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The Journal of Clinical Endocrinology & Metabolism Vol. 86, No. 6 2484-2493
Copyright © 2001 by The Endocrine Society

Original Articles: Hormones and Reproductive Health

Insulin-Like Growth Factor-Binding Protein 1 Stimulates Human Trophoblast Migration by Signaling through {alpha}5ß1 Integrin via Mitogen-Activated Protein Kinase Pathway1

Louise M. Gleeson, Chandan Chakraborty, Timothy McKinnon and Peeyush K. Lala

Departments of Anatomy and Cell Biology (L.M.G., T.M., P.K.L.) and Pathology (C.C.), The University of Western Ontario, London, Ontario, Canada N6C 5C1

Address all correspondence and requests for reprints to: Peeyush K. Lala, M.D., Department of Anatomy and Cell Biology, Medical Science Building, The University of Western Ontario, London, Ontario, Canada N6A 5C1. E-mail: pklala{at}julian.uwo.ca

Abstract

A highly migratory subpopulation of the human placental trophoblast, known as the extravillous trophoblast (EVT), invades the uterus and its vasculature, to establish adequate exchange of key molecules between the maternal and fetal circulations. During their formation, EVT cells selectively acquire {alpha}5ß1 integrin. We had shown that {alpha}5ß1 is required for their migratory function, and that EVT cell migration is stimulated by insulin-like growth factor-binding protein (IGFBP)-1 produced by the uterine decidua. The present study examined whether this stimulation is dependent on binding of the Arg-Gly-Asp (RGD) domain of IGFBP-1 to an RGD binding site on the {alpha}5ß1 integrin, followed by activation of focal adhesion kinase (FAK) and stimulation of the mitogen-activated protein kinase (MAPK) pathway. IGFBP-1 treatment increased migration of EVT cells, whereas an anti-{alpha}5ß1 integrin antibody blocked migration regardless of IGFBP-1 treatment. Migration stimulation by IGFBP-1 was abrogated by pretreatment with a Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP), but not a Gly-Arg-Gly-Glu-Ser-Pro (GRGESP) hexapeptide, and by mutation of the RGD domain of IGFBP-1 to Trp-Gly-Asp (WGD). IGFBP-1 treatment caused a rapid localization of immunoreactive FAK to cellular lamellipodia, a rapid increase in phosphorylation of FAK and extracellular-signal regulated kinases 1 and 2. Preincubation of EVT cells with Herbimycin A, a tyrosine kinase inhibitor, abrogated IGFBP-1 effects; whereas an MAPK kinase inhibitor, PD 98059, reduced migration regardless of IGFBP-1 treatment. These results indicate that IGFBP-1 stimulation of EVT cell migration occurs by binding of its RGD domain to the {alpha}5ß1 integrin, leading to activation of FAK and stimulation of MAPK pathway.




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