Journal
GLYCOBIOLOGY
Volume 16, Issue 12, Pages 1229-1241Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwl036
Keywords
fertilization; flagellasialin; polysialic acid; sea urchin; sperm motility
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Funding
- NICHD NIH HHS [HD12986] Funding Source: Medline
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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.
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