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Glycobiology Advance Access originally published online on August 3, 2006
Glycobiology 2006 16(12):1229-1241; doi:10.1093/glycob/cwl036
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Flagellasialin: a novel sulfated {alpha}2,9-linked polysialic acid glycoprotein of sea urchin sperm flagella

Shinji Miyata2,3, Chihiro Sato2,3, Hironobu Kumita2,3, Masaru Toriyama4, Victor D. Vacquier5 and Ken Kitajima1,2,3

2 Graduate School of Bioagricultural Sciences
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 Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093-0202

1 To whom correspondence should be addressed; e-mail: kitajima{at}agr.nagoya-u.ac.jp

Received on May 30, 2006; revised on August 1, 2006; accepted on August 2, 2006

A novel {alpha}2,9-linked polysialic acid (polySia)-containing glycoprotein of sea urchin sperm flagella was identified and named "flagellasialin." Flagellasialin from Hemicentrotus pulcherrimus shows a diverse relative molecular mass on sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) of 40–80 kDa. Flagellasialin is a 96-amino acid, threonine-rich, heavily O-glycosylated (80–90% by weight) glycoprotein with a single transmembrane segment at its C-terminus and no apparent cytosolic domain. Of 12 extracellular Thr residues, eight are O-glycosylated and three are nonglycosylated. Flagellasialin is highly expressed in the testis but cannot be detected in the ovary. The amino acid sequences of flagellasialin from three sea urchin species (H. pulcherrimus, Strongylocentrotus purpuratus, and Strongylocentrotus franciscanus) are identical, but some species differences exist in the three core glycan structures to which the sulfated {alpha}2,9-linked polyNeu5Ac chain is linked. Finally, the treatment of sperm with a specific antibody against the {alpha}2,9-linked polyNeu5Ac structure results in the elevation of intracellular Ca2+ and inhibition of sperm motility and fertilization, implicating flagellasialin as a regulator of these critical processes.

Key words: fertilization / flagellasialin / polysialic acid / sea urchin / sperm motility


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