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Endocrinology Vol. 144, No. 4 1620-1630
Copyright © 2003 by The Endocrine Society

ARTICLE

{alpha}vß3 Integrin Signaling Pathway Is Involved in Insulin-Like Growth Factor I-Stimulated Human Extravillous Trophoblast Cell Migration

Maryam Kabir-Salmani, Shigetatsu Shiokawa, Yoshihiro Akimoto, Keiji Sakai, Shinya Nagamatsu, Ken Sakai, Yukio Nakamura, Abbas Lotfi, Hayato Kawakami and Mitsutoshi Iwashita

Departments of Obstetrics and Gynecology (M.K.-S., S.S., K.J.S., K.S., Y.N., M.I.), Anatomy (Y.A., H.K.), Biochemistry (S.N.), Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Department of Biochemistry (A.L.), Tarbiat Modarres University, Tehran 14115-111, Iran

Address all correspondence to: M. Iwashita, M.D., Ph.D., Department of Obstetrics and Gynecology, Kyorin University School of Medicine, 6-20-2, Shinkawa, Mitaka, Tokyo 181-8611, Japan. E-mail: iwashita{at}netjoy.ne.jp.

IGF-I and -II provide paracrine and autocrine stimuli, respectively, for extravillous trophoblast (EVT) cell migration. This study examined the role of {alpha}vß3 integrin and its signaling pathway in IGF-I-stimulated migration. Migration assays were conducted using cultured EVT cells treated with or without IGF-I in the presence or absence of {alpha}IR3, Arg-Gly-Asp (RGD) hexapeptide, and antibody against {alpha}vß3 integrin. Morphological changes were studied using scanning electron microscopy. Colocalization of {alpha}5ß1 {alpha}vß3 integrins, vinculin, focal adhesion kinase, and paxillin were determined by immuno-cytochemistry and immunoblotting. The results showed that IGF-I could stimulate EVT cell migration in a time- and dose-dependent manner and addition of {alpha}IR3, Arg-Gly-Asp hexapeptide, and antibody against {alpha}vß3 integrin attenuated the IGF-I migratory effect. Scanning electron microscopy images revealed that IGF-I promoted lamellipodia formation. Immunostaining and immunoblotting exhibited the colocalization of {alpha}vß3 integrin with phosphorylated focal adhesion kinase, paxillin, and vinculin at focal adhesions after IGF-I treatment. Immunoblotting demonstrated an increase in focal adhesion kinase and paxillin tyrosine phosphorylation followed by tyrosine phosphorylation of IGF-I receptor in a time- and dose-dependent manner. These findings indicated {alpha}vß3 integrin localization in the core of focal adhesions of EVT cells and that {alpha}vß3 integrin signaling pathways are activated in IGF-I-mediated migration of these cells.




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