To determine cells DCB, whether the Wee1 signal transmission occurs as a result of aberrant activation TR. Smad2 phosphorylation is observed when cells were 3T3 CEGCN in the presence of SB431542, but not cultured with TGF. In addition, Smad2 phosphorylated in NIH3T3 cells after stimulation with TGF 1 untransfected and phosphorylation was inhibited by the addition of SB431542. A hypothesis that the abnormal signal transduction from the elimination of Gal epitope and transfer the signal transduction cascade TR is shown in Figure 9. The focus Gal epitope at the nonreducing end of the chain arranged No glycan, and the GlcNAc residue consists of the Gal epitope. When NIH3T3 cells were transfected with an expression vector EndoGalC, were the levels of Gal epitopes on their cell surface Che significantly reduced. Cytochemical F Staining with GS-II lectin, which Recogn t particularly the GlcNAc residue, reveals the appearance of the GlcNAc residue on the cell Surface of these cells. Interestingly, cells that EndoGalC verst Markets cell growth and are anf Lliger as non-transfected NIH3T3 cells TR-I inhibitors a correlation between the glycan and antennal TR-mediated signal transduction. For the first time, we make a correlation between the above-glycan and TR-mediated signal transduction. There are two assumptions about the activation in the cells, TR EndoGalC: independently of the Gal-epitope on the functions of TRs in blocking their aberrant activation break ngigen ligands, and the treatment with EndoGalC these machines k can and activated by the TR GlcNAc residue, which is suspended due to digestion of the Gal epitope with EndoGalC, although the mechanism of this activation is not known.
Previously, the extracellular Ren Dom NEN of TR has been reported that the ligand arrangement independent To prevent aberrant signaling and Independent. Furthermore, it was also reported that extracellular TR I and II and three glycosylation sites on the TR Ren has cathedral Ne are. Analysis of the cells treated Nacetylglucosaminidase noted that about 72% of the GlcNAc residues, which are exposed only after digestion EndoGalC, always on the cell is Che present. Even under these conditions we have observed the interaction between ligand-independent Ngigen TR I and II TR. Therefore, we could not get the M Opportunity exclusively S is that the GlcNAc residue involved in TR activation. In other words, we k Can not now say that the case is provided in Figure 9 v Llig is rigid. Fafeur et al. reported that signal transduction was inhibited when the level was reduced glycosylation of TRs significant. In Similar way Goetschy et al. reported that the affinity t of the non-glycosylated TR II TGF to 3 thousand receptors, which was normally glycosylated. Thus can the Warmth IMDb play multiple glycan r Important in the TGF-signaling, additionally Tzlich conveys to the negative regulation of signal transduction by TR. It was reported that the core fucose and GlcNAc halved, which were included as components of cytokine receptors, directly comparable Changes the cytokine-receptor-mediated signal transduction. Therefore, the structure of the epitope with Gal function as a novel modified.