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Gene Review:

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

Gallus gallus

Ozyigit, M.O. et al., Reich, A. et al., Dallas, S.L. et al.

Dallas, Rosser, Mundy, Bonewald,

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Disease relevance of MMP9

The aim of this study was to investigate the distribution of matrix metalloproteinase (MMP)-2, MMP-9, tissue inhibitor of matrix metalloproteinase (TIMP)-1 and TIMP-2 using immunohistochemistry in the ascites syndrome of broiler chickens in a salt-induced experimental model [1].

High impact information on MMP9

Studies using purified proteases showed that plasmin, elastase, MMP2, and MMP9 were able to cleave LTBP1 to produce 125-165-kDa fragments [2].
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 [3].

Anatomical context of MMP9

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].

References

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]
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]
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]

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