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Hydrogen peroxide‐mediated, lysyl oxidase‐dependent chemotaxis of vascular smooth muscle cells
Author(s) -
Li Wande,
Liu Guanmei,
Chou IihNan,
Kagan Herbert M.
Publication year - 2000
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 - 10.1002/1097-4644(20000915)78:4<550::aid-jcb4>3.0.co;2-8
Subject(s) - chemokinesis , lysyl oxidase , chemotaxis , vascular smooth muscle , chemistry , elastin , biochemistry , microbiology and biotechnology , enzyme , biology , smooth muscle , receptor , genetics , endocrinology
Lysyl oxidase (LO), an enzyme secreted by vascular smooth muscle cells (VSMC), initiates the covalent crosslinking of polypeptide chains within collagen and elastin. The present study reveals that purified LO strongly induces directional migration of VSMC in an in vitro assay system. LO‐dependent chemotaxis, but not chemokinesis, was abolished by β‐aminopropionitrile, an active site inhibitor of LO, or by catalase, as well as by prior heat denaturation. This indicates that the H 2 O 2 product of amine oxidation by LO is critical to the expression of its chemotactic activity. The results indicate that the chemotactic response requires direct access between LO and a substrate molecule (or molecules) tightly associated with the VSMC. The addition of LO to VSMC elevated the levels of intracellular H 2 O 2 , enhanced stress fiber formation, and focal adhesion assembly, is consistent with the induction of the chemotactic response. J. Cell. Biochem. 78:550–557, 2000. © 2000 Wiley‐Liss, Inc.