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Gene Review

MMP9  -  matrix metallopeptidase 9 (gelatinase B,...

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Disease relevance of MMP9

  • Although MMP-9 has been reported to play a role in bone resorption, the association of this enzyme during deciduous tooth resorption has not yet been clarified [1].
  • Five clinical E. coli mastitis milk samples and five milk samples from cows with healthy udders were analyzed to detect whether increased levels of gelatinolytic MMP-2 and MMP-9 have a role in naturally occurring mastitis with endotoxin involvement [2].
  • Increased concentrations of MMP-9 activity were found in the synovial fluids of cows with septic arthritis (P < 0.001) in comparison with fluids from normal joints [3].
  • Our results provide evidence that matrix metalloproteinases are activated in lung lesions from cattle with shipping fever and that M. haemolytica virulence products induce production, release, and especially activation of gelatinase B by bovine inflammatory cells in vitro [4].
  • In the work reported here, proteolytic activity previously found for hydatid cysts was further characterized as MMP-9 [5].

High impact information on MMP9

  • Further, FGF-2 neutralization reduced the amount of MMP-9 released in the supernatant of E1A-transfected cells and strongly inhibited BAEC differentiation, thus suggesting that wtE1A activates BAEC by a mechanism, at least partially, dependent on a FGF-2 autocrine/paracrine loop [6].
  • Furthermore, recombinant 92-kDa fibronectin type II-like repeats inhibited binding of the 92-kDa gelatinase to elastin [7].
  • Hence, regulation of the MMP-9/TIMP balance failed to correlate with the migratory or invasive capacity [8].
  • These results question a direct role for MMP-9 in endothelial cell motility and suggest that gelatinases may contribute in alternative ways to the angiogenic process [8].
  • Gelatinase B/MMP-9 was only detected upon treatment with either PMA or TGF-beta1 [8].

Biological context of MMP9


Anatomical context of MMP9


Associations of MMP9 with chemical compounds


Regulatory relationships of MMP9

  • In addition, we correlated this biphasic effect on tube formation with the capacity of TSP-1 to stimulate the activity of a matrix metalloproteinase-9 (MMP-9) in BAE cell collagen gel cultures [18].
  • Furthermore, we employed adenoviral PKC-alpha and found that weak PMA stimulation (5 ng/ml) enhanced ERK1/2 activation and MMP-9 secretion in these cells [19].

Other interactions of MMP9

  • In contrast, a transient increase in the number of MMP-9- and TIMP-2-positive cells was observed in mitogenic bovine whey extract treated ulcer biopsies compared with pretreatment levels (p<0.05) [20].
  • But once trophoblast cells began to migrate into the endometrial cell layer, MMP-2 production increased, and at the same time MMP-9 production also became evident in the medium [21].
  • Half of the medium was replaced every 2 days, and conditioned medium was analysed for oestradiol and matrix metalloproteinase 2 (MMP-2) and MMP-9 secretion [17].
  • Strikingly, the abrogation of MAP kinase signaling by a dominant-negative ERK-1 mutant inhibited glial-induced capillary network formation by reducing VEGF levels and MMP-9 activity and increasing the levels of tissue inhibitor of metalloproteinase-1 [11].
  • The TSP-1-mediated stimulation of MMP-9 activity was specific and dose- and time-dependent [18].

