PubMed:7638186 JSONTXT

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"S2","span":{"begin":94,"end":228},"obj":"Sentence"},{"id":"S3","span":{"begin":229,"end":480},"obj":"Sentence"},{"id":"S4","span":{"begin":481,"end":737},"obj":"Sentence"},{"id":"S5","span":{"begin":738,"end":929},"obj":"Sentence"},{"id":"S6","span":{"begin":930,"end":1115},"obj":"Sentence"},{"id":"S7","span":{"begin":1116,"end":1283},"obj":"Sentence"}],"text":"Interleukin 12 induces tyrosine phosphorylation and activation of STAT4 in human lymphocytes.\nInterleukin 12 (IL-12) is an important immunoregulatory cytokine whose receptor is a member of the hematopoietin receptor superfamily. We have recently demonstrated that stimulation of human T and natural killer cells with IL-12 induces tyrosine phosphorylation of the Janus family tyrosine kinase JAK2 and Tyk2, implicating these kinases in the immediate biochemical response to IL-12. Recently, transcription factors known as STATs (signal transducers and activators of transcription) have been shown to be tyrosine phosphorylated and activated in response to a number of cytokines that bind hematopoietin receptors and activate JAK kinases. In this report we demonstrate that IL-12 induces tyrosine phosphorylation of a recently identified STAT family member, STAT4, and show that STAT4 expression is regulated by T-cell activation. Furthermore, we show that IL-12 stimulates formation of a DNA-binding complex that recognizes a DNA sequence previously shown to bind STAT proteins and that this complex contains STAT4. These data, and the recent demonstration of JAK phosphorylation by IL-12, identify a rapid signal-transduction pathway likely to mediate IL-12-induced gene expression."}

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