PubMed:9278334 JSONTXT

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    Inflammaging

    {"project":"Inflammaging","denotations":[{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":214},"obj":"Sentence"},{"id":"T3","span":{"begin":215,"end":334},"obj":"Sentence"},{"id":"T4","span":{"begin":335,"end":478},"obj":"Sentence"},{"id":"T5","span":{"begin":479,"end":613},"obj":"Sentence"},{"id":"T6","span":{"begin":614,"end":865},"obj":"Sentence"},{"id":"T7","span":{"begin":866,"end":1113},"obj":"Sentence"},{"id":"T8","span":{"begin":1114,"end":1310},"obj":"Sentence"},{"id":"T9","span":{"begin":1311,"end":1482},"obj":"Sentence"},{"id":"T10","span":{"begin":1483,"end":1724},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":214},"obj":"Sentence"},{"id":"T3","span":{"begin":215,"end":334},"obj":"Sentence"},{"id":"T4","span":{"begin":335,"end":478},"obj":"Sentence"},{"id":"T5","span":{"begin":479,"end":613},"obj":"Sentence"},{"id":"T6","span":{"begin":614,"end":865},"obj":"Sentence"},{"id":"T7","span":{"begin":866,"end":1113},"obj":"Sentence"},{"id":"T8","span":{"begin":1114,"end":1310},"obj":"Sentence"},{"id":"T9","span":{"begin":1311,"end":1482},"obj":"Sentence"},{"id":"T10","span":{"begin":1483,"end":1724},"obj":"Sentence"}],"text":"Human monocyte binding to fibronectin enhances IFN-gamma-induced early signaling events.\nLeukocyte integrins are fundamentally important in modulating adhesion to extracellular matrix components and to other cells. This integrin-mediated adhesion controls leukocyte arrest and extravasation during the onset of inflammatory responses. Moreover, integrin-ligand interactions trigger signaling pathways that may influence leukocyte phenotype and function at sites of inflammation. In the current studies, we evaluated the combinatorial effects of monocyte adhesion and IFN-gamma on intracellular signaling pathways. IFN-gamma triggers a well-defined signal transduction pathway, which although not directly stimulated by monocyte adherence to fibronectin or arginine-glycine-aspartate (RGD)-coated substrata, was enhanced significantly in these matrix-adherent cells. Compared with monocytes in suspension or adherent on plastic surfaces, monocytes adherent to fibronectin or RGD exhibited a greater than threefold increase in steady state levels of IFN-gamma-induced mRNA for the high affinity Fc gammaRI receptor. By electrophoretic mobility shift assays, this increase in mRNA was associated with a 5- to 10-fold increase in the STAT1-containing DNA-binding complex that binds to Fc gammaRI promoter elements. Furthermore, the tyrosine phosphorylation of STAT1 and the tyrosine kinases JAK1 and JAK2 was enhanced significantly in RGD-adherent monocytes compared with control cells. These results suggest a novel mechanism by which integrin-mediated cell adhesion can modulate the magnitude of cytokine-induced signal transduction pathways, thereby amplifying cellular events leading to monocyte activation and inflammation."}

