This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Maruyama, T. Articles by Sabe, H. Search for Related Content PubMed PubMed Citation Articles by Maruyama, T. Articles by Sabe, H.

Tyrosine Phosphorylation and Subcellular Localization of Focal Adhesion Proteins during in Vitro Decidualization of Human Endometrial Stromal Cells

Department of Obstetrics and Gynecology, Keio University School of Medicine (T.M., Y.Y.), Tokyo 160-0016, Japan; and the Department of Biological Responses, Institute for Virus Research, Kyoto University (T.M., H.S.), Kyoto 606-8397, Japan

Address all correspondence and requests for reprints to: Dr. Tetsuo Maruyama, Department of Obstetrics and Gynecology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-0016, Japan. Fax: 81-3-3226-1667.

Human endometrial stromal cells undergo in vitro decidualization when treated with progesterone and estrogen. Using this model, we previously reported specific changes in the c-Src kinase activity and tyrosine phosphorylation of several proteins during in vitro decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. We here examined the tyrosine phosphorylation and subcellular localization of the focal adhesion proteins in stromal cells isolated from human endometrium. We found, however, that the total levels of FAK and paxillin tyrosine phosphorylation were not markedly changed during decidualization or after steroid withdrawal. In our culture system, numerous multicellular nodules were developed in cultures of decidualized stromal cells, within whose nodules the focal contacts were found to disappear. Moreover, disruption of the focal contacts was accompanied by disorganization of the actin-based cytoskeleton. These findings suggest that tyrosine phosphorylation of the endometrial paxillin and FAK is not tightly regulated by the kinase activity of c-Src during in vitro decidualization. The escape from regulation by c-Src may be in part due to the dissociation of the focal adhesion proteins/c-Src complex caused by the breakdown of the focal adhesion plaques as well as the loss of the actin-based cytoskeletal architecture.

This article has been cited by other articles:

				T. Nagashima, T. Maruyama, H. Uchida, T. Kajitani, T. Arase, M. Ono, H. Oda, M. Kagami, H. Masuda, S. Nishikawa, et al. Activation of SRC Kinase and Phosphorylation of Signal Transducer and Activator of Transcription-5 Are Required for Decidual Transformation of Human Endometrial Stromal Cells Endocrinology, March 1, 2008; 149(3): 1227 - 1234. [Abstract] [Full Text] [PDF]

				I. Ihnatovych, W. Hu, J. L. Martin, A. T. Fazleabas, P. de Lanerolle, and Z. Strakova Increased Phosphorylation of Myosin Light Chain Prevents in Vitro Decidualization Endocrinology, July 1, 2007; 148(7): 3176 - 3184. [Abstract] [Full Text] [PDF]

				N. Sakai, T. Maruyama, R. Sakurai, H. Masuda, Y. Yamamoto, A. Shimizu, I. Kishi, H. Asada, S. Yamagoe, and Y. Yoshimura Involvement of Histone Acetylation in Ovarian Steroid-induced Decidualization of Human Endometrial Stromal Cells J. Biol. Chem., May 2, 2003; 278(19): 16675 - 16682. [Abstract] [Full Text] [PDF]

				Y. Yamamoto, T. Maruyama, N. Sakai, R. Sakurai, A. Shimizu, T. Hamatani, H. Masuda, H. Uchida, H. Sabe, and Y. Yoshimura Expression and subcellular distribution of the active form of c-Src tyrosine kinase in differentiating human endometrial stromal cells Mol. Hum. Reprod., December 1, 2002; 8(12): 1117 - 1124. [Abstract] [Full Text] [PDF]