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

FEBS Letters

Kinoshita, Takeshi¹  Imai, Kazushi²  Okada, Yasunori²  Takino, Takahisa¹  Seiki, Motoharu¹  Sato, Hiroshi¹  Stetler Stevenson, William G.³ 

[1] Department of Molecular Virology and Oncology, cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920, Japan;Department of Molecular Immunology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920, Japan;Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, MD, USA

关键词: Metalloproteinase;    Activation;    Binding;    MT-MMP;    membrane-type matrix metalloproteinase;    TIMP;    tissue inhibitor of metalloproteinases;    TPA;    12-O-tetradecanoylphorbol acetate;   

DOI  :  10.1016/0014-5793(96)00389-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown