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Selectins transmembrane glycoproteins

Cell adhesion molecules (CAMs) are transmembrane glycoproteins that act at the cell surface to mediate specific binding interactions with other cell adhesion molecules on adjacent cells or with proteins in the extracellular matrix. They are responsible for the adhesion of various leukocytes with each other, with extracellular matrix and with other cell types. Several classes of molecules capable of mediating adhesion include selectins, integrins, cadherins, and immunoglobulin superfamily members [263-265]. Multiple members from every major family of cell adhesion molecules have been implicated in the development, maintenance, or repair of renal tissues... [Pg.112]

The three selectins are related both structurally and functionally. They are transmembrane proteins, with an N-terminal C-type actin domain, followed by an EGF repeat and a variable number of complement control protein (CCP) domains. Selectins bind carbohydrates, which are present in various glycoproteins. [Pg.1112]

Selectins are transmembrane proteins with membrane-distal Ca +-dependent lectin domains. This family of cell adhesion molecules is involved in the tethering and rolling of leukocytes on the blood vessel endothelium. Nicholson and colleagues [10] published the analysis of leukocyte selectin, CD62L, binding to the mucin-like glycoprotein, Gly-CAM-1. [Pg.1054]


See other pages where Selectins transmembrane glycoproteins is mentioned: [Pg.42]    [Pg.42]    [Pg.837]    [Pg.828]    [Pg.235]    [Pg.28]    [Pg.40]    [Pg.43]    [Pg.228]    [Pg.96]    [Pg.192]    [Pg.1788]    [Pg.209]    [Pg.262]    [Pg.216]    [Pg.316]    [Pg.314]    [Pg.220]    [Pg.985]   
See also in sourсe #XX -- [ Pg.235 ]




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