Molecular Human Reproduction, Vol. 8, No. 12, 1117-1124,
December 2002
© 2002 European Society of Human Reproduction and Embryology
Molecular events in the uterus |
Expression and subcellular distribution of the active form of c-Src tyrosine kinase in differentiating human endometrial stromal cells
1 Department of Obstetrics and Gynecology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582 and 2 Department of Molecular Biology, Osaka Bioscience Institute, 6-2-4, Furuedai, Suita City, Osaka 565-0874, Japan
Abstract
Decidual growth factors and locally produced cytokines are thought to activate specific phosphorylation signalling pathway(s), thereby eliciting a variety of decidual functions. We have previously reported the activation of c-Src tyrosine kinase during ovarian steroid-induced decidualization of cultured human endometrial stromal cells. As chicken c-Src is known to be activated upon dephosphorylation of tyrosine 527 (Y527, corresponding to Y530 in human), we here employed a monoclonal antibody, clone 28, directed against the active form of human c-Src whose Y530 is dephosphorylated, and investigated whether c-Src became dephosphorylated at Y530 and thereby activated during decidualization. We found that the active form of c-Src was up-regulated and demonstrated increased kinase activity during in-vitro decidualization. Immunohistochemistry revealed that decidual cells in early pregnancy decidua were intensely stained with clone 28 when compared with the stromal cells in the non-pregnant endometrium. Moreover, the active form of c-Src translocated from a perinuclear region to the cytoplasm upon decidualization. Thus, the Y530 dephosphorylation, kinase activation, and subcellular translocation of c-Src may be intracellular signalling events associated with decidualization in vivo as well as in vitro.
c-Src/decidualization/progesterone/tyrosine kinase/tyrosine phosphorylation
Notes
3 To whom correspondence should be addressed. E-mail: tetsuo{at}sc.itc.keio.ac.jp
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