Collagenase


Collagenase
matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
Symbol MMP1
Entrez 4312
HUGO 7155
OMIM 120353
RefSeq NM_002421
UniProt P03956
Other data
EC number 3.4.24.7
Locus Chr. 11 q21-q22
matrix metallopeptidase 8 (neutrophil collagenase)
Identifiers
Symbol MMP8
Entrez 4317
HUGO 7175
OMIM 120355
RefSeq NM_002424
UniProt P22894
Other data
EC number 3.4.24.34
Locus Chr. 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 that stimulate cells such as fibroblasts and osteoblasts, and cause indirect tissue damage.[citation needed]

Contents

Therapeutic uses

Collagenases have been approved for medical uses for

Collagenases and Peyronie's disease

Collagenase remains an investigational drug for the treatment of Peyronie's disease. [2] It has presented a documented efficiency in reducing the size of plaques or in some cases eliminating them.[3]

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. 
  2. ^ http://www.peyronies.org/pages/treatment.htm
  3. ^ http://www.andrologyjournal.org/cgi/content/full/30/4/397

External links