Abstract
The collagen contents of the Dupuytren contracture lesions have been extensively studied. Collagen type III is the predominant type of collagen in the early, nodular stages of the disease, while cords mostly contain highly cross-linked collagen type I. In Dupuytren contracture tissues, changes in transforming growth factor beta (TGF-β) signaling pathways promote collagen synthesis and the development of myofibroblasts. If an enzyme is to degrade the triple helix of collagen in the cord, it must first bind to sites on the triple helix, and subsequently unwind it, in order to then cleave one or more strands of the triple helix. Collagenase Clostridium histolyticum performs all three of these activities. Collagenase, after cord injection, is efficiently removed by a plasma protein known as α-2 macroglobulin.
| Original language | English |
|---|---|
| Title of host publication | Collagenase in Dupuytren Disease |
| Publisher | Springer International Publishing |
| Pages | 1-6 |
| Number of pages | 6 |
| ISBN (Electronic) | 9783319658223 |
| ISBN (Print) | 9783319658216 |
| DOIs | |
| State | Published - Jan 1 2018 |
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