Removal of fibrillar collagen C-propeptides

Stable Identifier
R-HSA-2002440
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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). Removal of propeptides is generally described as an extracellular process but can occur within the cell. Procollagen processing in tendon fibroblasts was initiated within the secretory pathway with the N-propetides removed first, in the ER or an intermediate between the ER and Golgi. The C peptides were removed later, probably at the cell membrane-ECM interface (Canty-Laird et al. 2012).

Collagen C-propeptides are cleaved by the tolloid family metalloproteinases bone morphogenic protein 1 (BMP1)/mammalian tolloid (mTLD), tolloid-like 1 (TLL1) and TLL2.

Procollagen types I-III are cleaved by BMP1/mTLD (Chicken types I and II, human type III, by chicken enzyme, Hojima et al. 1985, human types I, II, human enzyme, Scott et al. 1999), TLL-1 (human types I, II, human enzyme, Scott et al. 1999), and TLL-2 in the presence of PCOLCE (PCPE-1, Pappano et al. 2003, Petropoulou et al. 2005). Type V C-propeptide removal is mediated by furin-like proprotein convertases and/or BMP-1 depending on the chain type (Kessler et al. 2005).
Literature References
PubMed ID Title Journal Year
3905801 Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization

Prockop, DJ, van der Rest, M, Hojima, Y

J. Biol. Chem. 1985
10479448 Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis

Clark, TG, Blitz, IL, Scott, IC, Takahara, K, Cho, KW, Imamura, Y, Maas, SA, Greenspan, DS, Thomas, CL, Pappano, WN, Steiglitz, BM

Dev Biol 1999
Participants
Participates
Catalyst Activity

metalloendopeptidase activity of Procollagen C-proteinases [extracellular region]

This event is regulated
Orthologous Events
Authored
Reviewed
Created
Cite Us!