Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)

Hiroshi Sato, Takahisa Takino, Takeshi Kinoshita, Kazushi Imai, Yasunori Okada, William G. Stetler Stevenson, Motoharu Seiki

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Abstract

Gelatinase A is secreted as a proenzyme (progelatinase A) which is activated and bound on the surface of tumor and normal cells. We have reported that the expression of a membrane-type-1-matrix metalloproteinase (MT1-MMP) induces activation of progelatinase A. Here we demonstrate that the expression of MT1-MMP in COS-1 cells induces cell-surface binding of progelatinase A which is consequently processed to an intermediate form. Processing from the intermediate to the fully active form is dependent on the gelatinase A concentration. These results suggest that the cell-surface binding concentrates the gelatinase A intermediate form locally to allow autoproteolytic processing to the fully active form.

Original languageEnglish
Pages (from-to)238-240
Number of pages3
JournalFEBS Letters
Volume385
Issue number3
DOIs
Publication statusPublished - 1996 May 6

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Keywords

  • activation
  • binding
  • metalloproteinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Sato, H., Takino, T., Kinoshita, T., Imai, K., Okada, Y., Stetler Stevenson, W. G., & Seiki, M. (1996). Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP). FEBS Letters, 385(3), 238-240. https://doi.org/10.1016/0014-5793(96)00389-4