    jnlpba-st-training

    {"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":0,"end":14},"obj":"cell_type"},{"id":"T2","span":{"begin":26,"end":37},"obj":"protein"},{"id":"T3","span":{"begin":47,"end":56},"obj":"protein"},{"id":"T4","span":{"begin":89,"end":108},"obj":"protein"},{"id":"T5","span":{"begin":345,"end":353},"obj":"protein"},{"id":"T6","span":{"begin":567,"end":576},"obj":"protein"},{"id":"T7","span":{"begin":614,"end":623},"obj":"protein"},{"id":"T8","span":{"begin":741,"end":752},"obj":"protein"},{"id":"T9","span":{"begin":756,"end":805},"obj":"protein"},{"id":"T10","span":{"begin":843,"end":864},"obj":"cell_type"},{"id":"T11","span":{"begin":959,"end":970},"obj":"protein"},{"id":"T12","span":{"begin":1048,"end":1070},"obj":"RNA"},{"id":"T13","span":{"begin":1079,"end":1112},"obj":"protein"},{"id":"T14","span":{"begin":1173,"end":1177},"obj":"RNA"},{"id":"T15","span":{"begin":1230,"end":1266},"obj":"protein"},{"id":"T16","span":{"begin":1281,"end":1309},"obj":"DNA"},{"id":"T17","span":{"begin":1356,"end":1361},"obj":"protein"},{"id":"T18","span":{"begin":1370,"end":1386},"obj":"protein"},{"id":"T19","span":{"begin":1387,"end":1391},"obj":"protein"},{"id":"T20","span":{"begin":1396,"end":1400},"obj":"protein"},{"id":"T21","span":{"begin":1431,"end":1453},"obj":"cell_type"},{"id":"T22","span":{"begin":1468,"end":1481},"obj":"cell_type"},{"id":"T23","span":{"begin":1532,"end":1540},"obj":"protein"},{"id":"T24","span":{"begin":1594,"end":1602},"obj":"protein"}],"text":"Human monocyte binding to fibronectin enhances IFN-gamma-induced early signaling events.\nLeukocyte integrins are fundamentally important in modulating adhesion to extracellular matrix components and to other cells. This integrin-mediated adhesion controls leukocyte arrest and extravasation during the onset of inflammatory responses. Moreover, integrin-ligand interactions trigger signaling pathways that may influence leukocyte phenotype and function at sites of inflammation. In the current studies, we evaluated the combinatorial effects of monocyte adhesion and IFN-gamma on intracellular signaling pathways. IFN-gamma triggers a well-defined signal transduction pathway, which although not directly stimulated by monocyte adherence to fibronectin or arginine-glycine-aspartate (RGD)-coated substrata, was enhanced significantly in these matrix-adherent cells. Compared with monocytes in suspension or adherent on plastic surfaces, monocytes adherent to fibronectin or RGD exhibited a greater than threefold increase in steady state levels of IFN-gamma-induced mRNA for the high affinity Fc gammaRI receptor. By electrophoretic mobility shift assays, this increase in mRNA was associated with a 5- to 10-fold increase in the STAT1-containing DNA-binding complex that binds to Fc gammaRI promoter elements. Furthermore, the tyrosine phosphorylation of STAT1 and the tyrosine kinases JAK1 and JAK2 was enhanced significantly in RGD-adherent monocytes compared with control cells. These results suggest a novel mechanism by which integrin-mediated cell adhesion can modulate the magnitude of cytokine-induced signal transduction pathways, thereby amplifying cellular events leading to monocyte activation and inflammation."}

    pubmed-sentences-benchmark

    {"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"S2","span":{"begin":89,"end":214},"obj":"Sentence"},{"id":"S3","span":{"begin":215,"end":334},"obj":"Sentence"},{"id":"S4","span":{"begin":335,"end":478},"obj":"Sentence"},{"id":"S5","span":{"begin":479,"end":613},"obj":"Sentence"},{"id":"S6","span":{"begin":614,"end":865},"obj":"Sentence"},{"id":"S7","span":{"begin":866,"end":1113},"obj":"Sentence"},{"id":"S8","span":{"begin":1114,"end":1310},"obj":"Sentence"},{"id":"S9","span":{"begin":1311,"end":1482},"obj":"Sentence"},{"id":"S10","span":{"begin":1483,"end":1724},"obj":"Sentence"}],"text":"Human monocyte binding to fibronectin enhances IFN-gamma-induced early signaling events.\nLeukocyte integrins are fundamentally important in modulating adhesion to extracellular matrix components and to other cells. This integrin-mediated adhesion controls leukocyte arrest and extravasation during the onset of inflammatory responses. Moreover, integrin-ligand interactions trigger signaling pathways that may influence leukocyte phenotype and function at sites of inflammation. In the current studies, we evaluated the combinatorial effects of monocyte adhesion and IFN-gamma on intracellular signaling pathways. IFN-gamma triggers a well-defined signal transduction pathway, which although not directly stimulated by monocyte adherence to fibronectin or arginine-glycine-aspartate (RGD)-coated substrata, was enhanced significantly in these matrix-adherent cells. Compared with monocytes in suspension or adherent on plastic surfaces, monocytes adherent to fibronectin or RGD exhibited a greater than threefold increase in steady state levels of IFN-gamma-induced mRNA for the high affinity Fc gammaRI receptor. By electrophoretic mobility shift assays, this increase in mRNA was associated with a 5- to 10-fold increase in the STAT1-containing DNA-binding complex that binds to Fc gammaRI promoter elements. Furthermore, the tyrosine phosphorylation of STAT1 and the tyrosine kinases JAK1 and JAK2 was enhanced significantly in RGD-adherent monocytes compared with control cells. These results suggest a novel mechanism by which integrin-mediated cell adhesion can modulate the magnitude of cytokine-induced signal transduction pathways, thereby amplifying cellular events leading to monocyte activation and inflammation."}

