Reactome | Collagen types III, IV, V, VI, VIII, IX, XVI bind integrins alpha1beta1 and alpha2beta1

Collagen types III, IV, V, VI, VIII, IX, XVI bind integrins alpha1beta1 and alpha2beta1

Stable Identifier

R-HSA-2327695

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane, extracellular region

ReviewStatus

5/5

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Collagen types III, IV, V, VI, VIII, IX, XVI bind integrins alpha1beta1 and alpha2beta1

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The widely-expressed collagen receptors integrin alpha2beta1 and alpha1beta1 both bind collagen types I-IV (Tulla et al. 2001). Integrin alpha1beta1 binds to collagen type IV and VI with higher affinity than to types I-III, whereas alpha2beta1 has a higher affinity for collagen types I-III than for type IV (Tulla et al. 2001). Binding to collagen type I occurs at a site corresponding to residues 502-516 of the collagen alpha-1(I) chain (Knight et al. 1998, 2000, Xu et al. 2000).

Integrin alpha2beta also binds collagen types VIII (Saelman et al. 1992), IX (Käpylä et al. 2004), XI (Tuckwell et al. 1995), the noncollagenous domain 1 (NC1) of collagen types VII and X (Chen et al. 1999), and collagen type XVI, though this is bound with higher affinity by integrin alpha1beta1 (Eble et al. 2006). Both integrins interact
with collagen XVI via the A-domain of their alpha-subunits. A tryptic fragment of collagen XVI comprising collagenous domains 1–3 is bound by integrin alpha1beta1. Electron microscopy of this complex or integrin alpha1beta1 with full-length collagen XVI revealed two unique integrin alpha1beta1 binding sites (GLQGER and GIKGER) within the N-terminal half of the COL2 domain of collagen XVI (Grässel & Bauer 2013).

Integrin alpha1beta1 also binds collagen types IX (Käpylä et al. 2004), XVI (Eble et al. 2006), VIII though less strongly than alpha2 beta1 (Saelman et al. 1992), XIII (Nykvist et al. 2000) and arresten, the NC1 of alpha-1 type IV collagen (Colorado PC et al. 2000; Nyberg et al. 2008).

Integrin alpha10beta1 is able to bind collagen types I-VI, with a stronger binding affinity for types IV and VI, similar to the preferences of integrin alpha1beta1 (Tulla et al. 2001).

Integrin alpha11beta1 mediates cell adhesion to collagen types I and IV with a preference for I (Tiger et al. 2001).

Integrins alphaVbeta3 (Sudhakar et al. 2003) and alpha3beta1 (Borza et al. 2006) can bind tumstatin, the cleaved NC1 of alpha-3 type IV collagen. Integrins alphaVbeta3 and alphavbeta5 can bind camstatin, the cleaved NC1 of alpha-2 type IV collagen (Magnon et al. 2005).

Literature References

PubMed ID	Title	Journal	Year
15383545	The fibril-associated collagen IX provides a novel mechanism for cell adhesion to cartilaginous matrix Nissinen, L, Jäälinoja, J, Heino, J, Vehviläinen, P, Farndale, RW, Viitasalo, T, Ala-Kokko, L, Marjomäki, V, Ylöstalo, J, Säämänen, AM, Nykvist, P, Tulla, M, Birk, DE, Käpylä, J	J. Biol. Chem.	2004
16754661	Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains Niland, S, Kassner, A, Grässel, S, Mörgelin, M, Grifka, J, Eble, JA	J Biol Chem	2006
8118028	Platelet adhesion to collagen types I through VIII under conditions of stasis and flow is mediated by GPIa/IIa (alpha 2 beta 1-integrin) Nieuwenhuis, HK, Williams, S, Gralnick, HR, Saelman, EU, McKeown, L, Sage, EH, Hese, KM, de Groot, PG, Sixma, JJ, Heijnen, HF	Blood	1994
8344274	Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1 Kühn, K, Golbik, R, Eble, J, Kern, A	Eur. J. Biochem.	1993
11572855	Selective binding of collagen subtypes by integrin alpha 1I, alpha 2I, and alpha 10I domains Nissinen, L, Nykvist, P, Johnson, MS, Impola, U, Viitasalo, T, Tulla, M, Pentikäinen, OT, Heino, J, Käpylä, J	J. Biol. Chem.	2001