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Sulfogalactosylglycerolipid is involved in human gamete interaction
Author(s) -
Weerachatyanukul Wattana,
Rattanachaiyat Manee,
Carmona Euridice,
Furimsky Anna,
Mai Andrew,
Shoushtarian Ali,
Sirichotiyakul Supatra,
Ballakier Hanna,
Leader Arthur,
Tanphaichitr gnuj
Publication year - 2001
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1122
Subject(s) - sperm , biology , sperm motility , acrosome , gamete , zona pellucida , percoll , phosphatidylserine , motility , acrosome reaction , microbiology and biotechnology , andrology , biochemistry , in vitro , genetics , oocyte , embryo , phospholipid , membrane , medicine
Recent results from our laboratory have revealed the role of sulfogalactosylglycerolipid (SGG) in mouse sperm‐zona pellucida (ZP) binding. In this report, we demonstrated the presence of SGG in Percoll‐gradient centrifuged (PGC) human sperm by high performance thin layer chromatography with orcinol and Azure A staining, specific for glycolipids and sulfolipids, respectively. SGG in human PGC sperm was quantified by its affinity to Azure A to be 12–15 mol% of sperm lipids. Indirect immunofluorescence revealed that SGG existed on both live and aldehyde fixed human sperm in the head region. Pretreatment of human PGC sperm with affinity purified antiSGG Fab markedly inhibited sperm binding to the ZP in a concentration dependent manner, without any changes in the spontaneous acrosome rate or sperm motility parameters. Fluorescently labeled SGG liposomes also bound uniformly to isolated human ZP, while fluorescently labeled galactosylglycerolipid (GG, SGG's parental lipid) or phosphatidylserine (PS, negatively charged like SGG) liposomes did not. All of these results suggested the role of human sperm SGG in ZP binding. Mol. Reprod. Dev. 60: 569–578, 2001. © 2001 Wiley‐Liss, Inc.