PubMed:8419931 JSONTXT

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":161},"obj":"Sentence"},{"id":"S2","span":{"begin":162,"end":314},"obj":"Sentence"},{"id":"S3","span":{"begin":315,"end":615},"obj":"Sentence"},{"id":"S4","span":{"begin":616,"end":749},"obj":"Sentence"},{"id":"S5","span":{"begin":750,"end":926},"obj":"Sentence"},{"id":"S6","span":{"begin":927,"end":1094},"obj":"Sentence"}],"text":"Tyrosine phosphorylation is a mandatory proximal step in radiation-induced activation of the protein kinase C signaling pathway in human B-lymphocyte precursors.\nIonizing radiation triggers a signal in human B-lymphocyte precursors that is intimately linked to an active protein-tyrosine kinase regulatory pathway. We show that in B-lymphocyte precursors, irradiation with gamma-rays leads to (i) stimulation of phosphatidylinositol turnover; (ii) downstream activation by covalent modification of multiple serine-specific protein kinases, including protein kinase C; and (iii) activation of nuclear factor kappa B. All of the radiation-induced signals were effectively prevented by the protein-tyrosine kinase inhibitors genistein and herbimycin A. Thus, tyrosine phosphorylation is an important and perhaps mandatory proximal step in the activation of the protein kinase C signaling cascade in human B-lymphocyte precursors. Our report expands current knowledge of the radiation-induced signaling cascade by clarifying the chronological sequence of biochemical events that follow irradiation."}

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