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Co-expression of two distinct polysialic acids, 2,8- and 2,9-linked polymers of N-acetylneuraminic acid, in distinct glycoproteins and glycolipids in sea urchin sperm

Co-expression of two distinct polysialic acids, 2,8- and 2,9-linked polymers of... Naturally occurring polysialic acid (polySia) structures have a large diversity, primarily arising from the diversity in the sialic acid components as well as in the intersialyl linkages. In 2004, we demonstrated the presence of a new type of polySia, 8-O-sulfated N-acetylneuraminic acid (Neu5Ac) capped 2,9-linked polyNeu5Ac, on the O-glycans of a major 4080kDa sialoglycoprotein, flagellasialin, in sea urchin sperm. In this study, we demonstrated that another type of polySia, the 2,8-linked polyNeu5Ac, exclusively occurs on O-glycans of a 190kDa glycoprotein (190kDa-gp), whereas the 2,9-linked polyNeu5Ac is exclusively present on flagellasialin. The 190kDa-gp is localized in both flagellum and head of sperm. We also demonstrated that polysialogangliosides containing the 2,8-linked polyNeu5Ac are present in sperm head. Thus, this study shows two novel features of the occurrence of polySia in nature, the co-localization of polySia with different intersialyl linkages, the 2,8- and 2,9-linkages, in a single cell and the occurrence of 2,8-linked polyNeu5Ac in glycolipids. Anti-2,8-linked polyNeu5Ac antibody had no effect on fertilization, which contrasted with the previous results that anti-2,9-linked polyNeu5Ac antibody inhibited sperm motility and fertilization. Based on these properties, distinct functions of 2,8- and 2,9-polySia structures are implicated in fertilization. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Glycobiology Oxford University Press

Co-expression of two distinct polysialic acids, 2,8- and 2,9-linked polymers of N-acetylneuraminic acid, in distinct glycoproteins and glycolipids in sea urchin sperm

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References (45)

Publisher
Oxford University Press
Copyright
The Author 2011. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissionsoup.com
Subject
ORIGINAL ARTICLES
ISSN
0959-6658
eISSN
1460-2423
DOI
10.1093/glycob/cwr081
pmid
21725074
Publisher site
See Article on Publisher Site

Abstract

Naturally occurring polysialic acid (polySia) structures have a large diversity, primarily arising from the diversity in the sialic acid components as well as in the intersialyl linkages. In 2004, we demonstrated the presence of a new type of polySia, 8-O-sulfated N-acetylneuraminic acid (Neu5Ac) capped 2,9-linked polyNeu5Ac, on the O-glycans of a major 4080kDa sialoglycoprotein, flagellasialin, in sea urchin sperm. In this study, we demonstrated that another type of polySia, the 2,8-linked polyNeu5Ac, exclusively occurs on O-glycans of a 190kDa glycoprotein (190kDa-gp), whereas the 2,9-linked polyNeu5Ac is exclusively present on flagellasialin. The 190kDa-gp is localized in both flagellum and head of sperm. We also demonstrated that polysialogangliosides containing the 2,8-linked polyNeu5Ac are present in sperm head. Thus, this study shows two novel features of the occurrence of polySia in nature, the co-localization of polySia with different intersialyl linkages, the 2,8- and 2,9-linkages, in a single cell and the occurrence of 2,8-linked polyNeu5Ac in glycolipids. Anti-2,8-linked polyNeu5Ac antibody had no effect on fertilization, which contrasted with the previous results that anti-2,9-linked polyNeu5Ac antibody inhibited sperm motility and fertilization. Based on these properties, distinct functions of 2,8- and 2,9-polySia structures are implicated in fertilization.

Journal

GlycobiologyOxford University Press

Published: Dec 1, 2011

Keywords: flagellasialin polysialoganglioside ॅ2,8-polysialic acid ॅ2,9-polysialic acid sea urchin sperm

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