Collagenase

Title: Collagenase
CAS Registry Number: 9001-12-1
Additional Names: Clostridiopeptidase A
Trademarks: Iruxol (Knoll); Santyl (Knoll)
Literature References: Rare proteolytic enzyme capable of digesting native undenatured collagen, q.v., found in certain Clostridia bacteria culture filtrates. Crude prepn from C. histolyticum: Mandl et al., J. Clin. Invest. 32, 1323 (1953). Purified prepn: Keller, Mandl, Arch. Biochem. Biophys. 101, 81 (1963). Also isolated from culture media of human wound tissue, skin, bone, leukocytes, gingiva, cornea, rheumatoid synovium; from involuting rat uterus and tadpole tailfin tissue. Sepn of fractions A and B having the respective mol wts 105,000 and 57,400: Harper et al., Biochem. Biophys. Res. Commun. 18, 627 (1965). Amino acid composition: Mandl et al., Biochemistry 3, 1737 (1964); Yoshida, Noda, Biochim. Biophys. Acta 105, 562 (1965). Potential use in treatment of herniated discs: Sussman, FR 2008611 (1970 to Worthington Biochemical). Review of early studies: Mandl, Adv. Enzymol. 23, 163-264 (1961). Reviews: idem, Science 169, 1234-1238 (1970); Nordwig, Adv. Enzymol. Relat. Areas Mol. Biol. 34, 155-205 (1971); Lazarus, Br. J. Dermatol. 86, 193-199 (1972). Book: Collagenase, I. Mandl, Ed. (Gordon and Breach, N.Y., 1972) 215 pp.
Use: In investigation of the structure and biosynthesis of collagen; in dispersion of cells for tissue culture studies.
Therap-Cat: Debriding agent.
Keywords: Debriding Agent; Enzyme; Proteolytic.
Collinomycin Collinsonia Colloidal Bismuth Subcitrate Colocynthin Colony Stimulating Factors

matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
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)
Identifiers
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]