Removal of fibrillar collagen N-propeptides

Stable Identifier
R-HSA-2002428
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Fibrillar collagen is synthesized in the ER as procollagen with N- and C-terminal propeptides flanking the collagenous domain (Bellamy & Bornstein 1971). These propeptides, particularly the C-propeptide, inhibit fibril formation (Kadler et al. 1987). Type V collagen N-propeptide removal is partial, and reported to be mediated by BMP-1 which cleaves between the proline/arginine-rich protein domain and the variable domain of the alpha1 chain and between the small and the large collagenous domain of alpha3 chain (refs. in Colige et al. 2005). Mutations in procollagen peptide type V (COL5A1) can cause diseases such as Ehlers-Danlos Sydrome. Majority of the cases result from haploinsufficiency of COL5A1 protein that may lead to a disorganised extracellular matrix. Moreover, other mutations result in structural defects which may in turn result in defective collagen fibrils. The accumulation and interaction of this defective collagen fibrils may lead to ER stress and other complications in the cell (Takahara K et al. 2002, Symoens S et al. 2012).

Literature References
PubMed ID Title Journal Year
12646579 Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase

Wang, WM, Lee, S, Steiglitz, BM, Scott, IC, Lebares, CC, Allen, ML, Brenner, MC, Takahara, K, Greenspan, DS

J Biol Chem 2003
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of Procollagen N-proteinases [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
Cite Us!