Integrins alpha4beta1, alpha8beta1, alphaVbeta1, alphaVbeta3, alphaVbeta6 bind Fibronectin matrix

Stable Identifier
R-HSA-216050
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Several integrins are able to bind fibronectin (FN1). Alpha5beta1 is a specialist FN1 receptor (Singh et al. 2010). The alpha4beta1 (VAL-4) integrin has been suggested to play an important role in haemopoiesis. Fibronectin and VCAM-1 are the main ligands for VLA-4. The H1 region present in all FN isoforms represents the binding site for VLA-4, alphaIIbBeta3, which is highly expressed on platelets where it predominantly binds fibrinogen leading to thrombus formation but also binds FN1 (Savage et al. 1996). Alpha4beta1 mediates cell-cell contacts and cell-matrix contacts through the ligands VCAM-1 and FN1, respectively (Humphries et al. 1995), this is suggested to play an important role in haemopoiesis. The H1 region present in all FN isoforms represents the binding site for VLA-4. Integrins alpha3beta1, alpha4beta7, alphaVbeta1, 3 (Wu et al. 1996, Johansson et al. 1997), 6 (Busk et al. 1992) and alpha8beta1 (Muller et al. 1995, Farias et al. 2005) are all able to bind FN1.

Tenacious binding of free fibronectin to cells leads to enhanced fibronectin matrix assembly and the formation of a polymerized fibronectin "cocoon" around the cells. This process is enhanced in the presence of CEACAM molecules.

Literature References
PubMed ID Title Journal Year
9858236 Effect of the interaction between fibronectin and VLA-4 on the proliferation of human B cells, especially a novel human B-cell line, OPM-3

Yoshida, H, Nishiura, T, Karasuno, T, Matsumura, I, Ishikawa, J, Yoshimura, M, Yokota, T, Okajima, Y, Ogawa, M, Kanakura, Y, Tomiyama, Y, Matsuzawa, Y

Br J Haematol 1998
1588291 VLA-4-fibronectin interaction is required for the terminal differentiation of human bone marrow cells capable of spontaneous and high rate immunoglobulin secretion

Roldán, E, Garcia-Pardo, A, Brieva, JA

J Exp Med 1992
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