Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: Identification of a kinase anchor proteins as major substrates for tyrosine phosphorylation

被引:274
作者
Carrera, A
Moos, J
Ning, XP
Gerton, GL
Tesarik, J
Kopf, GS
Moss, SB
机构
[1] UNIV PENN,MED CTR,CTR RES REPROD & WOMENS HLTH,DEPT OBSTET & GYNECOL,PHILADELPHIA,PA 19104
[2] UNIV PENN,MED CTR,DEPT BIOL,PHILADELPHIA,PA 19104
[3] UNIV PENN,MED CTR,DEPT DEV & CELL BIOL,PHILADELPHIA,PA 19104
[4] UNIV GRANADA,DEPT BIOCHEM & MOL BIOL,FAC SCI,E-18071 GRANADA,SPAIN
关键词
D O I
10.1006/dbio.1996.0301
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Signal transduction pathways regulate various aspects of mammalian sperm function. When human sperm were incubated in a medium supporting capacitation, proteins became tyrosine-phosphorylated in a time-dependent manner. This phosphorylation was inhibited by genistein, a protein tyrosine kinase inhibitor. Phosphorylation was also reduced when sperm were incubated either in the presence of increasing concentrations of extracellular Ca2+ or in a medium containing the Ca2+ ionophore A23187. This Ca2+-induced dephosphorylation was calmodulin-dependent, suggesting that calcineurin was involved. Zn this regard, the calcineurin inhibitor deltamethrin inhibited the Ca2+ ionophore-induced dephosphorylation. A limited number of M(r) 80,000-105,000 polypeptides were the most prominent phosphotyrosine-containing proteins present in human sperm. Unlike mouse sperm, which contains a tyrosine-phosphorylated isoform of hexokinase, a phosphotyrosine-containing hexokinase in human sperm was not detected. Most of the tyrosine-phosphorylated proteins were Triton X-100-insoluble and were localized to the principal piece of the flagellum, the region where the cytoskeletal fibrous sheath is found. Prominent phosphotyrosine-containing proteins of M(r) 82,000 and 97,000 were identified as the human homologues of mouse sperm AKAP82, the major fibrous sheath protein, and pro-AKAP82, its precursor polypeptide, respectively. These proteins are A Kinase Anchor Proteins, polypeptides that sequester protein kinase A to subcellular locations. Taken together, these results suggest that protein tyrosine phosphorylation may be part of a signal transduction cascade(s) regulating events pertaining to capacitation and/or motility in mammalian sperm and that an interrelationship between tyrosine kinase and cAMP signaling pathways exists in these cells. (C) 1996 Academic Press, Inc.
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页码:284 / 296
页数:13
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