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MMP13  -  matrix metallopeptidase 13 (collagenase 3)

Gallus gallus

 
 
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High impact information on MMP-13

  • PGE2 dose-dependently inhibited the expression of the differentiation-related genes, colX, VEGF, MMP-13, and alkaline phosphatase gene, and enzyme activity with significant effects at concentrations as low as 10(-10) M [1].
  • Moreover, weight loading enhanced the penetration of blood vessels into the growth plates and enhanced the gene expression of the matrix metalloproteinases MMP9 and MMP13 in those growth plates [2].
  • 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 [3].
 

Anatomical context of MMP-13

 

Associations of MMP-13 with chemical compounds

References

  1. PGE2 inhibits chondrocyte differentiation through PKA and PKC signaling. Li, T.F., Zuscik, M.J., Ionescu, A.M., Zhang, X., Rosier, R.N., Schwarz, E.M., Drissi, H., O'Keefe, R.J. Exp. Cell Res. (2004) [Pubmed]
  2. Weight loading young chicks inhibits bone elongation and promotes growth plate ossification and vascularization. Reich, A., Jaffe, N., Tong, A., Lavelin, I., Genina, O., Pines, M., Sklan, D., Nussinovitch, A., Monsonego-Ornan, E. J. Appl. Physiol. (2005) [Pubmed]
  3. Search for an endogenous collagenase in chicken endochondral bone matrix vesicles. Chen, D., Golub, E.E. The Penn dental journal. (2001) [Pubmed]
  4. 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]
 
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