Proteomic characterization of human sperm plasma membrane‐associated proteins and their role in capacitation

Andrology ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 171-180 ◽  
Author(s):  
Gabriela Hernández‐Silva ◽  
Jorge Elías Fabián López‐Araiza ◽  
Aideé Saray López‐Torres ◽  
Fernando Larrea ◽  
Víctor Torres‐Flores ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Human Sperm ◽  
Sperm Plasma Membrane ◽  
Associated Proteins

Characterization of human sperm plasma membrane: Glycolipids and polypeptides

1987 ◽  
Vol 243 (2) ◽  
pp. 339-346 ◽  
Author(s):  
S. R. Mack ◽  
L. J. D. Zaneveld ◽  
R. N. Peterson ◽  
W. Hunt ◽  
L. D. Russell
Keyword(s):  
Plasma Membrane ◽  
Human Sperm ◽  
Sperm Plasma Membrane

scholarly journals A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1

Reproduction ◽  
2005 ◽  
Vol 130 (4) ◽  
pp. 497-508 ◽  
Author(s):  
Rachel Gibbons ◽  
Susan A Adeoya-Osiguwa ◽  
Lynn R Fraser
Keyword(s):  
Plasma Membrane ◽  
Binding Protein ◽  
Human Sperm ◽  
Surface Proteins ◽  
Mouse Sperm ◽  
Fertility Treatments ◽  
State Dependent ◽  
Sperm Plasma Membrane ◽  
Associated Proteins ◽  
Functional Consequences

Capacitation is a pivotal event for mammalian spermatozoa, involving the loss of surface proteins known as decapacitation factors (DF) and consequent acquisition of fertilizing ability. Earlier studies showed that a mouse sperm DF binds to a receptor, DF-R, whose attachment to the sperm plasma membrane appears to involve a glycosylphosphatidylinositol (GPI) anchor. In the present study, purification and subsequent sequencing of DF-R has identified this ~23 kDa protein as phosphatidyletha-nolamine-binding protein 1 (PEBP 1). To obtain functional evidence that supports sequence homology data, purified recombinant PEBP 1 and PEBP 2 were evaluated for biological activity. While PEBP 1 was able to remove DF activity in solution at concentrations above ~1 nmol/l, PEBP 2 was ineffective, even at 600 nmol/l; this confirmed that DF-R is PEBP 1. Anti-PEBP 1 antiserum recognized recombinant PEBP 1 and a ~23 kDa protein in both mouse and human sperm lysates. Immunolocalization studies revealed that DF-R/PEBP 1 is located on the acrosomal cap, the post-acrosomal region and the flagellum of both mouse and human spermatozoa, with epitope accessibility being capacitation state-dependent and reversible. Treatment of cells with a phospholipase able to cleave GPI anchors essentially abolished immunostaining, thus confirming the extracellular location of DF-R/PEBP 1. We suggest that DF-R/PEBP 1 plays its fundamental role in capacitation by causing alterations in the sperm plasma membrane in both head and flagellum, with functional consequences for membrane-associated proteins. Obtaining more detail about DF ↔ DF-R interactions could lead to useful applications in both fertility treatments and new contraceptive approaches.

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 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

A Time-Resolved Fluorescence Diphenylhexatriene (DPH) Anisotropy Characterization of a Series of Model Lipid Constructs for the Sperm Plasma Membrane

2006 ◽  
Vol 45 (21) ◽  
pp. 6939-6945 ◽  
Author(s):  
Gregory M. Troup ◽  
Steven P. Wrenn ◽  
Meirav Apel-Paz ◽  
Gustavo F. Doncel ◽  
T. Kyle Vanderlick
Keyword(s):  
Plasma Membrane ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Sperm Plasma Membrane

scholarly journals Identification of calcium-binding proteins associated with the human sperm plasma membrane

2010 ◽  
Vol 8 (1) ◽  
Author(s):  
Soren Naaby-Hansen ◽  
Alan Diekman ◽  
Jagathpala Shetty ◽  
Charles J Flickinger ◽  
Anne Westbrook ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Human Sperm ◽  
Calcium Binding Proteins ◽  
Sperm Plasma Membrane
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