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Gene Review

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

Gallus gallus

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Disease relevance of MMP2

  • It is suggested that MMP-2 and MMP-9 enzymes might play a role in the permeability increase of vessel walls by the destruction of the basement membranes in the salt-induced experimental ascites syndrome in broiler chickens [1].
  • The activity of gelatinase A, a member of the matrix metalloproteinase family, has been shown to increase in the posterior sclera during the development of induced myopia in several species [2].
  • Rous sarcoma virus-transformed cultures of chicken embryo fibroblasts (RSVCEF) secrete elevated levels of a 70 kDa progelatinase, an avian form of the 72 kDa matrix metalloproteinase-2 (MMP-2) [3].
  • Relatively high levels of matrix metalloproteinase MMP-2 activity have been found in pericardial effusions from affected chickens, suggesting a possible involvement of this enzyme in the aetiology of pericardial lesions [4].

High impact information on MMP2

  • Studies using purified proteases showed that plasmin, elastase, MMP2, and MMP9 were able to cleave LTBP1 to produce 125-165-kDa fragments [5].
  • Investigation of metalloproteinase activity showed there to be a reduction in MMP-2 levels in dyschondroplastic growth plate compared to normal growth plate [6].
  • Gelatinase A and TIMP-2 expression in the fibrous sclera of myopic and recovering chick eyes [2].
  • Gelatinase A activity within the fibrous scleras of form-deprived eyes and paired contralateral recovering eyes was evaluated by gelatin zymography [2].
  • METHODS: Total RNA was extracted from the posterior scleras of form-deprived chick eyes, eyes recovering from deprivation myopia, and paired contralateral control eyes, and subjected to northern blot analysis analyses using cDNA probes to chicken gelatinase A and TIMP-2 [2].

Biological context of MMP2

  • These patterns suggest that MMP-2 plays a role in cell motility during the EMT and during later morphogenesis [7].
  • Humoral and cellular immunity induced by tumor cell vaccine based on the chicken xenogeneic homologous matrix metalloproteinase-2 [8].
  • The activation of immunization by breaking immune tolerance to self-MMP-2 may be one of the promising approaches for the treatment of MMP-2-positive tumors [8].

Anatomical context of MMP2

  • RESULTS: The predominant gelatinolytic enzyme secreted by scleral fibroblasts was MMP-2 [9].
  • Comparisons of these expression patterns in multiple embryonic tissues suggest a probable role for MMP-2 in the migration phase of the EMT, in addition to mesenchyme dispersion and tissue remodeling [7].
  • Similarly, knockdown of MMP-2 expression in the dorsal neural tube using antisense morpholino oligos perturbs the EMT, but also does not affect migration of neural crest cells after they have detached from the neural tube [7].
  • MMP-2 is expressed as neural crest cells detach from the neural epithelium during an epithelial-mesenchymal transformation (EMT) but is rapidly extinguished as they disperse [7].
  • MMP-2 is also expressed in mesenchyme where tissue remodeling is in progress, such as in the developing feather germs, in the head mesenchyme, in the lateral plate mesoderm, and in the limb dermis, especially in the regions where tendons are developing [7].

Associations of MMP2 with chemical compounds


Other interactions of MMP2

  • Changes in scleral MMP-2, TIMP-2 and TGFbeta-2 mRNA expression after imposed myopic and hyperopic defocus in chickens [13].
  • Immunostaining of MMP-2 and MMP-9 was more intense and extensive in ascitic broilers than in the controls, although a decrease was seen with increasing age both in normal and ascitic chickens [1].
  • Western blots with antibodies to bacterial collagenase, matrix metallo-proteinases 13 (MMP-13), an endogenous collagenase, and MMP-2, an endogenous gelatinase, were also done to determine the presence of an endogenous collagenase [14].
  • These results indicate that MMP-2 activity and fibronectin expression are 2 strictly related components of angiogenesis occurring in vivo [15].

