Collagenases

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matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
SymbolMMP1
Entrez4312
HUGO7155
OMIM120353
RefSeqNM_002421
UniProtP03956
Other data
EC number3.4.24.7
LocusChr. 11 q21-q22
matrix metallopeptidase 8 (neutrophil collagenase)
Identifiers
SymbolMMP8
Entrez4317
HUGO7175
OMIM120355
RefSeqNM_002424
UniProtP22894
Other data
EC number3.4.24.34
LocusChr. 11 q21-q22


Collagenases are enzymes that break the peptide bonds in collagen.

They assist in destroying extracellular structures in pathogenesis of bacteria such as Clostridium. They are an exotoxin (a virulence factor) and help to facilitate 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.

Collagenase production can be induced during an immune response, by cytokines which stimulate cells such as fibroblasts and osteoblasts, and cause indirect tissue damage.[citation needed]

SANTYL Ointment, a Healthpoint, Ltd. product, is the only FDA approved product containing Collagenase as its primary ingredient.

They are categorized under EC number 3.4.24.

See also

References

  1. Gerard J. Tortora, Berdell R. Funke, Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 03-213-960-30.

External links



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