Volume 8, No 3, Sep 1998

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 8 Issue 3, September 1998: 179-186

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Cell surface activation of progelatinase A (proMMP-2) and cell migration.

Nagase H.

Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160, USA. Correspondence: Nagase H.(Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160, USA. )

Gelatinase A (MMP-2) is considered to play a critical role in cell migration and invasion. The proteinase is secreted from the cell as an inactive zymogen. In vivo it is postulated that activation of progelationase A (proMMP-2) takes place on the cell surface mediated by membrane-type matrix metalloproteinases (MT-MMPs). Recent studies have demonstrated that proMMP-2 is recruited to the cell surface by interacting with tissue inhibitor of metalloproteinases-2 (TIMP-2) bound to MT1-MMP by forming a ternary complex. Free MT1-MMP closely located to the ternary complex then activates proMMP-2 on the cell surface. MT1-MMP is found in cultured invasive cancer cells at the invadopodia. The MT-MMP/TIMP-2/MMP-2 system thus provides localized expression of proteolysis of the extracellular matrix required for cell migration.

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