from Wikipedia, the free encyclopedia

As collagenases are enzymes referred to which the peptide bond between proline and other amino acids cleaved. This means that these proteases are able to break down collagen . They occur in higher animals ( Coelomata ), bacteria and some archaea . Five collagenases are known in humans, all of which belong to the matrix metalloproteases ( EC  3.4.24.- ):

protein Gene
UniProt Length
Interstitial collagenase MMP1 P03956 170, 200 Cleavage into two enzymes (22 kDa, 27 kDa); splits collagen I, II, III, VII and X, HIV protein Tat
Gelatinase A MMP2 P08253 551 ubiquitous; Torg-Winchester Syndrome ; splits gelatin I, collagen IV, V, VII, X
Neutrophil collagenase MMP8 P22894 367 splits fibrillar collagen I, II, III
Gelatinase B MMP9 P14780 (92, 82, 67 kDa) Susceptibility to herniated disc , anadysplasia of the metaphysis ; smaller enzyme variants; splits gelatin I, V and collagen IV, V
Collagenase 3 MMP13 P45452 368 Dysplasias ; splits collagen I.

With the help of this enzyme, clostridia can spread particularly quickly through the breakdown of collagen in the connective tissue . Conversely, clostridial collagenase is used to support wound healing ( debridement ).


Vertebrate collagenases arise initially in the form of precursor proteins as procollagenases , which have to be activated post-translationally by enzymatic cleavage before use.

Dupuytren's disease

For the treatment of the fibrotic cords in the palm and fingers of Dupuytren's disease , a microbial collagenase ( trade name Xiapex ; manufacturer Pfizer ) was approved in May 2011 in the European Union , which is made up of the two collagenase enzymes AUX I and AUX II of the bacterium Clostridium histolyticum , which when injected into the nodes can dissolve them.


Individual evidence

  1. UniProt search result
  2. M. Pruteanu, NP Hyland et al. a .: Degradation of the extracellular matrix components by bacterial-derived metalloproteases: implications for inflammatory bowel diseases. In: Inflammatory bowel diseases. Volume 17, Number 5, May 2011, pp. 1189-1200, ISSN  1536-4844 . doi : 10.1002 / ibd.21475 . PMID 20853433 .
  3. J. Ramundo, M. Gray: Collagenase for enzymatic debridement: a systematic review. In: Journal of wound, ostomy, and continence nursing: official publication of The Wound, Ostomy and Continence Nurses Society / WOCN. Volume 36, Number 6 Suppl, 2009 Nov-Dec, pp. S4-11, ISSN  1528-3976 . doi : 10.1097 / WON.0b013e3181bfdf83 . PMID 19918148 . (Review).
  4. Collagenase in Dupuytren's contracture: additional benefit not proven , press release of the Institute for Quality and Efficiency in Health Care from January 1, 2012.
  5. Edward J. Campbell, J. Davis Cury, Cathy J. Lazarus, and Howard G. Welgus: Monocyte procollagenase and tissue inhibitor metalloproteinases. Identification, characterization, and regulation . (PDF) In: The Journal of Biological Chemistry . 262, No. 33, November 25, 1987, pp. 15862-15868. Retrieved March 3, 2013.