Collagenases
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 (HGNC) |
UniProt | Length (AA) |
Remarks |
---|---|---|---|---|
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 ).
biosynthesis
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.
literature
- J. Ramundo, M. Gray: Enzymatic wound debridement. In: Journal of wound, ostomy, and continence nursing: official publication of The Wound, Ostomy and Continence Nurses Society / WOCN. Volume 35, Number 3, 2008 May-Jun, pp. 273-280, ISSN 1071-5754 . doi : 10.1097 / 01.WON.0000319125.21854.78 . PMID 18496083 . (Review).
Individual evidence
- ↑ UniProt search result
- ↑ 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 .
- ↑ 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).
- ↑ 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.
- ↑ 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.