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Collagenase

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matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
SymbolMMP1
NCBI gene4312
HGNC7155
OMIM120353
RefSeqNM_002421
UniProtP03956
Other data
EC number3.4.24.7
LocusChr. 11 q21-q22
Search for
StructuresSwiss-model
DomainsInterPro
matrix metallopeptidase 8 (neutrophil collagenase)
Identifiers
SymbolMMP8
NCBI gene4317
HGNC7175
OMIM120355
RefSeqNM_002424
UniProtP22894
Other data
EC number3.4.24.34
LocusChr. 11 q21-q22
Search for
StructuresSwiss-model
DomainsInterPro

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]

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. [3] It has presented a documented efficiency in reducing the size of plaques or in some cases eliminating them.[4]

See also

References

  1. ^ Gerard J. Tortora, Berdell R. Funke, Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 0-321-39603-0.{{cite book}}: CS1 maint: multiple names: authors list (link)
  2. ^ http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1501117/
  3. ^ http://www.peyronies.org/pages/treatment.htm
  4. ^ http://www.andrologyjournal.org/cgi/content/full/30/4/397