マトリックスメタロプロテイナーゼ-2
(ゼラチナーゼA から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2024/07/17 01:42 UTC 版)
マトリックスメタロプロテイナーゼ-2（英: matrix metalloproteinase-2、略称: MMP-2）、または72 kDa IV型コラゲナーゼ（英: 72 kDa type IV collagenase）、ゼラチナーゼA（英: gelatinase A）は、ヒトではMMP2遺伝子にコードされる酵素である[5]。MMP2遺伝子は、16番染色体のq12.2に位置する[6]。
- ^ a b c GRCh38: Ensembl release 89: ENSG00000087245 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031740 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
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- ^ a b c Björklund M, Koivunen E (May 2005). “Gelatinase-mediated migration and invasion of cancer cells”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1755 (1): 37–69. doi:10.1016/j.bbcan.2005.03.001. hdl:10138/22049. PMID 15907591.
- ^ a b c d Mook OR, Frederiks WM, Van Noorden CJ (December 2004). “The role of gelatinases in colorectal cancer progression and metastasis”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1705 (2): 69–89. doi:10.1016/j.bbcan.2004.09.006. PMID 15588763.
- ^ Jacob A, Prekeris R (2015). “The regulation of MMP targeting to invadopodia during cancer metastasis”. Frontiers in Cell and Developmental Biology 3: 4. doi:10.3389/fcell.2015.00004. PMC 4313772. PMID 25699257.
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- ^ Montgomery AM, Reisfeld RA, Cheresh DA (September 1994). “Integrin alpha v beta 3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen”. Proceedings of the National Academy of Sciences of the United States of America 91 (19): 8856–60. Bibcode: 1994PNAS...91.8856M. doi:10.1073/pnas.91.19.8856. PMC 44705. PMID 7522323.
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- ^ Detry B, Erpicum C, Paupert J, Blacher S, Maillard C, Bruyère F, Pendeville H, Remacle T, Lambert V, Balsat C, Ormenese S, Lamaye F, Janssens E, Moons L, Cataldo D, Kridelka F, Carmeliet P, Thiry M, Foidart JM, Struman I, Noël A (May 2012). "Matrix metalloproteinase-2 governs lymphatic vessel formation as an interstitial collagenase". Blood. 119 (21): 5048–56. doi:10.1182/blood-2011-12-400267. PMID 22490679。
- ^ Massagué J (July 2008). “TGFbeta in Cancer”. Cell 134 (2): 215–30. doi:10.1016/j.cell.2008.07.001. PMC 3512574. PMID 18662538.
- ^ Bergers G, Brekken R, McMahon G, Vu TH, Itoh T, Tamaki K, Tanzawa K, Thorpe P, Itohara S, Werb Z, Hanahan D (October 2000). “Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis”. Nature Cell Biology 2 (10): 737–44. doi:10.1038/35036374. PMC 2852586. PMID 11025665.
- ^ Rojiani MV, Alidina J, Esposito N, Rojiani AM (2010). “Expression of MMP-2 correlates with increased angiogenesis in CNS metastasis of lung carcinoma”. International Journal of Clinical and Experimental Pathology 3 (8): 775–81. PMC 2993228. PMID 21151391.
- ^ McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM (August 2000). “Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3”. Science 289 (5482): 1202–6. Bibcode: 2000Sci...289.1202M. doi:10.1126/science.289.5482.1202. PMID 10947989.
- ^ a b Bein K, Simons M (October 2000). “Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity”. J. Biol. Chem. 275 (41): 32167–73. doi:10.1074/jbc.M003834200. PMID 10900205.
- ^ Morgunova E, Tuuttila A, Bergmann U, Tryggvason K (May 2002). “Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2”. Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7414–9. Bibcode: 2002PNAS...99.7414M. doi:10.1073/pnas.102185399. PMC 124245. PMID 12032297.
- ^ Overall CM, Tam E, McQuibban GA, Morrison C, Wallon UM, Bigg HF, King AE, Roberts CR (December 2000). “Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation”. J. Biol. Chem. 275 (50): 39497–506. doi:10.1074/jbc.M005932200. PMID 10991943.
- ^ a b Bigg HF, Shi YE, Liu YE, Steffensen B, Overall CM (June 1997). “Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2”. J. Biol. Chem. 272 (24): 15496–500. doi:10.1074/jbc.272.24.15496. PMID 9182583.
- ^ a b Kai HS, Butler GS, Morrison CJ, King AE, Pelman GR, Overall CM (December 2002). “Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain”. J. Biol. Chem. 277 (50): 48696–707. doi:10.1074/jbc.M209177200. PMID 12374789.
[続きの解説]
「マトリックスメタロプロテイナーゼ-2」の続きの解説一覧
- 1 マトリックスメタロプロテイナーゼ-2とは
- 2 マトリックスメタロプロテイナーゼ-2の概要
- 3 機能
- 4 関連文献
- 5 外部リンク
- マトリックスメタロプロテイナーゼ-2のページへのリンク
