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Sperm plasma membrane

About: Sperm plasma membrane is a research topic. Over the lifetime, 1016 publications have been published within this topic receiving 49964 citations.


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TL;DR: A role for glycoprotein modifying enzymes in the modification of sperm surface glycoproteins during epididymal maturation is strongly suggested.
Abstract: It is generally accepted that mammalian spermatozoa undergo biochemical and morphological changes during epididymal transit, collectively termed epididymal maturation. Although many details of the biochemical modification are not fully understood, lectin binding studies from several laboratories strongly suggest that glycan moieties of sperm plasma membrane glycoproteins are extensively modified as spermatozoa transit from the proximal to the distal epididymis. In the present article, we summarize our studies with two sets of glycan modifying enzymes, namely glycosyltransferases (synthetic enzymes) and glycosidases (hydrolytic enzymes) in rat spermatozoa collected from different regions of the epididymis, and similar enzyme activities present in the epididymal luminal fluid. Our data show that the activities of these enzyme are high in the epididymal luminal fluid (> 80% of the total enzyme activities was in the plasma). Evidence presented in this report also demonstrates that: (1) at least one sperm surface glycoprotein (apparent molecular mass of 86 kDa) is fucosylated in vitro when caput spermatozoa are incubated with GDP [14C]fucose; and (2) a peanut agglutinin (PNA)-positive glycoprotein of 135-150 kDa present on plasma membrane of sperm from the caput (but not cauda) epididymidis is degalactosylated by digestion with purified luminal fluid beta-D-galactosidase. Taken together, these results strongly suggest a role for glycoprotein modifying enzymes in the modification of sperm surface glycoproteins during epididymal maturation.

67 citations

Journal ArticleDOI
TL;DR: These components of the gamete fusion mechanism within the framework of gamete structure, membrane biology, cell signalling and cytoskeletal dynamics are discussed, and the topic of antipolyspermy defence at the oolemma level is revisited.
Abstract: Fertilisation is an orchestrated, stepwise process during which the participating male and female gametes undergo irreversible changes, losing some of their structural components while contributing others to the resultant zygote. Following sperm penetration through the egg coat, the sperm plasma membrane fuses with its oocyte counterpart, the oolemma. At least two plasma membrane proteins essential for sperm-oolemma fusion--IZUMO and CD9 on the male and female gametes, respectively--have been identified recently by classical cell biology approaches and confirmed by gene deletion. Oolemma-associated tetraspanin CD81, closely related to CD9, also appears to have an essential role in fusion. Additional proteins that may have nonessential yet still facilitating roles in sperm-oolemma adhesion and fusion include oolemma-anchored integrins and oocyte-expressed retroviral envelope proteins, sperm disintegrins, and sperm-borne proteins of epididymal origin such as CRISP1 and CRISP2. This review discusses these components of the gamete fusion mechanism within the framework of gamete structure, membrane biology, cell signalling and cytoskeletal dynamics, and revisits the topic of antipolyspermy defence at the oolemma level. Harnessing the mechanisms of sperm-egg fusion is of importance to animal biotechnology and to human assisted fertilisation, wherein male patients with reduced sperm fusibility have been identified.

67 citations

Journal ArticleDOI
TL;DR: The role of pig sperm surface AS-A in ZP binding was demonstrated by dose-dependent decreases of sperm-ZP binding upon sperm pretreatment with anti-AS-A IgG/Fab, and by the binding of Alexa-430-conjugated sperm surface As-A to homologous ZP.

67 citations

Journal ArticleDOI
TL;DR: Although these environmental estrogens have been suggested to mimic estrogen effects in the other cell types, probably acting through genomic receptors, in human spermatozoa they do not interfere with 17betaE(2) binding to its membrane receptor and with the short-term effects exerted by this steroid.

67 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20221
202121
202029
201920
201827
201726