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Fc receptor-y-chain

Differences in Fc receptor y-chain transmembrane domains (particularly polar or charged residues among the C-terminal 11 amino acids) influence cell membrane receptor expression and function [91]. The charged residues might protect Fc RI and FcYRIIIa receptors during membrane-associated receptor recycling in proteasomes associated with the endoplasmic reticulum or other intracellular structures [91]. [Pg.251]

Collagen signals through the same pathway as that of immune receptors. It induces phosphorylation on tyrosine on Fc receptor y-chain (FcRy), the non-receptor tyrosine kinase Syk and phospholipase Cy2 (PLCy2) . [Pg.90]

Gibbins J, Asselin J, Famdale R, Barnes M, Law CL, Watson SP Tyrosine ]dioephotylation of the Fc receptor y-chain in collagen-stimulated platelets.. J Biol Chem 271 18095-18099,1996... [Pg.100]

Tsuji M, Ezumi Y, Aral M, Takayama H A novel association of Fc recqitor y-chain with glycoprotein VI and frieirco-erqnession as a collagen receptor in human platelets. J Biol Chem 272 23528-23531, 1997... [Pg.100]

Figure 31-6 Three-dimensional ribbon representation of the structure of a complex of a soluble Fc fragment of a human IgGl molecule. Pro 329 of the IgG and Trp 87 and Trp 110 of the Fc-receptor fragment form a "proline sandwich/ which is shown in ball-and-stick form. The oligosaccharide attached to the Fc fragment of the antibody and the disulfide bridge between the two Cys 229 residues (at the N termini of the C2 domains of the heavy y chains) are also shown. The small spheres on the Fc receptor fragment are potential sites for N-glycosylation. From Sondermann et al.107 Courtesy of Uwe Jacob. Figure 31-6 Three-dimensional ribbon representation of the structure of a complex of a soluble Fc fragment of a human IgGl molecule. Pro 329 of the IgG and Trp 87 and Trp 110 of the Fc-receptor fragment form a "proline sandwich/ which is shown in ball-and-stick form. The oligosaccharide attached to the Fc fragment of the antibody and the disulfide bridge between the two Cys 229 residues (at the N termini of the C2 domains of the heavy y chains) are also shown. The small spheres on the Fc receptor fragment are potential sites for N-glycosylation. From Sondermann et al.107 Courtesy of Uwe Jacob.
Fig. 12. Tentative model of the signal transduction chain that links the perception of pectic fragments to defense responses in carrot cells. Abbreviations apy, heterotrimeric G protein CaM, calmodulin 4CL, 4-coumarate-CoA ligase CTX, cholera toxin FC, fusicoccine GDP-P-S and GTP-y-S, guanosine 5 -0-(2-thiodiphosphate) and guanosine 5 -0-(3-thiotriphosphate) IP3, 1,4,5-inositol trisphosphate PAL, phenylalanine ammonia-lyase PLC, phospholipase C PR, pathogenesis related PTX, pertussis toxin Rc, receptor SP, staurosporine. Activation and inhibition are symbolized by + and -respectively. Fig. 12. Tentative model of the signal transduction chain that links the perception of pectic fragments to defense responses in carrot cells. Abbreviations apy, heterotrimeric G protein CaM, calmodulin 4CL, 4-coumarate-CoA ligase CTX, cholera toxin FC, fusicoccine GDP-P-S and GTP-y-S, guanosine 5 -0-(2-thiodiphosphate) and guanosine 5 -0-(3-thiotriphosphate) IP3, 1,4,5-inositol trisphosphate PAL, phenylalanine ammonia-lyase PLC, phospholipase C PR, pathogenesis related PTX, pertussis toxin Rc, receptor SP, staurosporine. Activation and inhibition are symbolized by + and -respectively.

See other pages where Fc receptor-y-chain is mentioned: [Pg.358]    [Pg.359]    [Pg.62]    [Pg.96]    [Pg.35]    [Pg.206]    [Pg.358]    [Pg.359]    [Pg.62]    [Pg.96]    [Pg.35]    [Pg.206]    [Pg.50]    [Pg.160]    [Pg.207]    [Pg.208]    [Pg.248]    [Pg.345]    [Pg.1030]    [Pg.1571]    [Pg.194]    [Pg.437]    [Pg.44]    [Pg.437]    [Pg.208]    [Pg.70]    [Pg.5]    [Pg.39]   
See also in sourсe #XX -- [ Pg.383 , Pg.384 ]




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