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YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site

Shaija Samuel1, Katherine K Beifuss, Lori R Bernstein

  • 1Department of Molecular and Cellular Medicine, Texas A&M University System Health Science Center, College Station, TX 77843-1114, USA.

Biochimica Et Biophysica Acta
|September 8, 2007
PubMed

Insights

Y-box binding protein-1 (YB-1) represses matrix metalloproteinase-13 (MMP-13) gene activation by binding to its promoter. This discovery reveals a new regulatory mechanism for MMP-13 in cancer and arthritis.

Area of Science:

  • Molecular Biology
  • Biochemistry

Background:

  • Matrix metalloproteinases (MMPs) degrade the extracellular matrix, crucial in development, tissue remodeling, and disease.
  • MMP-13 is implicated in the pathogenesis of invasive cancers and arthritis.

Purpose of the Study:

  • To identify novel regulators of MMP-13 transactivation.
  • To investigate the role of Y-box binding protein-1 (YB-1) in MMP-13 gene expression.

Main Methods:

  • DNA affinity chromatography to assess YB-1 binding to the MMP-13 promoter AP-1 site.
  • Chromatin immunoprecipitation assays to confirm YB-1 binding in vivo.
  • Reporter assays to evaluate YB-1's effect on MMP-13 promoter activity.

Main Results:

  • YB-1 binds to the activator protein-1 (AP-1) DNA sequence in the MMP-13 promoter in vitro.
  • YB-1 binds to the MMP-13 gene promoter in living cells.
  • YB-1 represses tumor promoter-induced MMP-13 promoter transactivation.

Conclusions:

  • YB-1 acts as a novel repressor of MMP-13 transactivation.
  • This study demonstrates, for the first time, YB-1 binding to a mammalian AP-1 target gene promoter in vitro and in vivo.
  • YB-1 regulation of the MMP-13 promoter offers new insights into cancer and arthritis pathogenesis.

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