Analytical, diagnostic and therapeutic context of MMP9


  1. Expression of matrix metalloproteinase-9 mRNA and protein during deciduous tooth resorption in bovine odontoclasts. Linsuwanont, B., Takagi, Y., Ohya, K., Shimokawa, H. Bone (2002) [Pubmed]
  2. Increase in milk metalloproteinase activity and vascular permeability in bovine endotoxin-induced and naturally occurring Escherichia coli mastitis. Raulo, S.M., Sorsa, T., Tervahartiala, T., Latvanen, T., Pirilä, E., Hirvonen, J., Maisi, P. Vet. Immunol. Immunopathol. (2002) [Pubmed]
  3. Matrix metalloproteinases 2 and 9 activity in bovine synovial fluids. Arican, M., Coughlan, A.R., Clegg, P.D., Carter, S.D. Journal of veterinary medicine. A, Physiology, pathology, clinical medicine. (2000) [Pubmed]
  4. Potential involvement of gelatinases and their inhibitors in Mannheimia haemolytica pneumonia in cattle. Starr, A.E., Dan, T., Minhas, K., Shewen, P.E., Coomber, B.L. Infect. Immun. (2004) [Pubmed]
  5. A relevant enzyme in granulomatous reaction, active matrix metalloproteinase-9, found in bovine Echinococcus granulosus hydatid cyst wall and fluid. Marco, M., Baz, A., Fernandez, C., Gonzalez, G., Hellman, U., Salinas, G., Nieto, A. Parasitol. Res. (2006) [Pubmed]
  6. E1A stimulates FGF-2 release promoting differentiation of primary endothelial cells. Giampietri, C., Levrero, M., Felici, A., D'Alessio, A., Capogrossi, M.C., Gaetano, C. Cell Death Differ. (2000) [Pubmed]
  7. The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats. Shipley, J.M., Doyle, G.A., Fliszar, C.J., Ye, Q.Z., Johnson, L.L., Shapiro, S.D., Welgus, H.G., Senior, R.M. J. Biol. Chem. (1996) [Pubmed]
  8. Examining the relationship between the gelatinolytic balance and the invasive capacity of endothelial cells. Puyraimond, A., Weitzman, J.B., Babiole, E., Menashi, S. J. Cell. Sci. (1999) [Pubmed]
  9. The effect of endothelial cell overexpression of plasminogen activator inhibitor-1 on smooth muscle cell migration. Proia, R.R., Nelson, P.R., Mulligan-Kehoe, M.J., Wagner, R.J., Kehas, A.J., Powell, R.J. J. Vasc. Surg. (2002) [Pubmed]
  10. Effects of radiation on the levels of MMP-2, MMP-9 and TIMP-1 during morphogenic glial-endothelial cell interactions. Nirmala, C., Jasti, S.L., Sawaya, R., Kyritsis, A.P., Konduri, S.D., Ali-Osman, F., Rao, J.S., Mohanam, S. Int. J. Cancer (2000) [Pubmed]
  11. Glial cell-induced endothelial morphogenesis is inhibited by interfering with extracellular signal-regulated kinase signaling. Chandrasekar, N., Mohanam, S., Lakka, S.S., Dinh, D.H., Olivero, W.C., Gujrati, M., Rao, J.S. Clin. Cancer Res. (2003) [Pubmed]
  12. Characterization of gelatinases in bronchoalveolar lavage fluid and gelatinases produced by alveolar macrophages isolated from healthy calves. Lakritz, J., Marsh, A.E., Cockrell, M., Smith, M.F., Tyler, J.W. Am. J. Vet. Res. (2004) [Pubmed]
  13. Culture of bovine preantral follicles in a serum-free system: markers for assessment of growth and development. McCaffery, F.H., Leask, R., Riley, S.C., Telfer, E.E. Biol. Reprod. (2000) [Pubmed]
  14. Matrix metalloproteinases (MMP-2 and MMP-9) and tissue inhibitor-2 of matrix metalloproteinases (TIMP-2) in the placenta and interplacental uterine wall in normal cows and in cattle with retention of fetal membranes. Walter, I., Boos, A. Placenta (2001) [Pubmed]
  15. Calcification and identification of metalloproteinases in bovine pericardium after subcutaneous implantation in rats. Jorge-Herrero, E., Turnay, J., Calero, P., Olmo, N., López De Silanes, I., Martín Maestro, M., Lizarbe, M.A., Castillo-Olivares, J.L. Journal of materials science. Materials in medicine. (2001) [Pubmed]
  16. Gelatinases in soft tissue biomaterials. Analysis of different crosslinking agents. Calero, P., Jorge-Herrero, E., Turnay, J., Olmo, N., López de Silanes, I., Lizarbe, M.A., Maestro, M.M., Arenaz, B., Castillo-Olivares, J.L. Biomaterials (2002) [Pubmed]
  17. Effect of ascorbic acid on health and morphology of bovine preantral follicles during long-term culture. Thomas, F.H., Leask, R., Srsen, V., Riley, S.C., Spears, N., Telfer, E.E. Reproduction (2001) [Pubmed]
  18. Thrombospondin-1 modulates angiogenesis in vitro by up-regulation of matrix metalloproteinase-9 in endothelial cells. Qian, X., Wang, T.N., Rothman, V.L., Nicosia, R.F., Tuszynski, G.P. Exp. Cell Res. (1997) [Pubmed]
  19. Protein kinase C-alpha activation by phorbol ester induces secretion of gelatinase B/MMP-9 through ERK 1/2 pathway in capillary endothelial cells. Park, M.J., Park, I.C., Lee, H.C., Woo, S.H., Lee, J.Y., Hong, Y.J., Rhee, C.H., Lee, Y.S., Lee, S.H., Shim, B.S., Kuroki, T., Hong, S.I. Int. J. Oncol. (2003) [Pubmed]
  20. Mitogenic bovine whey extract modulates matrix metalloproteinase-2, -9, and tissue inhibitor of matrix metalloproteinase-2 levels in chronic leg ulcers. Varelias, A., Cowin, A.J., Adams, D., Harries, R.H., Cooter, R.D., Belford, D.A., Fitridge, R.A., Rayner, T.E. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society. (2006) [Pubmed]
  21. Matrix-metalloproteinases-2 and -9 production in bovine endometrial cell culture. Hashizume, K., Takahashi, T., Shimizu, M., Todoroki, J., Shimada, A., Hirata, M., Sato, T., Ito, A. J. Reprod. Dev. (2003) [Pubmed]
  22. The extracellular matrix produced by bovine corneal endothelial cells contains progelatinase A. Menashi, S., Vlodavsky, I., Ishai-Michaeli, R., Legrand, Y., Fridman, R. FEBS Lett. (1995) [Pubmed]
  23. Polarized distribution of metalloproteinases in the bovine interphotoreceptor matrix. Plantner, J.J., Drew, T.A. Exp. Eye Res. (1994) [Pubmed]
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