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Phosphorylation of Shc proteins in human sperm in response to capacitation and progesterone treatment
Author(s) -
Morte Carles,
Iborra Antoni,
Martínez Paz
Publication year - 1998
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199805)50:1<113::aid-mrd14>3.0.co;2-9
Subject(s) - capacitation , acrosome reaction , phosphorylation , sperm , biology , tyrosine phosphorylation , western blot , microbiology and biotechnology , gene isoform , signal transduction , protein phosphorylation , kinase , tyrosine , immunoprecipitation , acrosome , andrology , antibody , biochemistry , protein kinase a , immunology , genetics , gene , medicine
Several authors have demonstrated the involvement of tyrosine kinases during sperm capacitation and acrosome reaction. Shc proteins (p46 Shc , p52 Shc , and p66 Shc ) are cytoplasmic substrates of activated tyrosine kinases and are widely expressed in mammalian somatic tissues. Experiments were designed to demonstrate the presence of Shc in spermatozoa and to study its involvement in the signal transduction events leading to acrosome reaction. Anti‐Shc antibodies strongly reacted with the acrosomal region of methanol‐fixed human sperm. Only one Shc isoform (p52 Shc ) was detected on Western blot. To study the degree of phosphorylation of Shc during capacitation and acrosome reaction, sperm samples were divided into two groups: noncapacitated and capacitated/progesterone treated. Lysates from both groups were immunoprecipitated with anti‐phosphotyrosine antibodies and the precipitated (ie, phosphorylated) proteins were tested with anti‐Shc antibodies. The intensity of p52 Shc was clearly increased in capacitated/progesterone‐stimulated cells. Mol. Reprod. Dev. 50:113–120, 1998. © 1998 Wiley‐Liss, Inc.