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Endocrinology Vol. 140, No. 4 1657-1664
Copyright © 1999 by The Endocrine Society

ARTICLES

Insulin-Like Growth Factor I-Triggered Cell Migration and Invasion Are Mediated by Matrix Metalloproteinase-91

Emilia Mira, Santos Mañes, Rosa Ana Lacalle, Gabriel Márquez and Carlos Martínez-A

Department of Immunology and Oncology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Campus de Cantoblanco, E-28049 Madrid, Spain

Address all correspondence and requests for reprints to: Dr. Emilia Mira, Department of Immunology and Oncology, Centro Nacional de Biotecnología, Spanish Research Council CSIC, Universidad Autónoma de Madrid, Campus de Cantoblanco, E-28049 Madrid, Spain. E-mail: emira{at}cnb.uam.es

MCF-7 cells migrate through vitronectin-coated filters in response to insulin-like growth factor I (IGF-I); migration is inhibited by the matrix metalloproteinase (MMP) inhibitor BB-94, but not by the serine proteinase inhibitor aprotinin. MMP-9 was identified in the conditioned medium of MCF-7 cells; in addition, fluorescence-activated cell sorting analysis revealed its presence on the cell surface, where MMP-9 activity was also found using a specific fluorogenic peptide. Furthermore, the messenger RNA encoding MMP-9 was detected in MCF-7 cells by PCR. The IGF-I concentration leading to maximal MCF-7 invasion produces an increase in cell surface proteolytic activity after short incubation periods. At 18 h, however, preincubation of MCF-7 cells with IGF-I produces at 18 h a dose-dependent decrease in cell-associated MMP-9 activity and an increase in soluble MMP-9. MCF-7 invasion is dependent on the {alpha}vß5 integrin, a vitronectin receptor. The levels of {alpha}v- and ß5-subunits expressed in MCF-7 cells depend on the IGF-I concentration, which triggers an increase in both of these subunits. Based on these results, we suggest that IGF-I-induced MCF-7 cell migration is mediated by the MMP-9 activity on the cell surface and by {alpha}vß5 integrin.




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