Regulation of membrane type-matrix metalloproteinases

被引:140
作者
Hernandez-Barrantes, S [1 ]
Bernardo, M [1 ]
Toth, M [1 ]
Fridman, R [1 ]
机构
[1] Wayne State Univ, Dept Pathol, Detroit, MI 48201 USA
关键词
matrix metalloproteinases; proteases; tumor invasion; stroma;
D O I
10.1006/scbi.2001.0421
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Pericellular proteolysis is a hallmark of tumor cell metastasis. The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a distinctive group of membrane-bound MMPs that are central mediators of surface proteolytic events that regulate tumor cell motility, metastasis and angiogenesis. As membrane-tethered proteases, the MT-MMPs exhibit unique regulatory mechanisms and interactions with metalloproteinase inhibitors and other relevant molecules. This review will focus on new emerging information on the mechanisms that regulate MT-MMP processing, activity and inhibition, and their significance for enzyme function in the tumor microenvironment.
引用
收藏
页码:131 / 138
页数:8
相关论文
共 81 条
  • [1] Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes
    Atkinson, SJ
    Crabbe, T
    Cowell, S
    Ward, RV
    Butler, MJ
    Sato, H
    Seiki, M
    Reynolds, JJ
    Murphy, G
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (51) : 30479 - 30485
  • [2] Bando E, 1998, ONCOL REP, V5, P1483
  • [3] Membrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matter
    Beliën, ATJ
    Paganetti, PA
    Schwab, ME
    [J]. JOURNAL OF CELL BIOLOGY, 1999, 144 (02) : 373 - 384
  • [4] Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    Belkin, AM
    Akimov, SS
    Zaritskaya, LS
    Ratnikov, BI
    Deryugina, EI
    Strongin, AY
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (21) : 18415 - 18422
  • [5] Bigg HF, 2001, CANCER RES, V61, P3610
  • [6] Structural properties of matrix metalloproteinases
    Bode, W
    Fernandez-Catalan, C
    Tschesche, H
    Grams, F
    Nagase, H
    Maskos, K
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 1999, 55 (04) : 639 - 652
  • [7] Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    Brooks, PC
    Stromblad, S
    Sanders, LC
    vonSchalscha, TL
    Aimes, RT
    StetlerStevenson, WG
    Quigley, JP
    Cheresh, DA
    [J]. CELL, 1996, 85 (05) : 683 - 693
  • [8] The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A - A kinetic study
    Butler, GS
    Butler, MJ
    Atkinson, SJ
    Will, H
    Tamura, T
    van Westrum, SS
    Crabbe, T
    Clements, J
    d'Ortho, MP
    Murphy, G
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (02) : 871 - 880
  • [9] Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
    Butler, GS
    Will, H
    Atkinson, SJ
    Murphy, G
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 244 (02): : 653 - 657
  • [10] Human tissue inhibitor of metalloproteinases 3 interacts with both the N- and C-terminal domains of gelatinases A and B - Regulation by polyanions
    Butler, GS
    Apte, SS
    Willenbrock, F
    Murphy, G
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (16) : 10846 - 10851