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| MMP-19 shares a typical MMP structural domain, containing the signal peptide, propeptide, catalytic domain, hinge region, and four hemopexin repeats (Pendás et al., 1997). |
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Description | MMP-19 is a secreted protein. It contains a signal peptide for targeting to secretory vesicles. Like most secreted MMPs, MMP-19 is translated and secreted as catalytic inactive proproteins (zymogens), which needed to be activated by proteolytic cleavage of the propeptide region by other extracellular matrix (EMC) proteinases (Ra and Parks, 2007). MMP-19 is a zinc-dependent endopeptidase. The catalytic domain contains the active site for zinc ion binding and functions in catalytic activity such as substrate degradation. The hemopexin domain is responsible for substrate recognition (Ra and Parks, 2007). The catalytic activities of MMPs were reported to be regulated by tissue inhibitor of metalloproteinases (TIMPs). MMP-19 is reported to be strongly inhibited by TIMP-2, TIMP-3, and TIMP-4, and less efficiently by TIMP-1 (Clark et al., 2008). |
Expression | MMP-19 was found to be expressed in a wide range of normal tissue types, such as nasopharyngeal epithelial cells, lung, breast, skin, intestine, pancreas, spleen, and ovary. MMP-19 was down-regulated or lost during neoplastic progression in nasopharyngeal carcinoma (NPC), mammary gland tumor, skin neoplasm, intestine, and colon cancers (Pendás et al., 1997; Djonov et al., 2001; Impola et al., 2003; Bister et al., 2004; Chan et al., 2011). |
Localisation | MMP-19 is located in the cytoplasm and secreted into the extracellular matrix. |
Function | MMP-19 is a member of the MMP family of zinc-dependent endopeptidases. The catalytic domain responsible for degradation of various components of the ECM include collagen type IV, nidogen-1, fibronectin, tenascin-C isoform, aggrecan, and laminin-5-gamma-2-chain (Stracke et al., 2000; Shiomi et al., 2010). MMP-19 is involved in many physiological activities such as cell proliferation, migration, and anti-angiogenesis. |
Differential expression of three matrix metalloproteinases, MMP-19, MMP-26, and MMP-28, in normal and inflamed intestine and colon cancer. |
Bister VO, Salmela MT, Karjalainen-Lindsberg ML, Uria J, Lohi J, Puolakkainen P, Lopez-Otin C, Saarialho-Kere U. |
Dig Dis Sci. 2004 Apr;49(4):653-61. |
PMID 15185874 |
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Matrix metalloproteinase-19 inhibits growth of endothelial cells by generating angiostatin-like fragments from plasminogen. |
Brauer R, Beck IM, Roderfeld M, Roeb E, Sedlacek R. |
BMC Biochem. 2011 Jul 25;12:38. doi: 10.1186/1471-2091-12-38. |
PMID 21787393 |
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Catalytic activity of Matrix metalloproteinase-19 is essential for tumor suppressor and anti-angiogenic activities in nasopharyngeal carcinoma. |
Chan KC, Ko JM, Lung HL, Sedlacek R, Zhang ZF, Luo DZ, Feng ZB, Chen S, Chen H, Chan KW, Tsao SW, Chua DT, Zabarovsky ER, Stanbridge EJ, Lung ML. |
Int J Cancer. 2011 Oct 15;129(8):1826-37. doi: 10.1002/ijc.25855. Epub 2011 Apr 1. |
PMID 21165953 |
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The regulation of matrix metalloproteinases and their inhibitors. |
Clark IM, Swingler TE, Sampieri CL, Edwards DR. |
Int J Biochem Cell Biol. 2008;40(6-7):1362-78. doi: 10.1016/j.biocel.2007.12.006. Epub 2007 Dec 24. (REVIEW) |
PMID 18258475 |
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MMP-19: cellular localization of a novel metalloproteinase within normal breast tissue and mammary gland tumours. |
Djonov V, Hogger K, Sedlacek R, Laissue J, Draeger A. |
J Pathol. 2001 Sep;195(2):147-55. |
PMID 11592092 |
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Matrix metalloproteinase-19 is expressed by proliferating epithelium but disappears with neoplastic dedifferentiation. |
Impola U, Toriseva M, Suomela S, Jeskanen L, Hieta N, Jahkola T, Grenman R, Kahari VM, Saarialho-Kere U. |
Int J Cancer. 2003 Mar 1;103(6):709-16. |
PMID 12516088 |
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Earlier onset of tumoral angiogenesis in matrix metalloproteinase-19-deficient mice. |
Jost M, Folgueras AR, Frerart F, Pendas AM, Blacher S, Houard X, Berndt S, Munaut C, Cataldo D, Alvarez J, Melen-Lamalle L, Foidart JM, Lopez-Otin C, Noel A. |
Cancer Res. 2006 May 15;66(10):5234-41. |
PMID 16707448 |
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Overexpression of asparagine synthetase and matrix metalloproteinase 19 confers cisplatin sensitivity in nasopharyngeal carcinoma cells. |
Liu RY, Dong Z, Liu J, Zhou L, Huang W, Khoo SK, Zhang Z, Petillo D, Teh BT, Qian CN, Zhang JT. |
Mol Cancer Ther. 2013 Oct;12(10):2157-66. doi: 10.1158/1535-7163.MCT-12-1190. Epub 2013 Aug 16. |
PMID 23956056 |
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Structure of the human MMP-19 gene. |
Mueller MS, Mauch S, Sedlacek R. |
Gene. 2000 Jul 11;252(1-2):27-37. |
PMID 10903435 |
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Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. |
Pendas AM, Knauper V, Puente XS, Llano E, Mattei MG, Apte S, Murphy G, Lopez-Otin C. |
J Biol Chem. 1997 Feb 14;272(7):4281-6. |
PMID 9020145 |
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Control of matrix metalloproteinase catalytic activity. |
Ra HJ, Parks WC. |
Matrix Biol. 2007 Oct;26(8):587-96. Epub 2007 Jul 7. (REVIEW) |
PMID 17669641 |
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Matrix metalloproteinase 19 processes the laminin 5 gamma 2 chain and induces epithelial cell migration. |
Sadowski T, Dietrich S, Koschinsky F, Ludwig A, Proksch E, Titz B, Sedlacek R. |
Cell Mol Life Sci. 2005 Apr;62(7-8):870-80. |
PMID 15868410 |
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Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis. |
Sedlacek R, Mauch S, Kolb B, Schatzlein C, Eibel H, Peter HH, Schmitt J, Krawinkel U. |
Immunobiology. 1998 Feb;198(4):408-23. |
PMID 9562866 |
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Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases. |
Shiomi T, Lemaitre V, D'Armiento J, Okada Y. |
Pathol Int. 2010 Jul;60(7):477-96. doi: 10.1111/j.1440-1827.2010.02547.x. (REVIEW) |
PMID 20594269 |
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Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). |
Stracke JO, Fosang AJ, Last K, Mercuri FA, Pendas AM, Llano E, Perris R, Di Cesare PE, Murphy G, Knauper V. |
FEBS Lett. 2000 Jul 28;478(1-2):52-6. |
PMID 10922468 |
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Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1. |
Titz B, Dietrich S, Sadowski T, Beck C, Petersen A, Sedlacek R. |
Cell Mol Life Sci. 2004 Jul;61(14):1826-33. |
PMID 15241558 |
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