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Incidence of sperm-tail tyrosine phosphorylation and hyperactivated motility in normozoospermic and asthenozoospermic human sperm samples Biocell
Yunes,Roberto; Doncel,Gustavo F.; Acosta,Anibal A..
Our objective was to study the incidence of sperm-tail phosphotyrosine immunoreactivity in normozoospermic and asthenozoospermic human sperm samples, its association with sperm motion parameters, particularly hyperactivated motility, and its potential involvement in the pathogenesis of asthenozoospermia. The work was conducted as a prospective experimental study in the Sperm Biology and Andrology laboratories of the Jones Institute, a medical school-based fertility center. The study subjects were healthy fertile male donors (normozoospermic samples) and infertile patients (asthenozoospermic samples) attending the center. Recently ejaculated semen samples were washed twice to eliminate seminal plasma and a swim-up was performed to select the motile...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Sperm motility; Hyperactivation; Asthenozoospermia; Tyrosine-phosphorylation; Protein-tyrosine kinase.
Ano: 2003 URL: http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0327-95452003000100004
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Porcine oviduct sperm binding glycoprotein and its deleterious effect on sperm: a mechanism for negative selection of sperm? Biol. Res.
Teijeiro,Juan M; Dapino,Dora G; Marini,Patricia E.
In their journey through the oviduct some subpopulations of sperm are preserved in a reservoir, while others are negatively selected. Sperm binding glycoprotein (SBG) is a pig oviductal epithelial cell glycoprotein that produces, under capacitating conditions, acrosome alteration, p97 tyrosine-phosphorylation and reduction of the motility of sperm. In this paper, we show that SBG is accessible at the extracellular surface of the oviductal epithelial cells, supporting a sperm interaction biological role in situ. We analyze the possible dependence of the tyrosine-phosphorylation of p97 on the PKA mechanism, finding that apparently it is not PKA dependent. Also, after SBG treatment the phosphorylated proteins locate mainly at the detached periacrosomal region...
Tipo: Journal article Palavras-chave: Acrosome alteration; Tyrosine-phosphorylation.
Ano: 2011 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602011000400003
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