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Originally published In Press as doi:10.1074/jbc.M205630200 on September 18, 2002

J. Biol. Chem., Vol. 277, Issue 47, 44854-44863, November 22, 2002
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Signaling Pathways Transduced through the Elastin Receptor Facilitate Proliferation of Arterial Smooth Muscle Cells*

Satsuki Mochizuki, Bertrand Brassart, and Aleksander HinekDagger

From the Cardiovascular Research Program, The Hospital for Sick Children and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G 1X8, Canada

In this report we demonstrate that soluble peptides, elastin degradation products stimulate proliferation of arterial smooth muscle cells. We show that these effects are due to generation of intracellular signals transduced through the cell surface elastin receptor, which consists of peripheral 67-kDa elastin-binding protein (EBP) (spliced variant of beta -galactosidase), immobilized to the transmembrane sialidase and the protective protein. We found that elastin receptor-transduced signaling triggers activation of G proteins, opening of L-type calcium channels, and a sequential activation of tyrosine kinases: FAK, c-Src, platelet-derived growth factor-receptor kinase and then Ras-Raf-MEK1/2-ERK1/2 phosphorylation cascade. This, in turn, causes an increase in expression of cyclins and cyclin-dependent kinases, and a consequent increase in cellular proliferation. The EBP-transduced signals also induce tyrosine kinase-dependent phosphorylation of beta -tubulin, LC3, microtubule-associated protein 1, and alpha -actin and troponin-T, which could be linked to reorganization of cytoskeleton. We have also disclosed that induction of these signals can be abolished by anti-EBP antibody or by galactosugars, which cause shedding of EBP from the cell surface. Moreover, elastin-derived peptides did not induce proliferation of EBP-deficient cells derived from patients bearing a nonsense mutation of the beta -galactosidase gene or sialidase-deficient cells from patients with congenital sialidosis.

* This work was supported in part by the Canadian Institute of Health Research (Grant PG 13920) and by the Stroke Foundation of Ontario (Grant NA 4381) (to A. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger A Career Investigator of the Heart and Stroke Foundation of Ontario (CI 4198). To whom correspondence should be addressed: Cardiovascular Research Program, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada. Tel.: 416-813-6725; Fax: 416-813-7480; E-mail: alek.hinek@sickkids.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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