The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

MMP2  -  matrix metallopeptidase 2 (gelatinase A,...

Canis lupus familiaris

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of MMP2

  • Increased expression of MMP-2, MMP-9 (type IV collagenases/gelatinases), and MT1-MMP in canine X-linked Alport syndrome (XLAS) [1].
  • METHODS AND RESULTS: We measured hemodynamics, LV function, MMP-2 and MMP-9, and TIMP-3 and TIMP-4 in the ischemic zone (IZ) and nonischemic zone (NIZ) after in vivo IR (90 minutes anterior ischemia; 120 minutes reperfusion) in 28 dogs that were randomized to sham, IR controls, and IR plus the ARB valsartan [2].
  • In controls, IR induced LV dysfunction, infarction, and IZ remodeling; increased MMP-9 and decreased TIMP-3 in the IZ compared with the NIZ (low TIMP-3/MMP-9 ratio); and did not change MMP-2 or TIMP-4 [2].
  • We characterized clinical and clinicopathological features, and the involvement of gelatinolytic matrix metalloproteinases (MMP-2 and -9) in canine pulmonary eosinophilia (PE) [3].
  • Therefore, although distinct patterns of expression of MMP-2 and MT-MMP1 were shown by these carcinomas, functional studies by means of zymography would be required to provide useful information on tumour behaviour [4].

High impact information on MMP2

  • MMP-2 activation preceded MT1-MMP upregulation [5].
  • We characterized the role of inflammatory mediators and extracellular signal-regulated kinases (ERKs) in the control of arterialized vein graft expression of MMP-9, MMP-2, and membrane-type 1-MMP (MT1-MMP) and of the tissue inhibitor of metalloproteinases-2 (TIMP-2) [5].
  • In cultured smooth muscle cells, both thrombin and TNF-alpha upregulated MT1-MMP expression; however, only thrombin activated MMP-2 [5].
  • While mast cell density decreased to normal at 24 weeks, both chymase and MMP-2 activity remained increased throughout the entire 24-week period post-MR [6].
  • MMP-1, MMP-2, TIMP-1, TIMP-2, and urokinase-type PA levels in the distribution of the LAD were higher in the laser group than in the control or sham group [7].

Biological context of MMP2


Anatomical context of MMP2

  • Zymography showed that the cell lines produce high levels of MMP-2 and MMP-9, enzymes directly involved in crucial aspects of the metastatic process [10].
  • Synthetic MMP inhibitors as well as recombinant tissue inhibitor of metalloproteinases 2 and 3 suppress the invasion of collagen gels and restore the capacity of C7-caMEK1 cells to form cysts, thereby implicating the membrane type-1 MMP/MMP-2 proteolytic system in epithelial cell invasiveness and loss of multicellular organization [11].
  • MMP-2 was strongly stained in neointima, but very weak in endothelium [12].
  • Immunolabelling for both MMP-2 and MT1-MMP was also seen on the tumour cell membranes [4].
  • MMP-2 and MT1-MMP were mainly expressed in the cytoplasm of carcinoma cells and in fibroblasts [4].

Associations of MMP2 with chemical compounds

  • The cGMP analogue 8-bromo-cGMP (10(-4) mol/L) mimicked the BNP effect, whereas inhibition of protein kinase G by KT5823 (10(-6) mol/L) significantly (P<0.05) attenuated BNP-induced zymographic MMP-2 abundance [13].

Regulatory relationships of MMP2

  • In the present study, we examined necropsy samples of renal cortex from normal and XLAS dogs for MMP-3 and MMP-7 as they have the potential to activate MMP-2 and MMP-9 [14].

Other interactions of MMP2

  • Gelatin zymography revealed increases in 92-kDa MMP-9 activity and 86-kDa MMP-9 activity at the LV pacing site relative to the remote site, whereas MMP-2 activity was unaffected [15].
  • CLINICAL RELEVANCE: These findings suggest that MMP-2, -9, cathepsin S, and TRAP may be important mediators of progressive joint destruction in dogs with CCL rupture [16].


