D.A. (1988). Filamentous actin organization in the unfertilized sea urchin egg cortex. Dev. Biol. 127, 388–48.CrossRefGoogle ScholarPubMed
Henson, J.H., Begg, D.A., Beaulieu, S.M., Fishkind, D.J., Bonder, E.M., Terasaki, M., Lebeche, D. & Kamminer, B. (1989), A calsequestrin-like protein in the endoplasmic reticulum of the sea urchin: localization and dynamics in the eggs and first cell cycle embryo. J. Cell Biol. 109, 149–61.CrossRefGoogle ScholarPubMed
Higashi, H. & Yamgata, T. (1992). Mechanism for ganglioside mediated modulation of a calmodulin-dependent enzyme. J. Biol. chem. 267, 9839–43.CrossRefGoogle ScholarPubMed
Higashi, H., Omori, A. & Yamagata, T. (1992). Calmodulin, a ganglioside-binding protein. J. Biol. chem. 267. 9831–8.CrossRefGoogle ScholarPubMed
Hoshi, M. & Nagai, Y. (1970).Biochemistry of mucolipids of sea urchin gametes and embryos. III. Mucolipids during early development. Jpn. J. Exp. Med. 40, 361–5.Google Scholar
Hoshi, M. & Nagai, Y. (1975). Novel sialoshingolipids from spermatozoa of the sea urchin Anthocidaris crassispina Biochim. Biophys. Acta 388, 152–62.Google ScholarPubMed
Kubo, H. & Hoshi, M. (1990). Immunocytochemical study of the distribution of a ganglioside in sea urchin eggs. J. Biochem.(Tokyo) 108, 193–9.CrossRefGoogle ScholarPubMed
Kubo, H., Irie, A., Inagaki, F. & Hoshi, M. (1990). Gangliosides from the eggs of the sea urchin, Anthocidaris crassispina. J. Biochem. (Tokyo). 108, 185–92.CrossRefGoogle ScholarPubMed
Lee, H.C., Epel, D. (1983). Changes in intrcelluar acidic compartments in sea urchin eggs after activation. Biol. 98, 446–54.Google ScholarPubMed
Matyas, G.R. & Morré, D.J. (1987). Subcellular distribution and biosynthesis of rat liver gangliosides. Biochim. Biophys. Acta 921, 599–614.CrossRefGoogle ScholarPubMed
Nagi, Y. & Hoshi, M. (1975). Sialosphingolipids of sea urchin eggs and spermatzoa showing a characteristic comnposition for species and gamete. Biochim. Biophys. Acta 388, 146–51.Google Scholar
Rahmann, H. (1992). Calcium-ganglioside interactions and modulation of neuronal functions. In: Current Aspects of the Neurosciences 4, ed. N.N., Osborne, pp. 87–125. London: Macmillan press.CrossRefGoogle Scholar
Sakakibara, K., Momoi, T.Uchida, T. & Nagai, Y. (1981). Evidence for association of glycosphingolipid with a colchicine-sensitive microtubule-like cytoskeletal structure of cultured cells. Nature. 293, 76–9.CrossRefGoogle ScholarPubMed
Sardet, C. (1984). The ultrastructure of the sea urchin egg cortex isolated before and after fertilization. Dev. Biol. 105, 196–210.CrossRefGoogle ScholarPubMed
Schwarzmann, G. & Sandhoff, K. (1990). Metabolism and intracellular transport of glycosphingolipids. Biochemistry 29, 10865–71.CrossRefGoogle ScholarPubMed
Silver, R.B., Cole, R.D, & Cande, W.Z. (1980). Isoation of mitotic apparatus containg vesicles with calcium sequestration activity. Cell 19, 505–16.CrossRefGoogle Scholar
Suzuki, A. & Yamakawa, T. (1981). The different distribution of asialo GM1 and Forssman antigen in the small intestine fo mouse demonstrated by immunofluorescence staining. J. Biochem. (Tokyo) 90, 1541–4.CrossRefGoogle Scholar
Terasaki, M. & Jaffe, L. A. (1991). Organization of the sea urchin egg endoplasmic reticulum and its reorganization at fertlilization. J. Cell Biol. 114, 929–40.CrossRefGoogle Scholar
Terasaki, M. & Jaffe, L.A. (1991). Organization of the sea urchin egg endoplasmic reticulum and its reorganzation at fertilization. J. Cell Biol. 114, 929–40.CrossRefGoogle ScholarPubMed
Terasaki, M. & Sardet, C. (1991).Demonstration of calcium uptake and release by sea urchin egg cortical endoplasmic reticulum.J. Cell Biol. 115, 1031–7.CrossRefGoogle ScholarPubMed
Terasaki, M., Song, J.D., Weiss, M.J. & Chen, L.B. (1984). Localization of endoplasmic reticulum in living and glutaraldehyde fixed cells with fluorescent dyes. Cell. 38, 101–8.CrossRefGoogle ScholarPubMed
Teraski, M., Henson, J.Begg, D., Kaminer, B. & Sardet, C. (1991). Characterization of sea urchin egg endoplasmic reticulum in cortical preparations. Dev. Biol. 148, 398–401.CrossRefGoogle Scholar
Vacquier, V.D. (1975). The isolation of intact cortical granules form sea urchin eggs: Calcium ions trigger granular discharge. Dev. Biol. 43, 62–74.CrossRefGoogle Scholar
van Genderen, I.L., van Meer, G., Slot, J.W., Geuze, H.J. & voorhout, W.F. (1991). Subcellular localization of Forss-man glycolipid in epithelial MDCK Cells by immuno-electronmicroscopy after freeze-substitution. J. Cell Biol. 115, 1009–19.CrossRefGoogle ScholarPubMed
Wattenberg, B.W. (1990).Glycolipid and glycoproterin transport through the golgi complex are similar biochemically and kinetically reconstitution of glycolipid transport in a cell free system. J. Cell Biol. 111, 421–8.CrossRefGoogle Scholar
Wessel, G. M., Marchase, R.B. & McClay, D.R. (1984). Ontogeny of the basal lamina in the sea urchin embryo. Dev. Biol. 103, 235–45.CrossRefGoogle ScholarPubMed