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发布于:2020-11-27 17:28:11  访问:3 次 回复:0 篇
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[7]["Compound T"
In contrast to the delayed and low induction of p in AT cells in response to IR, p was induced with UV irradiation in both and AT cell lines and normal lymphoblasts. With all three cell lines, p was phosphorylated on serine in response to UV irradiation. In response to a specific signal induced by UV irradiation, the increased levels of phosphoserine p correlated with increased levels of total p protein. In conclusion, p is specifically phosphorylated on serine in response to IR and UV irradiation in both normal and AT lymphoblasts.We asked whether the ability of p to transactivate downstream target genes was altered in SYY and ML cells that had been treated with ALLN as compared with irradiated cells.Cellular p protein levels were equivalent after treatment with IR or ALLN, and both treatments led to greater levels than that observed in unirradiated cells. Phosphorylation of p correlated with both induction of p protein and increased transcription of presponsive genes.We asked whether the differences in p transactivation sell Avapritinib activity could in part be explained by differential binding of p to specific DNA sequences in an electrophoretic mobility shift assay. SYY nuclear extracts were isolated hr after treatment of cells with m of ALLN or increasing doses of IR.The extent of p binding to an oligonucleotide containing the pwaf promoter binding site was compared among the different extracts.Specificity of DNA binding was verified by competition experiments with either fold excess wildtype and antibody supershift. We then asked whether p, which had been posttranslationally modified in response to IR, had altered stability when bound to DNA.We compared the dissociation rates of p from different lysates in an offrate experiment using pwaf oligonucleotide as probe.SYY nuclear lysates prepared from control, ALLN, or irradiated cells were incubated with labeled oligonucleotide until equilibrium was achieved.The rate at which p dissociated from the radiolabeled probe was measured after the addition of fold excess of wildtype, unlabeled probe. Discussion p is a critical mediator of cellular responses to genotoxic stress.Following DNA damage, there is a posttranscriptional induction of p protein and subsequent activation of p.The mechanism by which p becomes activated is unknown.Phosphorylation is one potential mechanism by which cells might regulate the activity of p after genotoxic stress.In vivo experiments have demonstrated clearly that p is a phosphoprotein. In vitro studies have identified multiple sites of phosphorylation within the amino and carboxyl termini within p.Although several kinases have been shown to phosphorylate specific sites within p in vitro, it has not yet been demonstrated that phosphorylation at these sites is important for the function and regulation of p in vivo.Phosphorylation at the carboxyl terminus of p may be important in this regulation.Several protein kinases have been demonstrated to phosphorylate p within this domain.In all cases, phosphorylation within the carboxyl terminus of p enhanced the ability of p to bind DNA in vitro.sell Avapritinib However, as is the case for phosphorylation sites within the amino terminus of p, de novo phosphorylation of p at the carboxyl terminus in response to a signal transduction pathway in vivo has not been demonstrated.
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