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Papers In Press, published online ahead of print November 6, 2001
Department of Pathology, Weill Medical College of Cornell University, New York, NY 10021
Corresponding Author: rtkraeme{at}med.cornell.edu
In response to vascular injury, smooth muscle cells migrate from the media into the intima, where they contribute to the development of neointimal lesions. Increased matrix metalloproteinase (MMP) expression contributes to the migratory response of smooth muscle cells by releasing them from their surrounding extracellular matrix. MMPs may also participate in the remodeling of extracellular matrix in vascular lesions that could lead to plaque weakening and subsequent rupture. Neurotrophins and their receptors, the trk family of receptor tyrosine kinases, are expressed in neointimal lesions, where they induce smooth muscle cell migration. We now report that NGF-induced activation of the trk A receptor tyrosine kinase induces MMP-9 expression in both primary cultured rat aortic smooth muscle cells and in a smooth muscle cell line genetically manipulated to express trk A. The response to NGF was specific for MMP-9 expression, as the expression of MMP-2, MMP-3 or the tissue inhibitor of metalloproteinase-2 (TIMP-2) was not changed. Activation of the Shc/MAP-kinase pathway mediates the induction of MMP-9 in response to NGF, as this response is abrogated in cells expressing a mutant trk A receptor which does not bind Shc and by pretreatment of cells with the MEK-1 inhibitor, U0126. Thus, these results indicate that the neurotrophin/trk receptor system, by virtue of its potent chemotactic activity for smooth muscle cells and its ability to induce MMP-9 expression, is a critical mediator in the remodeling which occurs in the vascular wall in response to injury.
J. Biol. Chem, 10.1074/jbc.M108989200
Submitted on September 17, 2001
Revised on November 5, 2001
Accepted on November 6, 2001
Nerve growth factor activation of Erk-1 and Erk-2 induces matrix metalloproteinase 9 expression in vascular smooth muscle cells
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