From Wikipedia, the free encyclopedia
Jump to: navigation, search
matrix metallopeptidase 1 (interstitial collagenase)
Symbol MMP1
Entrez 4312
HUGO 7155
OMIM 120353
RefSeq NM_002421
UniProt P03956
Other data
Locus Chr. 11 q21-q22
matrix metallopeptidase 8 (neutrophil collagenase)
Symbol MMP8
Entrez 4317
HUGO 7175
OMIM 120355
RefSeq NM_002424
UniProt P22894
Other data
Locus Chr. 11 q21-q22

Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the pathogenesis of bacteria such as Clostridium. They are a considered a virulence factor, facilitating the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs.[1]

Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. This stops large structures from forming inside the cell itself.

In addition to being produced by some bacteria, collagenase can be made by the body as part of its normal immune response. This production is induced by cytokines, which stimulate cells such as fibroblasts and osteoblasts, and can cause indirect tissue damage.[citation needed]

Therapeutic uses[edit]

Collagenases have been approved for medical uses for

Peyronie's disease[edit]

Collagenase remains an investigational drug for the treatment of Peyronie's disease. [3] It has presented a documented efficiency in reducing the size of plaques or in some cases eliminating them.[4]

See also[edit]


  1. ^ Gerard J. Tortora, Berdell R. Funke, Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 0-321-39603-0. 
  2. ^
  3. ^
  4. ^

External links[edit]