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Formation of collagen networks
Stable Identifier
R-HSA-2213207
Type
Reaction [transition]
Species
Homo sapiens
Compartment
extracellular region
ReviewStatus
5/5
Locations in the PathwayBrowser
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Extracellular matrix organization (Homo sapiens)
Collagen formation (Homo sapiens)
Assembly of collagen fibrils and other multimeric structures (Homo sapiens)
Formation of collagen networks (Homo sapiens)
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Collagens IV, VI, VIII and X form open networks. Type IV networks are irregular. Type VIII and X form hexagonal networks. Type VI collagen forms tetramers which aggregate linearly to form beaded filaments, but also associates laterally through the globular domains so forming a network (Baldock et al. 2003, Knupp et al. 2006, ). Type IV collagen is the predominant collagen type in basement membranes (Parkin et al. 2011). It assembles into three distinct networks with differing combinations of alpha chains, namely alpha1.alpha1.alpha2, alpha3.alpha4.alpha5 and alpha1.alpha2.alpha5.alpha6, (Siebold et al. 1988, Gunwar et al. 1998, Borza et al. 2001), the last of these forms through the association of alpha5.alpha5.alpha6 triple-helical protomers and alpha1.alpha1.alpha2 protomers, interacting tail-to-tail at the retained NC1 domains. Further associations are formed by tetramerization of the 7S domain at the N terminus (Timpl et al. 1981, Siebold et al. 1987). These interactions are the most significant for network formation, but a third interaction occurs whereby type IV collagen dimers interact through lateral association (Yurchenco & Furthmayr 1984, Yurchenco & Ruben 1987, Yurchenko & Patton 2009). Collagen type VI forms tetramers and subsequently several types of higher-order structure (Ball et al. 2001, Beecher et al. 2011) that are probably influenced by the association of other matrix constituents such as hyaluronan (Kielty et al. 1992), fibrillin (Ueda & Yue 2003), biglycan and decorin (Wiberg et al. 2001).
Type VIII collagen forms a hexagonal lattice in Descemet's membrane (Shuttleworth 1997). These are thought to be derived from tetrahedral structures that form when 4 type VIII molecules associate via hydrophobic patches on their C-termini, which then associate via their N-terminals (Stephan et al. 2004). Type X collagen is very similar to type VIII and in vitro forms hexagonal arrays, believed to arise from interactions of the globular domains (Kwan et al. 1991, Jacenko et al. 2001). In vivo type X collagen is found associated with cartilage fibrils in the form of fine filaments (Schmidt & Linsenmayer 1990), which may represent hexagonal lattices that have collapsed during sample preparation (Gordon & Hahn 2010).
Literature References
PubMed ID
Title
Journal
Year
19693541
Collagens
Hahn, RA
,
Gordon, MK
Cell Tissue Res
2010
Participants
Input
Network forming tropocollagens [extracellular region]
(Homo sapiens)
Output
Collagen networks [extracellular region]
(Homo sapiens)
Participates
as an event of
Assembly of collagen fibrils and other multimeric structures (Homo sapiens)
Orthologous Events
Formation of collagen networks (Bos taurus)
Formation of collagen networks (Caenorhabditis elegans)
Formation of collagen networks (Canis familiaris)
Formation of collagen networks (Dictyostelium discoideum)
Formation of collagen networks (Drosophila melanogaster)
Formation of collagen networks (Gallus gallus)
Formation of collagen networks (Mus musculus)
Formation of collagen networks (Rattus norvegicus)
Formation of collagen networks (Sus scrofa)
Formation of collagen networks (Xenopus tropicalis)
Authored
Jupe, S (2012-04-30)
Reviewed
Raleigh, S (2012-10-08)
Ricard-Blum, S (2012-11-19)
Kalamajski, S (2012-10-08)
Created
Jupe, S (2012-04-30)
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