The Role of Membrane-Type 1 Matrix Metalloproteinase-Substrate Interactions in Pathogenesis

被引:6
作者
Lee, Hyun [1 ,2 ]
Ibrahimi, Lucas [1 ]
Azar, Dimitri T. [3 ]
Han, Kyu-Yeon [3 ]
机构
[1] Univ Illinois, Coll Pharm, Dept Pharmaceut Sci, Chicago, IL 60612 USA
[2] Univ Illinois, Res Resources Ctr, Biophys Core, Chicago, IL 60607 USA
[3] Univ Illinois, Illinois Eye & Ear Infirm, Coll Med, Dept Ophthalmol & Visual Sci, Chicago, IL 60612 USA
基金
美国国家卫生研究院;
关键词
MT1-MMP; MMPs substrates; proteolysis; VEGFR-1; FGFRs; angiogenesis; ENDOTHELIAL GROWTH-FACTOR; APOLIPOPROTEIN-A-I; INTERGLOBULAR DOMAIN; TISSUE INHIBITOR; PROSTATE-CANCER; CELL-ADHESION; COLLAGEN STRUCTURE; MT1-MMP; ACTIVATION; EXPRESSION;
D O I
10.3390/ijms24032183
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
A protease is an enzyme with a proteolytic activity that facilitates the digestion of its substrates. Membrane-type I matrix metalloproteinase (MT1-MMP), a member of the broader matrix metalloproteinases (MMP) family, is involved in the regulation of diverse cellular activities. MT1-MMP is a very well-known enzyme as an activator of pro-MMP-2 and two collagenases, MMP-8 and MMP-13, all of which are essential for cell migration. As an anchored membrane enzyme, MT1-MMP has the ability to interact with a diverse group of molecules, including proteins that are not part of the extracellular matrix (ECM). Therefore, MT1-MMP can regulate various cellular activities not only by changing the extra-cellular environment but also by regulating cell signaling. The presence of both intracellular and extra-cellular portions of MT1-MMP can allow it to interact with proteins on both sides of the cell membrane. Here, we reviewed the MT1-MMP substrates involved in disease pathogenesis.
引用
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页数:16
相关论文
共 136 条
[1]  
Agrawal V, 2011, TISSUE ENG PT A, V17, P2435, DOI [10.1089/ten.tea.2011.0036, 10.1089/ten.TEA.2011.0036]
[2]   Matrix Metalloproteinase Gene Activation Resulting from Disordred Epigenetic Mechanisms in Rheumatoid Arthritis [J].
Araki, Yasuto ;
Mimura, Toshihide .
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2017, 18 (05)
[3]   Matrix metalloproteinases:: New routes to the use of MT1-MMP as a therapeutic target in angiogenesis-related disease [J].
Arroyo, A. G. ;
Genis, L. ;
Gonzalo, P. ;
Matias-Roman, S. ;
Pollan, A. ;
Galvez, B. G. .
CURRENT PHARMACEUTICAL DESIGN, 2007, 13 (17) :1787-1802
[4]   The laminin family [J].
Aumailley, Monique .
CELL ADHESION & MIGRATION, 2013, 7 (01) :48-55
[5]   Membrane type 1 matrix metalloprotease cleaves laminin-10 and promotes prostate cancer cell migration [J].
Bair, EL ;
Chen, ML ;
McDaniel, K ;
Sekiguchi, K ;
Cress, AE ;
Nagle, RB ;
Bowden, GT .
NEOPLASIA, 2005, 7 (04) :380-389
[6]   The FGF family: biology, pathophysiology and therapy [J].
Beenken, Andrew ;
Mohammadi, Moosa .
NATURE REVIEWS DRUG DISCOVERY, 2009, 8 (03) :235-253
[7]   Fibronectin Regulates Wnt7a Signaling and Satellite Cell Expansion [J].
Bentzinger, C. Florian ;
Wang, Yu Xin ;
von Maltzahn, Julia ;
Soleimani, Vahab D. ;
Yin, Hang ;
Rudnicki, Michael A. ;
Rudnicki, A. .
CELL STEM CELL, 2013, 12 (01) :75-87
[8]   TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metal loproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP [J].
Bernardo, MM ;
Fridman, R .
BIOCHEMICAL JOURNAL, 2003, 374 :739-745
[9]   Functions of cell surface heparan sulfate proteoglycans [J].
Bernfield, M ;
Götte, M ;
Park, PW ;
Reizes, O ;
Fitzgerald, ML ;
Lincecum, J ;
Zako, M .
ANNUAL REVIEW OF BIOCHEMISTRY, 1999, 68 :729-777
[10]  
BLOCHBERGER TC, 1992, J BIOL CHEM, V267, P347