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Cell surface association of matrix metalloproteinase-9 (gelatinase B)

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Abstract

Matrix metalloproteinase (MMP)-9 (gelatinase B) belongs to the MMP family of zinc-dependent endopeptidases that has been associated with tumor cell invasion and metastasis and tumor-induced angiogenesis. As a secreted MMP, pro-MMP-9 is released into the extracellular environment by both tumor and stroma cells, where it fulfills its proteolytic functions degrading both extracellular matrix (ECM) and non-ECM proteins. A major dilemma in our understanding of MMP-9 function is how the released protease is targeted to the right location and how its activity is controlled at the pericellular space. It has been proposed that MMP-9 interact with cell surface components and that this type of interaction positively regulates enzymatic activation and activity. However, recent evidence shows that association of MMP-9 with the cell surface is mediated by a distinct array of surface proteins that serve to regulate multiple aspects of the enzyme function including localization, inhibition and internalization. How these distinct mechanisms regulate the overall MMP-9 activity at the pericellular space remains an important goal in our understanding of MMP-9 function at the cell surface. Furthermore, the study of surface-associated MMP-9 imposes new conceptual and methodological challenges with particular consideration to the unique structural and functional characteristics of this key enzyme.

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Authors and Affiliations

  1. Department of Pathology, School of Medicine, USA

    Rafael Fridman & Marta Toth

  2. Proteases and Cancer Program, Karmanos Cancer Institute, Wayne State University, Detroit, MI, 48201, USA

    Rafael Fridman & Shahriar Mobashery

  3. Department of Chemistry, Wayne State University, Detroit, MI, 48201, USA

    Samy O. Meroueh & Shahriar Mobashery

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  1. Rafael Fridman
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Fridman, R., Toth, M., Chvyrkova, I. et al. Cell surface association of matrix metalloproteinase-9 (gelatinase B). Cancer Metastasis Rev 22, 153–166 (2003). https://doi.org/10.1023/A:1023091214123

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