REVIEW PAPER
Metalloproteinases of the extracellular matrix and their inhibitors
 
More details
Hide details
1
Faculty of Biotechnology and Environment Sciences, The John Paul II Catholic University of Lublin, Lublin, Poland
 
2
Department of General Surgery, Independent Public Hospital and Health Care Center in Lubartów, Lublin, Poland
 
3
Department of Molecular Biology, Institute of Biotechnology, The John Paul II Catholic University of Lublin, Lublin, Poland
 
 
Submission date: 2016-01-19
 
 
Final revision date: 2016-03-09
 
 
Acceptance date: 2016-03-25
 
 
Publication date: 2016-07-20
 
 
BioTechnologia 2016;97(2):129-136
 
KEYWORDS
TOPICS
ABSTRACT
The dynamic equilibrium between the synthesis and degradation of the extracellular matrix is to a large extent mediated by matrix metalloproteinase (MMP) enzymes, which are antagonized by tissue inhibitors of metalloproteinases (TIMPs). Tissue-degrading enzymes of the metalloproteinase family have been implicated in the pathogenesis of several conditions involving the extracellular matrix. MMPs are a family of zinc-dependent endopeptidases capable of degrading practically all components of the extracellular matrix. Recent insights suggest that MMPs may also have a broader spectrum of functions, including regulation of the inflammatory response and cytokine signaling. MMPs have been subdivided according to their main degradation activity and the continuously growing list of known substrates. Metalloproteinases are promising drug targets, and they are subjected to pharmacological inhibition by clinically available drugs such as tetracyclines and bisphosphonates. Interest in MMPs has recently increased, because their expression is frequently related to tumor progression. As such, metalloproteinases have diagnostic potential as markers to predict the outcome of disease processes. This review introduces the members of the MMP family and discusses their domain structure and function, their significance in physiology and pathology and the mechanism of inhibition by TIMPs.
REFERENCES (20)
1.
Dziankowska-Bartkowiak B., Waszczykowska E., Żebrowska A. (2004) The role of metalloproteinases and their inhibitors in the pathomechanism of skin diseases. Alerg. Astma Immun. 9(2): 71-79 (in Polish).
 
2.
Filipiak K., Kubiński K., Hellman U., Ramos A., de Pascual- Teresa B. (2014) Human protein kinase CK2 phosphorylates matrix metalloproteinase 2 and inhibits its activity. Chembiochem. 15(13): 1873-1876.
 
3.
Gill S., Parks W. (2008) Metalloproteinases and their inhibitors: Regulators of wound healing. Int. J. Biochem. Cell Biol. 40(6-7): 1334-1347.
 
4.
Gorman J., Ispanovic E., Haas T. (2011) Regulation of matrix metalloproteinase expression. Drug Discov. Today: Dis. Models 8(1): 5-11.
 
5.
Groblewska M., Mroczko B., Szmitkowski M. (2010) The role of selected matrix metalloproteinases and their inhibitors in colorectal cancer development. Post. Hig. Med. Dośw. 64: 22-30 (in Polish).
 
6.
Klein T., Bischoff R. (2011) Physiology and pathophysiology of matrix metalloproteinases. Amino Acids 41: 271-290.
 
7.
Konopka Ł., Brzezińska-Błaszczyk E. (2008) Role of matrix metalloproteinases in oral diseases – New therapeutic opportunities. Dent. Med. Probl. 45(3): 229-235 (in Polish).
 
8.
Kowalski M., Walczak A., Majsterek I. (2008) Matrix metalloproteinases (MMPs): Modern molecular markers of openangle glaucoma diagnosis and therapy. Post. Hig. Med. Dośw. 62: 582-592 (in Polish).
 
9.
Kwiatkowski P., Godlewski J., Śliwińska-Jewsiewicka A., Kmieć Z. (2008) The role of matrix metalloproteinases in tumor invasion. Pol. Ann. Med. 15(1): 66-76 (in Polish).
 
10.
Lipka D., Boratyński J. (2008). Metalloproteinases. Structure and function. Post Hig. Med. Dośw. 62: 328-336 (in Polish).
 
11.
Łukasiewicz M, Mroczko B, Szmitkowski M. (2008) The role of metalloproteinases and their inhibitors in pancreatic cancer. Post Hig. Med. Dośw. 62: 141-147 (in Polish).
 
12.
Murphy G., Nagase H. (2008) Progress in matrix metalloproteinase research. Mol. Aspects Med. 29(5): 290-308.
 
13.
Rottenberger Z., Kolev K. (2011) Matrix metalloproteinases at key junctions in the pathomechanism of stroke. Centr. Eur. J. Biol. 6(4): 471-485.
 
14.
Sariahmetoglu M., Crawford B.D., Leon H., Sawicka J., Li L., Ballermann B.J., Holmes C., Berthiaume L.G., Holt A., Sawicki G., Schultz R. (2007) Regulation of matrix metalloproteinase- 2 (MMP-2) activity by phosphorylation. FASEB J. 21(10): 2486-2495.
 
15.
Śliwowska I., Kopczyński Z. (2005) Matrix metalloproteinases – biochemical characteristics and clinical value determination in breast cancer patients. Współcz. Onkol. 9(8): 327-335 (in Polish).
 
16.
Tallant C., Marrero A., Gomis-Rüth F.X. (2010) Matrix metalloproteinases: Fold and function of their catalytic domains. Biochim. Biophys. Acta 1803: 20-28.
 
17.
Wasilewska A., Taranta-Janusz K., Zoch-Zwierz W., Rybi-Szumińska A., Kołodziejczyk Z. (2009) Role of matrix metalloproteinases (MMP) and their tissue inhibitors (TIMP) in nephrology. Przegl. Lek. 66(9): 485-490 (in Polish).
 
18.
Ziemiańska K., Konopka A., Wilczyński G. (2012) The role of extracellular proteolysis in synaptic plasticity of the central nervous system. Post Hig. Med. Dośw. 66: 968-975 (in Polish).
 
19.
Zygmunt K., Zygmunt L. (2013) The importance of metalloproteinases and their tissue inhibitors in the neoplastic process. Przegl. Med. Uniw. Rzesz. Inst. Leków 3: 410-417 (in Polish).
 
20.
Żebrowski M., Kierus-Gudaj A., Żebrowska A. (2003) The role of metalloproteinases in the pathomechanism of ischemic heart disease. Forum Kardiol. 8(2): 53-57 (in Polish).
 
eISSN:2353-9461
ISSN:0860-7796
Journals System - logo
Scroll to top