Occurrence of wax esters and 1-O-alkyl-2,3-diacylglycerols in goat epididymal sperm plasma membrane

Lipids ◽  
1992 ◽  
Vol 27 (1) ◽  
pp. 75-78 ◽  
Author(s):  
Ajay P. S. Rana ◽  
Gopal C. Majumder ◽  
Suniti Misra ◽  
Amitabha Ghosh
Keyword(s):  
Plasma Membrane ◽  
Wax Esters ◽  
Epididymal Sperm ◽  
Sperm Plasma Membrane

scholarly journals Dissecting the PRSS37 interactome and potential mechanisms leading to ADAM3 loss in PRSS37 null sperm

2021 ◽  
Author(s):  
Wenfeng Xiong ◽  
Chunling Shen ◽  
Chaojie Li ◽  
Xiaohong Zhang ◽  
Haoyang Ge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Male Infertility ◽  
Molecular Chaperones ◽  
Epididymal Sperm ◽  
Sperm Migration ◽  
Sperm Plasma Membrane ◽  
Sperm Membrane ◽  
A Disintegrin And Metalloproteinase

A disintegrin and metalloproteinase 3 (ADAM3) is a sperm membrane protein critical for sperm migration from the uterus into the oviduct and sperm-egg binding in mice. Disruption of PRSS37 results in male infertility concurrent with the absence of mature ADAM3 from cauda epididymal sperm. However, how PRSS37 modulates ADAM3 maturation remains largely unclear. Here, we determine PRSS37 interactome by GFP immunoprecipitation coupled with mass spectrometry in PRSS37-EGFP knock-in mice. Three molecular chaperones (CLGN, CALR3 and PDILT) and three ADAM proteins (ADAM2, ADAM6B and ADAM4) were identified to be interacting with PRSS37. Coincidently, five of them (except ADAM4) have been reported to interact with precursor ADAM3 and regulate its maturation. We further demonstrated that PRSS37 also interacts directly with precursor ADAM3 and its deficiency impedes the association between PDILT and ADAM3. This could contribute to improper translocation of ADAM3 to the germ cell surface, leading to ADAM3 loss in PRSS37 null mature sperm. The understanding of the maturation mechanisms of pivotal sperm plasma membrane proteins will pave the way toward novel strategies for contraception and treatment of unexplained male infertility.

Lipid changes of goat sperm plasma membrane during epididymal maturation

1991 ◽  
Vol 1061 (2) ◽  
pp. 185-196 ◽  
Author(s):  
Ajay P.S. Rana ◽  
Gopal C. Majumder ◽  
Suniti Misra ◽  
Amitabha Ghosh
Keyword(s):  
Plasma Membrane ◽  
Epididymal Maturation ◽  
Sperm Plasma Membrane

Mechanism of human sperm activation by extracellular ATP

1996 ◽  
Vol 270 (6) ◽  
pp. C1709-C1714 ◽  
Author(s):  
C. Foresta ◽  
M. Rossato ◽  
P. Chiozzi ◽  
F. Di Virgilio
Keyword(s):  
Plasma Membrane ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Extracellular Atp ◽  
Effective Concentration ◽  
Na Channel ◽  
Monovalent Cations ◽  
Sperm Activation ◽  
Gated Channel ◽  
Sperm Plasma Membrane

We have identified the mechanism whereby extracellular ATP (ATPe) triggers the acrosome reaction in human spermatozoa. This nucleotide opens a ligand-gated ion channel expressed on the sperm plasma membrane. ATPe threshold and 50% effective concentration calculated on the total added ATPe are 0.1 and 2 mM, respectively, corresponding to a free ATP concentration (ATP4-) of 3 and 200 microM, respectively. The ATPe-gated channel is selective for monovalent cations (Na+, choline, and methylglucamine), whereas on the contrary, permeability to Ca2+ is negligible. Isosmolar replacement of extracellular Na+ with sucrose fully blocked ATPe-dependent sperm activation, thus suggesting a mandatory role for Na+ influx. These results show that human sperm express an ATPe-gated Na+ channel that might have an important role in sperm activation before egg fertilization.

scholarly journals Immunocytochemical localization and biochemical characterization of a novel plasma membrane-associated, neutral pH optimum α-l-fucosidase from rat testis and epididymal spermatozoa

1996 ◽  
Vol 318 (3) ◽  
pp. 821-831 ◽  
Author(s):  
Manuel AVILÉS ◽  
Irene ABASCAL ◽  
José Angel MARTÍNEZ-MENÁRGUEZ ◽  
María Teresa CASTELLS ◽  
Sheri R. SKALABAN ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Biochemical Characterization ◽  
Gradient Centrifugation ◽  
Light And Electron Microscopy ◽  
Enzymic Activity ◽  
Epididymal Sperm ◽  
Sucrose Density Gradient Centrifugation ◽  
Ph Optimum ◽  
Neutral Ph

1. Immunocytochemical and biochemical techniques have been used to localize and characterize a novel plasma membrane-associated, neutral-pH-optimum α-l-fucosidase from rat spermatozoa. Light and electron microscopy specifically localized the fucosidase on the plasma membrane of the convex region of the principal segment of testicular and cauda epididymal sperm heads. Immunoreactivity for α-l-fucosidase was also detected in the Golgi apparatus of spermatocytes and spermatids but no immunoreactivity was observed in the acrosome. 2. Fractionation of epididymal sperm homogenates indicated that over 90% of the α-l-fucosidase activity was associated with the 48000 g pellet. This pellet-associated activity could be solubilized with 0.5 M NaCl but not with 0.5% Triton X-100, suggesting that fucosidase is peripherally associated with membranes. Sucrose-density-gradient centrifugation of sperm homogenates indicated that fucosidase was enriched in the plasma membrane-enriched fraction. Analysis of α-l-fucosidase on intact epididymal sperm indicated that the enzyme was active, displayed linear kinetics and had a pH–activity curve (with an optimum near 7) which was comparable to that of fucosidase from epididymal sperm extracts. These results further suggest that fucosidase is associated with plasma membranes, and that its active site is accessible to fucoconjugates. Evidence that most of the fucosidase is associated with the exterior of the plasma membrane came from studies in which intact sperm had fucosidase activity comparable to that of sperm sonicates, and from studies in which approx. 90% of the fucosidase activity on intact sperm could be released from the sperm by gentle shaking with 0.5 M NaCl. Isoelectric focusing indicated that the NaCl-solubilized epididymal sperm fucosidase appears to have one major and one minor isoform with pIs near 7.2 and 5.2, respectively. SDS/PAGE and Western blotting indicated that the NaCl-solubilized extract of epididymal sperm contains two protein bands of 54 and 50 kDa which were highly immunoreactive with the IgG fraction of anti-fucosidase antibodies. Although the function of the novel sperm fucosidase is not known, its specific localization to the plasma membrane of the region of the rat sperm head involved in sperm–egg binding and its high enzymic activity at neutral pH on intact sperm suggest that this enzyme may have a role in sperm–egg interactions.

scholarly journals Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

2006 ◽  
Vol 120 (1) ◽  
pp. 33-44 ◽  
Author(s):  
P. C. N. Chiu ◽  
M.-K. Chung ◽  
R. Koistinen ◽  
H. Koistinen ◽  
M. Seppala ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Zona Pellucida ◽  
Human Sperm ◽  
Sperm Plasma Membrane ◽  
Glycodelin A
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