PLK epitope and the transformation of growth factor receptor in signal

E EndoGalC that the overexpression PLK led to accelerated proliferation of NIH3T3 mouse fibroblasts. Pharmacological and biochemical analyzes have shown an association between the involved Gal epitope and the transformation of growth factor receptor in signal transduction. Taken together, we have revealed for the first time linked the existence of a new mechanism of signal transduction regulators with the sugar moiety. Results reduced Gal epitope in cells that led EndoGalC We an expression unit EndoGalC, CEGCN in NIH3T3 cells and stable transfectants were successfully obtained after G418 selection. A transfected cell lines were selected just increments and found Rabbit conjugated with fluorescein isothiocyanate lectin IB4 GS or GS II for their content of glycans on the cell Monitor surface expressed by flow cytometry. GS is a IB4 isolectin of Bandeiraea simplicifolia isolated which binds specifically to galactosyl residues non-reducing, including normal Gal epitope. Isolectin GS II binds specifically to the terminal GlcNAc residue, which would be the first sugar in the surface of the cell surface exposed to digestion with EndoGalC. The analysis by flow cytometry CEGCN 3T3 cells showed more than 96% reduction in the concentration of endogenous Gal epitope relative to that in transfected NIH3T3 cells. In addition, the quantity, the GlcNAc residues on the cell Surface of 3T3 cells that sugar is the terminal t CEGCN end of the chain No glycan is about 7 times exposed abundant relative to the untransfected NIH3T3 cells. These results show that the introduced gene is expressed EndoGalC functionability in 3T3 CEGCN and the resulting protein products Is hig. Erh Hte cell growth in cells that EndoGalC order correlations between the expression EndoGalC and receives To identify hte cell proliferation, we studied the growth of 3T3 cells and parental CEGCN untransfected NIH3T3 cells.
As shown in Figure 3A, was the proliferation by 60% faster in 3T3 CEGCN that transfected into NIH3T3 cells. Both 3T3 and NIH3T3 CEGCN reached a plateau at 5-t Pendent culture, although CEGCN 3T3 cells showed a tendency to lose contact inhibition. For example, multi-layered cell growth h Frequently observed in some culture wells, w While NIH3T3 cells did not show this kind of growth. In addition, this enzyme is not the glycan structure of the wild-type NIH3T3 cells, presumably because of the lack of expression of the GlcNAc residues on their cell surface Surface. Then, the equalized m Interactions between TR I and II in the N TR acetylglucosaminidase CEGCN 3T3 cells, which rated the Immunpr Zipitation method. I was executed together with TR Filled TR II, even after treatment with N-acetylglucosaminidase. In contrast, no interaction between TR I and TR II in wild-type NIH3T3 cells was found, even if they were incubated with serum-free medium. These results show that the GlcNAc residues are not sensitive to N-acetylglucosaminidase in ligand-independent Independent activation of TRS are involved in EndoGalC expressing cells, although we exclusively not S that Residues Walls exposed GcNAc that are resistant to enzymatic digestion are involved in the activation. Close Of course, we examined the level of protein phosphorylation in 3T3 Smad2 EC.

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