Journal
HUMAN REPRODUCTION
Volume 24, Issue 11, Pages 2856-2867Publisher
OXFORD UNIV PRESS
DOI: 10.1093/humrep/dep265
Keywords
glycodelin; spermatozoa; cumulus matrix; alpha 2-macroglobulin; hyaluronic acid
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Funding
- Committee on Research and Conference Grant
- University of Hong Kong
- Hong Kong Research Grant Council [HKU7514/05M, HKU7647/06M]
- Helsinki University Central Hospital Research Funds
- Cancer Society of Finland
- Academy of Finland
- University of Helsinki
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BACKGROUND: Glycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix. METHODS: GIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS: Mass spectrometry analysis suggested that GIP contained the N-terminal region of alpha 2-macroglobulin, confirmed by western blot with anti-alpha 2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled alpha 2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION: The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and -F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.
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