Collagen type VII binds laminin-322 and collagen IV

Stable Identifier
R-HSA-2396234
Type
Reaction [binding]
Species
Homo sapiens
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Anchoring fibrils are structures in skin that consist largely of collagen VII. They extend from the epidermal basement membrane to the dermal stroma where they connect with reticular fibre bundles, largely composed of collagen III (Fleischmajer et al. 1980). The long loop region of collagen VII entraps fibrillar collagens in the papillary dermis (Burgeson 1993). Type VII collagen binds laminin-332 (laminin-5) through the beta3 short arm, and also binds both type IV collagen and interstitial banded collagen fibrils - represented here by their major constituent, collagen I (Nakishima et al. 2005, Brittingham et al. 2006, Villone et al. 2008). Mutations of collagen VII are a cause of dystrophic epidermolysis bullosa, a blistering skin disease where separation occurs in the dermis at the level of anchoring fibrils (Chung & Uitto 2010, Uitto et al. 2010).

Literature References
PubMed ID Title Journal Year
16272566 Regulation of cell adhesion and type VII collagen binding by the beta3 chain short arm of laminin-5: effect of its proteolytic cleavage

Nakashima, Y, Kariya, Y, Yasuda, C, Miyazaki, K

J. Biochem. 2005
18599485 Supramolecular interactions in the dermo-epidermal junction zone: anchoring fibril-collagen VII tightly binds to banded collagen fibrils

Villone, D, Fritsch, A, Koch, M, Bruckner-Tuderman, L, Hansen, U, Bruckner, P

J. Biol. Chem. 2008
16563355 High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV

Brittingham, R, Uitto, J, Fertala, A

Biochem. Biophys. Res. Commun. 2006
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