    genia-medco-coref

    {"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":26,"end":37},"obj":"NP"},{"id":"C2","span":{"begin":215,"end":246},"obj":"NP"},{"id":"C3","span":{"begin":382,"end":400},"obj":"NP"},{"id":"C4","span":{"begin":401,"end":405},"obj":"NP"},{"id":"C5","span":{"begin":567,"end":576},"obj":"NP"},{"id":"C6","span":{"begin":614,"end":623},"obj":"NP"},{"id":"C7","span":{"begin":633,"end":675},"obj":"NP"},{"id":"C8","span":{"begin":677,"end":682},"obj":"NP"},{"id":"C9","span":{"begin":741,"end":752},"obj":"NP"},{"id":"C10","span":{"begin":959,"end":970},"obj":"NP"},{"id":"C11","span":{"begin":1048,"end":1070},"obj":"NP"},{"id":"C12","span":{"begin":1173,"end":1177},"obj":"NP"},{"id":"C13","span":{"begin":1226,"end":1266},"obj":"NP"},{"id":"C14","span":{"begin":1267,"end":1271},"obj":"NP"},{"id":"C15","span":{"begin":1505,"end":1522},"obj":"NP"},{"id":"C16","span":{"begin":1526,"end":1531},"obj":"NP"},{"id":"C17","span":{"begin":1532,"end":1563},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-relat","subj":"C4","obj":"C3"},{"id":"R2","pred":"coref-ident","subj":"C6","obj":"C5"},{"id":"R3","pred":"coref-relat","subj":"C8","obj":"C7"},{"id":"R4","pred":"coref-ident","subj":"C9","obj":"C1"},{"id":"R5","pred":"coref-ident","subj":"C10","obj":"C9"},{"id":"R6","pred":"coref-ident","subj":"C12","obj":"C11"},{"id":"R7","pred":"coref-relat","subj":"C14","obj":"C13"},{"id":"R8","pred":"coref-relat","subj":"C16","obj":"C15"},{"id":"R9","pred":"coref-ident","subj":"C17","obj":"C2"}],"text":"Human monocyte binding to fibronectin enhances IFN-gamma-induced early signaling events.\nLeukocyte integrins are fundamentally important in modulating adhesion to extracellular matrix components and to other cells. This integrin-mediated adhesion controls leukocyte arrest and extravasation during the onset of inflammatory responses. Moreover, integrin-ligand interactions trigger signaling pathways that may influence leukocyte phenotype and function at sites of inflammation. In the current studies, we evaluated the combinatorial effects of monocyte adhesion and IFN-gamma on intracellular signaling pathways. IFN-gamma triggers a well-defined signal transduction pathway, which although not directly stimulated by monocyte adherence to fibronectin or arginine-glycine-aspartate (RGD)-coated substrata, was enhanced significantly in these matrix-adherent cells. Compared with monocytes in suspension or adherent on plastic surfaces, monocytes adherent to fibronectin or RGD exhibited a greater than threefold increase in steady state levels of IFN-gamma-induced mRNA for the high affinity Fc gammaRI receptor. By electrophoretic mobility shift assays, this increase in mRNA was associated with a 5- to 10-fold increase in the STAT1-containing DNA-binding complex that binds to Fc gammaRI promoter elements. Furthermore, the tyrosine phosphorylation of STAT1 and the tyrosine kinases JAK1 and JAK2 was enhanced significantly in RGD-adherent monocytes compared with control cells. These results suggest a novel mechanism by which integrin-mediated cell adhesion can modulate the magnitude of cytokine-induced signal transduction pathways, thereby amplifying cellular events leading to monocyte activation and inflammation."}

