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Cell adhesion, integrin-recognition

Figure 48-3. Schematic representation of fibronectin. Seven functional domains of fibronectin are represented two different types of domain for heparin, cell-binding, and fibrin are shown. The domains are composed of various combinations of three structural motifs (I, II, and III), not depicted in the figure. Also not shown is the fact that fibronectin is a dimer joined by disulfide bridges near the carboxyl terminals of the monomers. The approximate location of the RGD sequence of fibronectin, which interacts with a variety of fibronectin integrin receptors on cell surfaces, is indicated by the arrow. (Redrawn after Yamada KM Adhesive recognition sequences. Figure 48-3. Schematic representation of fibronectin. Seven functional domains of fibronectin are represented two different types of domain for heparin, cell-binding, and fibrin are shown. The domains are composed of various combinations of three structural motifs (I, II, and III), not depicted in the figure. Also not shown is the fact that fibronectin is a dimer joined by disulfide bridges near the carboxyl terminals of the monomers. The approximate location of the RGD sequence of fibronectin, which interacts with a variety of fibronectin integrin receptors on cell surfaces, is indicated by the arrow. (Redrawn after Yamada KM Adhesive recognition sequences.
Figure 48-4. Schematic representation of a cell interacting through various integrin receptors with collagen, fibronectin, and laminin present in the ECM. (Specific subunits are not indicated.) (Redrawn after Yamada KM Adhesive recognition sequences. J Biol Chem 1991 266 12809.)... Figure 48-4. Schematic representation of a cell interacting through various integrin receptors with collagen, fibronectin, and laminin present in the ECM. (Specific subunits are not indicated.) (Redrawn after Yamada KM Adhesive recognition sequences. J Biol Chem 1991 266 12809.)...
Cheresh, D. A., Berliner, S. A., Vicente, V., and Ruggeri, Z. M. (1989). Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells. Cell 58, 945-953. [Pg.286]

Diamond, M. S., Garcia-Aguilar, J., Bickford, J. K., Corbi, A. L., and Springer, T. A. (1993). The I domain is a major recognition site on the leukocyte integrin Mac-1 (CDllb/CD18) for four distinct adhesion ligands. J. Cell. Biol. 120, 1031-1043. [Pg.58]

Chereih DA, Berliner SA, Vicente V, Ruggeri ZM Recognition of distinct adhesive sites on fibrinogen by rdated integrins on platdet and endothelial cdls. Cell 1989 58 945-953. [Pg.339]

The inflammatory response is initiated by stimuli released from sites of tissue injury that results in the expression of selectins on the endothelial layer. These selectins (E(endothelial)-selectin and P(platelet)-selectin) function through recognition of oligosaccharides on the opposing leukocyte cell surface [194]. This interaction eventually weakly tethers the leukocyte to the endothelial layer, at which point integrin binding events lead to firm adhesion and extravasation of the leukocyte into the tissue. In certain disease processes, excessive leukoc)4e infiltration becomes deleterious to the body, and inhibitors of this process are desirable. Rheumatoid arthritis, asthma, organ transplant rejection, and reperfusion injury are just a few of the cases in which these events occur [27]. [Pg.1843]

Shimizu, Y., van Seventer, G., Morgan, K. J., and Shaw, S., Role of adhesion molecules in T-cell recognition. Fundamental similarities between four integrins on resting human T cells (LFA-1, VLA-4, VLA-6) in expression, binding and costimulation, Immunol. Rev., 114, 109, 1992. [Pg.110]


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