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Vol. 10, Issue 10, 3463-3471, October 1999

Integrin-mediated Adhesion of Endothelial Cells Induces JAK2 and STAT5A Activation: Role in the Control of c-fos Gene Expression

Maria Felice Brizzi,^* Paola Defilippi, Arturo Rosso,^* Mascia Venturino, Giovanni Garbarino,^* Atsushi Miyajima,^§ Lorenzo Silengo, Guido Tarone, and Luigi Pegoraro^*

Departments of  ^*Internal Medicine  Genetics, Biology, and Biochemistry, University of Torino, 10126 Torino, Italy; and  ^§Institute of Molecular and Cellular Biosciences, University of Tokyo, 113-0032 Tokyo, Japan

Integrin-mediated adhesion induces several signaling pathways leading to regulation of gene transcription, control of cell cycle entry and survival from apoptosis. Here we investigate the involvement of the Janus kinase (JAK)/signal transducers and activators of transcription (STAT) pathway in integrin-mediated signaling. Plating primary human endothelial cells from umbilical cord and the human endothelial cell line ECV304 on matrix proteins or on antibody to 1- or v-integrin subunits induces transient tyrosine phosphorylation of JAK2 and STAT5A. Consistent with a role for the JAK/STAT pathway in regulation of gene transcription, adhesion to matrix proteins leads to the formation of STAT5A-containing complexes with the serum-inducible element of c-fos promoter. Stable expression of a dominant negative form of STAT5A in NIH3T3 cells reduces fibronectin-induced c-fos mRNA expression, indicating the involvement of STAT5A in integrin-mediated c-fos transcription. Thus these data present a new integrin-dependent signaling mechanism involving the JAK/STAT pathway in response to cell-matrix interaction.

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   These authors contributed equally to this work.
   Corresponding author. E-mail address: pegoraro{at}sinet.it.

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Molecular Biology of the Cell
Vol. 10, 3463-3471, October 1999
Copyright © 1999 by The American Society for Cell Biology

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