Cell surface binding sites for progesterone on human spermatozoa
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چکیده
منابع مشابه
Cell surface binding sites for progesterone on human spermatozoa.
This study demonstrates the presence of [3H]-progesterone binding protein on the cell surface of human spermatozoa. The binding protein is masked and is exposed after treatment of spermatozoa with surfactants such as digitonin. Specific binding of [3H]-progesterone is observed after the washed spermatozoa or the crude cell membrane fractions are treated with 0.1% digitonin at 0-4 degrees C for ...
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Recent studies (e.g. Blackmore, P. F., Beebe, S. J., Danforth, D. R., and Alexander, N.) (1990) J. Biol. Chem. 265, 1376-1380) have shown that in human sperm, progesterone produces a rapid increase in intracellular free calcium ([Ca2+]i) and an induction of the acrosome reaction (e.g. Osman, R. A., Andria, M. L., Jones, A. D., and Meizel, S. (1989) Biochem, Biophys. Res. Commun. 160, 828-833). ...
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Progesterone, primarily recognized as a female steroid hormone, is reported to affect several sperm functions especially capacitation, motility and acrosome reaction. These effects of progesterone on the spermatozoa are mediated via the progesterone binding sites/progesterone receptor (PR) on the acrosomal membrane. These receptors in response to progesterone increase the intercellular Ca2+ lev...
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A D-mannosylated albumin (DMA) neoglycoprotein was assessed to validate experimentally a probe capable of detecting mannose-binding sperm receptors involved in human sperm-egg interaction. DMA specifically blocked zona binding of swim-up human spermatozoa in a concentration-dependent manner. While no considerable effect was observed on sperm-zona initial contact, almost 50% of spermatozoa bound...
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OBJECTIVE The purpose of this study was to understand the interactions of apoA-I with cells expressing ABCA1. METHODS AND RESULTS The binding of wild-type (WT) and mutant forms of human apoA-I to mouse J774 macrophages was examined. Analysis of total binding at 37 degrees C of 125I-WT apoA-I to the cells and specifically to ABCA1, as determined by covalent cross-linking, revealed saturable hi...
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ژورنال
عنوان ژورنال: Molecular Human Reproduction
سال: 1998
ISSN: 1460-2407
DOI: 10.1093/molehr/4.5.413