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PKC‐MEK‐MAPK‐dependent signal transduction pathway mediates the stimulation of lysyl oxidase expression by serum and PDGF in rat aortic smooth muscle cells
Author(s) -
SmithMungo Lynda,
Kagan Herbert M.
Publication year - 2002
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10181
Subject(s) - lysyl oxidase , platelet derived growth factor receptor , signal transduction , stimulation , mapk/erk pathway , microbiology and biotechnology , protein kinase c , chemistry , smooth muscle , medicine , endocrinology , biology , growth factor , biochemistry , enzyme , receptor
Abstract Lysyl oxidase (LO) plays a critical role in the stabilization and insolubilization of fibrous structural proteins of the extracellular matrix and has been implicated in the suppression of Ras‐induced tumorigenesis. Several prior reports demonstrate that the expression of this catalyst is strongly influenced by a variety of effectors of cell function and is responsive to the growth state of fibrogenic cells. Using specific inhibitors of components of signal transduction pathways, the present study reveals that a PKC‐MEK‐MAPK‐dependent pathway is critical to the enhanced expression of the LO gene in response to variations in the levels of the serum component of the growth medium and in response to platelet‐derived growth factor (PDGF). PDGF is shown to be the major component of fetal bovine serum, which stimulates the activity of a LO promoter construct. J. Cell. Biochem. 85: 775–784, 2002. © 2002 Wiley‐Liss, Inc.