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Papers In Press, published online ahead of print June 4, 2003
J. Biol. Chem, 10.1074/jbc.M305238200
Submitted on May 19, 2003
Revised on June 4, 2003
Accepted on June 4, 2003

Autocrine growth factor regulation of lysyl oxidase expression in transformed fibroblasts

Amitha H. Palamakumbura, Pascal Sommer, and Philip C. Trackman

Division of Oral Biology, Boston University School of Dental Medicine, Boston, MA 02118

Corresponding Author: trackman{at}bu.edu

Lysyl oxidase catalyzes oxidative deamination of peptidyl lysine and hydroxylsine residues in collagens and lysine residues in elastin to form peptidyl aldehydes that are required for the formation of covalent cross-links in normal extracellular matrix biosynthesis. Lysyl oxidase in addition has tumor suppressor activity, and phenotypic reversion of transformed cell lines is accompanied by increased lysyl oxidase expression. The mechanism of low expression of lysyl oxidase in tumor cells is unknown. The present study investigates the hypothesis that autocrine growth factor pathways maintain low lysyl oxidase expression levels in c-H-ras transformed fibroblasts (RS485 cell line). Autocrine pathways were blocked with suramin, a general inhibitor of growth factor receptor binding, and resulted in more than a 10-fold increase in lysyl oxidase expression and pro-enzyme production. This regulation was found to be reversible, and occurred at the transcriptional level determined using lysyl oxidase promoter/reporter gene assays. Function blocking anti-FGF-2 antibody enhanced lysyl oxidase expression in the absence of suramin. Finally, addition of FGF-2 to suramin treated cells completely reversed suramin stimulation of lysyl oxidase mRNA levels. Data support that an FGF-2 autocrine pathway inhibits lysyl oxidase transcription in the tumorigenic transformed RS485 cell line. This finding may be of therapeutic significance, and in addition provides a new experimental approach to investigate the mechanism of tumor suppressor activity of lysyl oxidase.


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