Identification of a novel integrin alphaMbeta2 binding site in CCN1 (CYR61), a matricellular protein expressed in healing wounds and atherosclerotic lesions Schober et al. 2003

Identification of a novel integrin alphaMbeta2 binding site in CCN1 (CYR61), a matricellular protein expressed in healing wounds and atherosclerotic lesions Schober et al. 2003

Interplay between rolling and firm adhesion elucidated with a cell-free system engineered with two distinct receptor-ligand pairs.Eniola AO et al. . The interaction between integrin lymphocyte function-associated antigen-1 (LFA-1) and its ligand intercellular adhesion molecule-1 (ICAM-1) is critical in immunological and inflammatory reactions,The extracellular domains of LFA-1 are composed of the large and complex αL and β2 subunits (Song et al. 2005).

Identification of integrin alpha(M)beta(2) as an adhesion receptor on peripheral blood monocytes for Cyr61 (CCN1) and connective tissue growth factor (CCN2): immediate-early gene products expressed in atherosclerotic lesions. Blood. 2002 .

The leukocyte integrin alpha-D beta-2 binds VCAM-1: evidence for a binding interface between I domain and VCAM-1 (Van der Vieren et al. 1999).

The integrin alpha-X-beta-2 has an important role in host defense. Alpha-X-beta-2 functions as a receptor for the complement C3 cleavage product iC3b (Micklem & Sim 1985), fibrinogen [(Loike et al. 1991)&1671533], and ICAM-1 (Diamond et al. 1993).

The integrin alpha-X-beta-2 has an important role in host defense. Alpha-X-beta-2 functions as a receptor for the complement C3 cleavage product iC3b (Micklem & Sim 1985), fibrinogen (Loike et al. 1991) , and ICAM-1 (Diamond et al. 1993).

The integrin alpha-X-beta-2 has an important role in host defense. Alpha-X-beta-2 functions as a receptor for the complement C3 cleavage product iC3b (Micklem & Sim 1985), fibrinogen (Loike et al. 1991), and ICAM-1 (Diamond et al. 1993).

(Song et al. 2005) reported a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the ligand-binding domain of integrin alpha-L-beta-2.

The extracellular domain of LFA-1 are composed of the large and complex integrin α-L and β2 subunits. Pig ICAM-2 expressed on stable transfectants supported firm adhesion of cells expressing human LFA-1 (Godwin et al. 2004).

ICAM-5 (telencephalin) is expressed on telencephalic neurons. ICAM-5 may act as a major adhesion molecule for leukocyte binding to neurons by binding to integrin alpha-L-beta-2 (Tian et al. 2000).

ICAM-4 is a red cell intercellular adhesion molecule. Cell transfectants expressing various integrins were used to demonstrate that integrins alpha-L-beta-2, alpha-M-beta-2, and alpha-IIb-beta-3 bind specifically and dose dependently to the recombinant ICAM-4-Fc protein. Cell surface ICAM-4 interacts with the cell surface alpha-V-beta-3 integrin (Hermand et al. 2004).

ICAM-4 is a red cell intercellular adhesion molecule. Cell transfectants expressing various integrins were used to demonstrate that integrins alpha-L-beta-2, alpha-M-beta-2, and alpha-IIb-beta-3 bind specifically and dose dependently to the recombinant ICAM-4-Fc protein. Cell surface ICAM-4 interacts with the cell surface alpha-V-beta-3 integrin (Hermand et al. 2004).