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Papers In Press, published online ahead of print June 12, 2003
J. Biol. Chem, 10.1074/jbc.M301931200
Submitted on February 24, 2003
Revised on June 10, 2003
Accepted on June 12, 2003

K-Ras regulates the steady-state expression of matrix metalloproteinase 2 in fibroblasts

Jinhui Liao, Janice C. Wolfman, and Alan Wolfman

Dept. Cell Biology, NC10, Cleveland Clinic Foundation, Cleveland, OH 44195

Corresponding Author: wolfmaa{at}ccf.org

Fibroblasts constitutively express MMP-2 which specifically cleaves type IV collagen, a major structural component of basement membranes. Expression of a dominant negative Ras protein significantly inhibited MMP-2 transcription, thereby suggesting a role for steady-state Ras function in the regulation of MMP-2 expression. Kirsten-Ras (K-Ras) knockout fibroblasts expressed undetectable basal levels of MMP-2, whereas N-Ras knockout fibroblasts expressed constitutive levels of MMP-2 similar to that observed in wild-type control fibroblasts. The transcription of MMP-2 was significantly increased by transient expression of c-K(B)-Ras, but not c-K(A)-Ras. Experimental results using pharmacological inhibitors, dominant negative constructs and AKT1 negative mouse embryo fibroblasts, suggest that steady-state MMP-2 expression is regulated by c-K(B)-Ras through a PI3K:AKT1-dependent, steady-state signaling pathway. Since the majority of the MMP-2 assays were performed using conditioned media from serum-starved fibroblasts, these data also highlight our previous observations that Ras proteins have functions in the absence of acute mitogenic stimulation. This is the first demonstration of a specific steady-state function attributable to the c-K(B)-Ras isoform.


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