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A more recent version of this article appeared on May 11, 2001
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M100426200v1
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Papers In Press, published online ahead of print February 6, 2001
J. Biol. Chem, 10.1074/jbc.M100426200
Submitted on January 17, 2001
Revised on February 6, 2001
Accepted on February 6, 2001

Oxidative protein cross-linking reactions involving L-tyrosine in transforming growth factor-beta1-stimulated fibroblasts

Jose M. Larios, Rohit Budhiraja, Barry L. Fanburg, and Victor J. Thannickal

Pulmonary and Critical Care Division, New England Medical Center, Boston, MA 02111

Corresponding Author: vthannickal{at}lifespan.org

The mechanisms by which ligand-stimulated generation of reactive oxygen species (ROS) in non-phagocytic cells mediate biologic effects are largely unknown. The pro-fibrotic cytokine, transforming growth factor-b1 (TGF-beta 1), generates extracellular hydrogen peroxide (H2O2) in contrast to intracellular ROS production by certain mitogenic growth factors in human lung fibroblasts. To determine if tyrosine residues in fibroblast-derived extracellular matrix (ECM) proteins may be targets of H2O2-mediated, dityrosine-dependent cross-linking reactions in response to TGF-b1, we utilized fluorophore-labeled tyramide, a structurally related phenolic compound that forms dimers with tyrosine, as a probe to detect such reactions under dynamic cell culture conditions. With this approach, a distinct pattern of fluorescent labeling that appears to preferentially target extracellular matrix (ECM) proteins was observed in TGF-beta 1-treated cells, but not in control cells. This reaction required the presence of a heme peroxidase and was inhibited by catalase or diphenyliodonium (a flavoenzyme inhibitor), similar to the effect on TGF-beta 1-induced dityrosine formation. Exogenous addition of H2O2 to control cells that do not release extracellular H2O2 produced a similar fluorescent labeling reaction. These results support the concept that, in the presence of heme peroxidases in-vivo, TGF-beta 1-induced H2O2 production by fibroblasts may mediate oxidative dityrosine-dependent cross-linking of ECM protein(s). This effect may be important in the pathogenesis of human fibrotic diseases characterized by over-expression/activation of TGF-beta 1.


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