    GENIAcorpus

    {"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":0,"end":14},"obj":"cell_type"},{"id":"T2","span":{"begin":26,"end":37},"obj":"protein_family_or_group"},{"id":"T3","span":{"begin":47,"end":56},"obj":"protein_molecule"},{"id":"T4","span":{"begin":89,"end":108},"obj":"protein_family_or_group"},{"id":"T5","span":{"begin":163,"end":194},"obj":"cell_component"},{"id":"T6","span":{"begin":256,"end":272},"obj":"other_name"},{"id":"T7","span":{"begin":311,"end":333},"obj":"other_name"},{"id":"T8","span":{"begin":345,"end":353},"obj":"protein_family_or_group"},{"id":"T9","span":{"begin":456,"end":477},"obj":"other_name"},{"id":"T10","span":{"begin":545,"end":562},"obj":"other_name"},{"id":"T11","span":{"begin":567,"end":576},"obj":"protein_molecule"},{"id":"T12","span":{"begin":580,"end":612},"obj":"other_name"},{"id":"T13","span":{"begin":614,"end":623},"obj":"protein_molecule"},{"id":"T14","span":{"begin":719,"end":737},"obj":"other_name"},{"id":"T15","span":{"begin":741,"end":752},"obj":"protein_family_or_group"},{"id":"T16","span":{"begin":756,"end":805},"obj":"protein_family_or_group"},{"id":"T17","span":{"begin":843,"end":864},"obj":"cell_type"},{"id":"T18","span":{"begin":919,"end":935},"obj":"other_organic_compound"},{"id":"T19","span":{"begin":959,"end":970},"obj":"protein_family_or_group"},{"id":"T20","span":{"begin":974,"end":977},"obj":"peptide"},{"id":"T21","span":{"begin":1048,"end":1057},"obj":"protein_molecule"},{"id":"T22","span":{"begin":1079,"end":1112},"obj":"protein_molecule"},{"id":"T23","span":{"begin":1117,"end":1154},"obj":"other_name"},{"id":"T24","span":{"begin":1173,"end":1177},"obj":"RNA_family_or_group"},{"id":"T25","span":{"begin":1230,"end":1266},"obj":"protein_complex"},{"id":"T26","span":{"begin":1281,"end":1309},"obj":"DNA_domain_or_region"},{"id":"T27","span":{"begin":1356,"end":1361},"obj":"protein_molecule"},{"id":"T28","span":{"begin":1370,"end":1386},"obj":"protein_family_or_group"},{"id":"T29","span":{"begin":1387,"end":1391},"obj":"protein_molecule"},{"id":"T30","span":{"begin":1396,"end":1400},"obj":"protein_molecule"},{"id":"T31","span":{"begin":1431,"end":1434},"obj":"peptide"},{"id":"T32","span":{"begin":1468,"end":1481},"obj":"cell_type"},{"id":"T33","span":{"begin":1532,"end":1540},"obj":"protein_family_or_group"},{"id":"T34","span":{"begin":1594,"end":1602},"obj":"protein_family_or_group"},{"id":"T35","span":{"begin":1660,"end":1675},"obj":"other_name"},{"id":"T36","span":{"begin":1687,"end":1706},"obj":"other_name"},{"id":"T37","span":{"begin":1711,"end":1723},"obj":"other_name"}],"text":"Human monocyte binding to fibronectin enhances IFN-gamma-induced early signaling events.\nLeukocyte integrins are fundamentally important in modulating adhesion to extracellular matrix components and to other cells. This integrin-mediated adhesion controls leukocyte arrest and extravasation during the onset of inflammatory responses. Moreover, integrin-ligand interactions trigger signaling pathways that may influence leukocyte phenotype and function at sites of inflammation. In the current studies, we evaluated the combinatorial effects of monocyte adhesion and IFN-gamma on intracellular signaling pathways. IFN-gamma triggers a well-defined signal transduction pathway, which although not directly stimulated by monocyte adherence to fibronectin or arginine-glycine-aspartate (RGD)-coated substrata, was enhanced significantly in these matrix-adherent cells. Compared with monocytes in suspension or adherent on plastic surfaces, monocytes adherent to fibronectin or RGD exhibited a greater than threefold increase in steady state levels of IFN-gamma-induced mRNA for the high affinity Fc gammaRI receptor. By electrophoretic mobility shift assays, this increase in mRNA was associated with a 5- to 10-fold increase in the STAT1-containing DNA-binding complex that binds to Fc gammaRI promoter elements. Furthermore, the tyrosine phosphorylation of STAT1 and the tyrosine kinases JAK1 and JAK2 was enhanced significantly in RGD-adherent monocytes compared with control cells. These results suggest a novel mechanism by which integrin-mediated cell adhesion can modulate the magnitude of cytokine-induced signal transduction pathways, thereby amplifying cellular events leading to monocyte activation and inflammation."}