Analytical, diagnostic and therapeutic context of MMP2


  1. The identification of matrix metalloproteinases and their tissue inhibitors in broiler chickens by immunohistochemistry. Ozyigit, M.O., Kahraman, M.M., Sonmez, G. Avian Pathol. (2005) [Pubmed]
  2. Gelatinase A and TIMP-2 expression in the fibrous sclera of myopic and recovering chick eyes. Rada, J.A., Perry, C.A., Slover, M.L., Achen, V.R. Invest. Ophthalmol. Vis. Sci. (1999) [Pubmed]
  3. Native TIMP-free 70 kDa progelatinase (MMP-2) secreted at elevated levels by RSV transformed fibroblasts. Stefansson, S., Aimes, R.T., Seward, N.B., Alexander, D.S., Quigley, J.P. J. Cell. Physiol. (1994) [Pubmed]
  4. Lesions of the pericardium and their significance in the aetiology of heart failure in broiler chickens. Olkowski, A.A., Wojnarowicz, C., Rathgeber, B.M., Abbott, J.A., Classen, H.L. Res. Vet. Sci. (2003) [Pubmed]
  5. Proteolysis of latent transforming growth factor-beta (TGF-beta )-binding protein-1 by osteoclasts. A cellular mechanism for release of TGF-beta from bone matrix. Dallas, S.L., Rosser, J.L., Mundy, G.R., Bonewald, L.F. J. Biol. Chem. (2002) [Pubmed]
  6. Collagen expression in chicken tibial dyschondroplasia. Wardale, R.J., Duance, V.C. J. Cell. Sci. (1996) [Pubmed]
  7. MMP-2 plays an essential role in producing epithelial-mesenchymal transformations in the avian embryo. Duong, T.D., Erickson, C.A. Dev. Dyn. (2004) [Pubmed]
  8. Humoral and cellular immunity induced by tumor cell vaccine based on the chicken xenogeneic homologous matrix metalloproteinase-2. Yi, T., Wei, Y.Q., Tian, L., Zhao, X., Li, J., Deng, H.X., Wen, Y.J., Zou, C.H., Tan, G.H., Kan, B., Su, J.M., Jiang, Y., Mao, Y.Q., Chen, P., Wang, Y.S. Cancer Gene Ther. (2007) [Pubmed]
  9. Involvement of mechanical stretch in the gelatinolytic activity of the fibrous sclera of chicks, in vitro. Fujikura, H., Seko, Y., Tokoro, T., Mochizuki, M., Shimokawa, H. Jpn. J. Ophthalmol. (2002) [Pubmed]
  10. Retinoic acid treatment elevates matrix metalloproteinase-2 protein and mRNA levels in avian growth plate chondrocyte cultures. Nie, D., Ishikawa, Y., Yoshimori, T., Wuthier, R.E., Wu, L.N. J. Cell. Biochem. (1998) [Pubmed]
  11. Changes in mRNA expression of MMP-2 in the Müllerian duct of chicken embryo. Ha, Y., Tsukada, A., Saito, N., Shimada, K. Gen. Comp. Endocrinol. (2004) [Pubmed]
  12. Changes in the tibial growth plates of chickens with thiram-induced dyschondroplasia. Rath, N.C., Richards, M.P., Huff, W.E., Huff, G.R., Balog, J.M. J. Comp. Pathol. (2005) [Pubmed]
  13. Changes in scleral MMP-2, TIMP-2 and TGFbeta-2 mRNA expression after imposed myopic and hyperopic defocus in chickens. Schippert, R., Brand, C., Schaeffel, F., Feldkaemper, M.P. Exp. Eye Res. (2006) [Pubmed]
  14. Search for an endogenous collagenase in chicken endochondral bone matrix vesicles. Chen, D., Golub, E.E. The Penn dental journal. (2001) [Pubmed]
  15. Temporal expression of the matrix metalloproteinase MMP-2 correlates with fibronectin immunoreactivity during the development of the vascular system in the chick embryo chorioallantoic membrane. Ribatti, D., Nico, B., Vacca, A., Iurlaro, M., Roncali, L. J. Anat. (1999) [Pubmed]
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