PMID: 9159228Aug 15, 1996Paper

Involvement of protein tyrosine phosphorylation of human sperm in capacitation/acrosome reaction and zona pellucida binding

Frontiers in Bioscience : a Journal and Virtual Library
R K Naz

Abstract

The aim of this article is to review the surface molecules that are involved in capacitation/acrosomal exocytosis and zona pellucida (ZP) binding in context of tyrosine phosphorylation leading to signal transduction in human sperm. During capacitation, at least 7 proteins (200, 112, 104, 48, 42, 31 and 25 kD) are phosphorylated as studied by the 32P metabolic labeling assay, and 14 proteins (122, 105, 95, 89, 73, 62, 48, 46, 40, 33, 30, 28, 25 and 22 kD) are autophosphorylated as demonstrated in the in vitro kinase assay. Of the 7-14 proteins, two proteins of 95 and 51 kD molecular identities were phosphorylated at tyrosine residues. Treatment with Talpha1 enhanced and anti-FA-1 monoclonal antibody completely blocked phosphorylation of all the relevant proteins. Sperm proteins belonging to four molecular regions, namely 95 kD (double band), 63 kD (one band), 51 kD (one band) and 14-18 kD (three bands) were involved in ZP binding. Three of these, namely 95 kD, 51 kD and 14-18 kD proteins demonstrated the presence of tyrosine phosphorylation, and the 51 kD protein (that is FA-1 antigen) also showed autophosphorylating activity. These findings, along with the other available data, indicate a vital role of protein tyrosine phosphor...Continue Reading

Citations

Sep 18, 1998·Molecular Reproduction and Development·R K Naz
Oct 30, 1999·Archives of Andrology·R K Naz, P Padman
Dec 3, 1999·Immunological Reviews·R K Naz
Jun 10, 2020·Reproduction in Domestic Animals = Zuchthygiene·Sunil Kumar PatilJanivara Parameshwaraiah Ravindra
Jun 14, 2000·Animal Reproduction Science·E Töpfer-PetersenM Ekhlasi-Hundrieser

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