Glycobiology Advance Access originally published online on May 26, 2004
Glycobiology 2004 14(9):827-840; doi:10.1093/glycob/cwh100
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Glycobiology vol. 14 no. 9 © Oxford University Press 2004; all rights reserved.
A major flagellum sialoglycoprotein in sea urchin sperm contains a novel polysialic acid, an
2,9-linked poly-N-acetylneuraminic acid chain, capped by an 8-O-sulfated sialic acid residue
2 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan; 3 Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan; 4 Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Ohya, Shizuoka 422-8529, Japan; and 5 Institute for Advanced Research, Nagoya University, Nagoya 464-8601, Japan
Received on April 7, 2004; revised on May 15, 2004; accepted on May 21, 2004
A new type of polysialic acid (polySia) structure was demonstrated to occur in a major unknown sialoglycoprotein with a diverse molecular mass of 4080 kDa in sea urchin sperm. The polySia-containing glycan structure was determined to be HSO3
8Neu5Ac
2
9(Neu5Ac
2
9)n2 Neu5Ac
2
6GalNAc
1
Ser/Thr (n, on average 15), based on carbohydrate analysis of the sialoglycopeptide obtained by an exhaustive protease digestion of whole sperm, fluorometric anion-exchange high-performance liquid chromatography, and methylation analysis. The sulfate group was predominantly localized to the nonreducing terminus of the polySia chain. This is the first example of an
2,9-linked polySia structure in animal sperm. The polySia-containing sialoglycoprotein was present in sperm flagellum but not in the head. Furthermore, this sialoglycoprotein localized in the sperm lipid raft, which contains an enriched ganglioside (Neu5Ac
2
8Neu5Ac
2
6GlcCer), a receptor for sperm-activating peptide (speract), and its associated guanylate cyclase (Ohta et al. [2000] Glycoconj. J., 17, 205214).
1 To whom correspondence should be addressed; e-mail: kitajima{at}agr.nagoya-u.ac.jp
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