Membrane type-matrix metalloproteinases and tumor progression

被引:121
作者
Sounni, NE [1 ]
Noel, A [1 ]
机构
[1] Univ Liege, Lab Tumor & Dev Biol, B-4000 Liege, Belgium
关键词
MT-MMP; protease inhibitors; cell signaling; tumor angiogenesis; cancer;
D O I
10.1016/j.biochi.2004.07.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Matrix metalloproteinases (MMPs) are a family of zinc endopeptidases that process growth factors, growth factor binding proteins, cell surface proteins, degrade extracellular matrix (ECM) components and thereby play a central role in tissue remodeling and tumor progression. Membrane-type matrix metalloproteinases (MT-MMPs) are a recently discovered subgroup of intrinsic plasma membrane proteins. Their functions have been extended from pericellular proteolysis and control of cell migration to cell signaling, control of cell proliferation and regulation of multiple stages of tumor progression including growth and angiogenesis. This review sheds light on the new functions of MT-MMPs and their inhibitors in tumor development and angiogenesis, and presents recent investigations that document their influence on various cell functions. (c) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:329 / 342
页数:14
相关论文
共 183 条
[81]   Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor [J].
Maquoi, E ;
Sounni, NE ;
Devy, L ;
Olivier, F ;
Frankenne, F ;
Krell, HW ;
Grams, F ;
Foidart, JM ;
Noël, A .
CLINICAL CANCER RESEARCH, 2004, 10 (12) :4038-4047
[82]  
Masui T, 2003, CLIN CANCER RES, V9, P1779
[83]   Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils [J].
Matsuda, A ;
Itoh, Y ;
Koshikawa, N ;
Akizawa, T ;
Yana, I ;
Seiki, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (38) :36350-36357
[84]   Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3 [J].
McQuibban, GA ;
Gong, JH ;
Tam, EM ;
McCulloch, CAG ;
Clark-Lewis, I ;
Overall, CM .
SCIENCE, 2000, 289 (5482) :1202-1206
[85]   Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo [J].
McQuibban, GA ;
Gong, JH ;
Wong, JR ;
Wallace, JL ;
Clark-Lewis, I ;
Overall, CM .
BLOOD, 2002, 100 (04) :1160-1167
[86]   Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1 [J].
McQuibban, GA ;
Butler, GS ;
Gong, JH ;
Bendall, L ;
Power, C ;
Clark-Lewis, I ;
Overall, CM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (47) :43503-43508
[87]   Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer [J].
Michael, M ;
Babic, B ;
Khokha, R ;
Tsao, M ;
Ho, J ;
Pintilie, M ;
Leco, K ;
Chamberlain, D ;
Shepherd, FA .
JOURNAL OF CLINICAL ONCOLOGY, 1999, 17 (06) :1802-1808
[88]   Human membrane type-2 matrix metalloproteinase is defective in cell-associated activation of progelatinase A [J].
Miyamori, H ;
Takino, T ;
Seiki, M ;
Sato, H .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 267 (03) :796-800
[89]   Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases [J].
Miyamori, H ;
Takino, T ;
Kobayashi, Y ;
Tokai, H ;
Itoh, Y ;
Seiki, M ;
Sato, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (30) :28204-28211
[90]   Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway [J].
Morrison, CJ ;
Butler, GS ;
Bigg, HF ;
Roberts, CR ;
Soloway, PD ;
Overall, CM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (50) :47402-47410