Matrix metalloproteinases
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1 Matrix metalloproteinases,, Domain 2-2. TIMPs 2-3. MMPs, 3. 4.
2 1. Collagens, proteoglycans (Extracellular matrix, ECM),,. matrixins matrix metalloproteinases (MMPs) [1, 2]. MMPs,, cytokines [3]. MMP α-macroglobulins tissue inhibitors of metalloproteinases (TIMPs). review matrixin,. MMPsprepro- pro-mmp [2]. 20 MMP Fig.1 domain motifs MMPs domaintable I. domain propeptide domain (80 ), PRCG(V/N)PD. Cyspro-MMP [4]. Catalytic domain (170 ) HEXXHXXGXXH Met-turn methionine [5]. C- hemopexin domain (210 )4 β-propeller. hemopexin domain collagens collagenases [6]. MMP-2 hemopexin domainmt1-mmp pro-mmp-2 [7]. MMP-23, hemopexin domain cysteine-rich, proline-rich IL-1 [8]. catalytic hemopexin domain proline-rich linker
3 , transmembrane domainmt- MMPs [9]. I. MMPs [2] Protein MMP Domain composition Collagenase 1 MMP-1 B Gelatinase A MMP-2 C Stromelysin 1 MMP-3 B Matrilysin MMP-7 A Collagenase 2 MMP-8 B Gelatinase B MMP-9 D Stromelysin 2 MMP-10 B Stromelysin 3 MMP-11 E Macrophage elastase MMP-12 B Collagenase 3 MMP-13 B MT1-MMP MMP-14 F MT2-MMP MMP-15 F MT3-MMP MMP-16 F MT4-MMP MMP-17 F Collagenase 4 (Xenopus) MMP-18 B (No trivial name) MMP-19 B Enamelysin MMP-20 B XMMP (Xenopus) MMP-21 G CMMP (chicken) MMP-22 B No trivial name) MMP-23 H. 1. MMP Domain [2]
4
5 4. 1. McCawley, L. J., and Matrisian, L. M. (2000) Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol. Med. Today 6, Nagase, H., and Woessner, J. F. Jr. (1999) Matrix metalloproteinases. J. Biol. Chem. 274, Fini, M. E., Cook, J. R., Mohan, R., and Brinckerhoft, C. E. (1998) in Matrix Metalloproteinases (Parks, W. C., and Mecham, R. P., eds) pp , Academic Press, San Diego. 4. Van Wart, H. E., and Birkedal-Hansen, H. (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. U. S. A. 87, Bode, W., Gomis-Ruth, F. X., and Stocker, W. (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331, Bode, W. (1995) A helping hand for collagenases: the haemopexin-like domain. Structure 3, Strongin, A. Y., Collier, I., Bannikov, G., Marmer, B. L., Grant, G. A., and Goldberg, G. I. (1995) Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, Gururajan, R., Grenet, J., Lahti, J. M., and Kidd, V. J. (1998) Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3. Genomics 52, Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., and Seiki, M. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370,
6 10. Gomez, D. E., Alonso, D. F., Yoshiji, H., and Thorgeirsson, U. P. (1997) Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur. J. Cell Biol. 74, Murphy, A. N., Unsworth, E. J., and Stetler-Stevenson, W. G. (1993) Tissue inhibitor of metalloproteinases-2 inhibits bfgf-induced human microvascular endothelial cell proliferation. J. Cell. Physiol. 157, Chesler, L., Golde, D. W., Bersch, N., and Johnson, M. D. (1995) Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1. Blood 86, Smith, M. R., Kung, H. F., Durum, S. K., Colburn, N. H., and Sun, Y. (1997) TIMP- 3 induces cell death by stabilizing TNF-alpha receptors on the surface of human colon carcinoma cells. Cytokine 9, Ahonen, M., Baker, A. H., and Ka ha ri, V. M. (1998) Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells. Cancer Res. 58, Felbor, U., and Weber, B. H. (1998) Sorsby's fundus dystrophy. A genetically homogeneous disease Ophthalmologe 95,
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