  1. Increased expression of MMP-2, MMP-9 (type IV collagenases/gelatinases), and MT1-MMP in canine X-linked Alport syndrome (XLAS). Rao, V.H., Lees, G.E., Kashtan, C.E., Nemori, R., Singh, R.K., Meehan, D.T., Rodgers, K., Berridge, B.R., Bhattacharya, G., Cosgrove, D. Kidney Int. (2003) [Pubmed]
  2. Improved balance between TIMP-3 and MMP-9 after regional myocardial ischemia-reperfusion during AT1 receptor blockade. Sawicki, G., Menon, V., Jugdutt, B.I. J. Card. Fail. (2004) [Pubmed]
  3. Clinical findings, bronchoalveolar lavage fluid cytology and matrix metalloproteinase-2 and -9 in canine pulmonary eosinophilia. Rajamäki, M.M., Järvinen, A.K., Sorsa, T., Maisi, P. Vet. J. (2002) [Pubmed]
  4. Expression of matrix metalloprotease-2 (MMP-2) and the activator membrane type 1 (MT1-MMP) in canine mammary carcinomas. Papparella, S., Restucci, B., Paciello, O., Maiolino, P. J. Comp. Pathol. (2002) [Pubmed]
  5. Matrix metalloproteinase expression in vein grafts: role of inflammatory mediators and extracellular signal-regulated kinases-1 and -2. Sharony, R., Pintucci, G., Saunders, P.C., Grossi, E.A., Baumann, F.G., Galloway, A.C., Mignatti, P. Am. J. Physiol. Heart Circ. Physiol. (2006) [Pubmed]
  6. Cardiac mast cell- and chymase-mediated matrix metalloproteinase activity and left ventricular remodeling in mitral regurgitation in the dog. Stewart, J.A., Wei, C.C., Brower, G.L., Rynders, P.E., Hankes, G.H., Dillon, A.R., Lucchesi, P.A., Janicki, J.S., Dell'Italia, L.J. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  7. Role of MMPs and plasminogen activators in angiogenesis after transmyocardial laser revascularization in dogs. Li, W., Tanaka, K., Chiba, Y., Kimura, T., Morioka, K., Uesaka, T., Ihaya, A., Sasaki, M., Tsuda, T., Yamada, N. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  8. Remodeling of the vascular tunica media is essential for development of collateral vessels in the canine heart. Cai, W.J., Kocsis, E., Wu, X., Rodríguez, M., Luo, X., Schaper, W., Schaper, J. Mol. Cell. Biochem. (2004) [Pubmed]
  9. Matrix-dependent mechanism of neutrophil-mediated release and activation of matrix metalloproteinase 9 in myocardial ischemia/reperfusion. Lindsey, M., Wedin, K., Brown, M.D., Keller, C., Evans, A.J., Smolen, J., Burns, A.R., Rossen, R.D., Michael, L., Entman, M. Circulation (2001) [Pubmed]
  10. Characterisation of three novel canine osteosarcoma cell lines producing high levels of matrix metalloproteinases. Loukopoulos, P., O'Brien, T., Ghoddusi, M., Mungall, B.A., Robinson, W.F. Res. Vet. Sci. (2004) [Pubmed]
  11. Constitutively active mitogen-activated protein kinase kinase MEK1 disrupts morphogenesis and induces an invasive phenotype in Madin-Darby canine kidney epithelial cells. Montesano, R., Soriano, J.V., Hosseini, G., Pepper, M.S., Schramek, H. Cell Growth Differ. (1999) [Pubmed]
  12. Expression of endothelial nitric oxide synthase in the vascular wall during arteriogenesis. Cai, W.J., Kocsis, E., Luo, X., Schaper, W., Schaper, J. Mol. Cell. Biochem. (2004) [Pubmed]
  13. Brain natriuretic Peptide is produced in cardiac fibroblasts and induces matrix metalloproteinases. Tsuruda, T., Boerrigter, G., Huntley, B.K., Noser, J.A., Cataliotti, A., Costello-Boerrigter, L.C., Chen, H.H., Burnett, J.C. Circ. Res. (2002) [Pubmed]
  14. Dysregulation of renal MMP-3 and MMP-7 in canine X-linked Alport syndrome. Rao, V.H., Lees, G.E., Kashtan, C.E., Delimont, D.C., Singh, R., Meehan, D.T., Bhattacharya, G., Berridge, B.R., Cosgrove, D. Pediatr. Nephrol. (2005) [Pubmed]
  15. Abnormal cardiac wall motion and early matrix metalloproteinase activity. García, R.A., Brown, K.L., Pavelec, R.S., Go, K.V., Covell, J.W., Villarreal, F.J. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  16. Collagenolytic protease expression in cranial cruciate ligament and stifle synovial fluid in dogs with cranial cruciate ligament rupture. Muir, P., Danova, N.A., Argyle, D.J., Manley, P.A., Hao, Z. Veterinary surgery : VS : the official journal of the American College of Veterinary Surgeons. (2005) [Pubmed]
WikiGenes - Universities