Localization of a 25 kDa human sperm surface protein: its role in in- vitro human sperm capacitation [published erratum appears in Mol Hum Reprod 1997 Jul;3(8):638]
Autor: | Maitrayee Banerjee, Mridula Chowdhury |
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Rok vydání: | 1997 |
Předmět: |
chemistry.chemical_classification
endocrine system Embryology urogenital system Superoxide Obstetrics and Gynecology Mannose Cell Biology Biology Sperm Sialic acid chemistry.chemical_compound Reproductive Medicine chemistry Biochemistry Capacitation Genetics Receptor Glycoprotein Molecular Biology reproductive and urinary physiology Mannose receptor Developmental Biology |
Zdroj: | Molecular Human Reproduction. 3:109-114 |
ISSN: | 1460-2407 |
Popis: | A human endometrial sialic acid-binding glycoprotein (SABP) binds specifically to a 25 kDa protein on the plasma membranes of human non-capacitated sperm heads. In-vitro labelling of the sperm surface sialoglycoconjugates and subsequent incubation with SABP, suggests removal of some sialoglycoconjugate moieties from the sperm surface upon interaction with SABP. SABP also induces the exposure of mannose ligand receptors on the sperm surface and increases the production of superoxide anion (O2 .–). Key words:human sperm capacitation/mannose receptor/SABP/sialoglycoconjugates/superoxide anion |
Databáze: | OpenAIRE |
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