PubMed:20018936
Annnotations
bionlp-st-epi-2011-training
{"project":"bionlp-st-epi-2011-training","denotations":[{"id":"T1","span":{"begin":35,"end":45},"obj":"Protein"},{"id":"T2","span":{"begin":68,"end":91},"obj":"Protein"},{"id":"T3","span":{"begin":100,"end":117},"obj":"Protein"},{"id":"T4","span":{"begin":131,"end":154},"obj":"Protein"},{"id":"T5","span":{"begin":206,"end":235},"obj":"Protein"},{"id":"T6","span":{"begin":340,"end":345},"obj":"Protein"},{"id":"T7","span":{"begin":366,"end":373},"obj":"Protein"},{"id":"T8","span":{"begin":394,"end":399},"obj":"Protein"},{"id":"T9","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T10","span":{"begin":522,"end":527},"obj":"Protein"},{"id":"T11","span":{"begin":583,"end":593},"obj":"Protein"},{"id":"T12","span":{"begin":627,"end":632},"obj":"Protein"},{"id":"T13","span":{"begin":695,"end":717},"obj":"Protein"},{"id":"T14","span":{"begin":882,"end":890},"obj":"Protein"},{"id":"T15","span":{"begin":920,"end":959},"obj":"Protein"},{"id":"T16","span":{"begin":960,"end":961},"obj":"Protein"},{"id":"T17","span":{"begin":966,"end":1012},"obj":"Protein"},{"id":"T18","span":{"begin":1013,"end":1014},"obj":"Protein"},{"id":"T19","span":{"begin":1068,"end":1078},"obj":"Protein"},{"id":"T20","span":{"begin":1080,"end":1087},"obj":"Protein"},{"id":"T21","span":{"begin":1120,"end":1125},"obj":"Protein"},{"id":"T22","span":{"begin":1192,"end":1199},"obj":"Protein"},{"id":"T23","span":{"begin":1218,"end":1263},"obj":"Protein"},{"id":"T24","span":{"begin":1264,"end":1265},"obj":"Protein"},{"id":"T25","span":{"begin":1296,"end":1306},"obj":"Protein"},{"id":"T26","span":{"begin":1354,"end":1362},"obj":"Protein"},{"id":"T27","span":{"begin":1373,"end":1378},"obj":"Protein"},{"id":"T28","span":{"begin":1394,"end":1399},"obj":"Protein"},{"id":"T29","span":{"begin":1437,"end":1441},"obj":"Protein"},{"id":"T30","span":{"begin":1454,"end":1456},"obj":"Protein"},{"id":"T31","span":{"begin":1476,"end":1478},"obj":"Protein"},{"id":"T32","span":{"begin":1511,"end":1516},"obj":"Protein"},{"id":"T33","span":{"begin":1522,"end":1527},"obj":"Protein"},{"id":"T34","span":{"begin":1560,"end":1573},"obj":"Protein"},{"id":"T35","span":{"begin":1578,"end":1611},"obj":"Protein"},{"id":"T36","span":{"begin":1627,"end":1635},"obj":"Protein"},{"id":"T37","span":{"begin":1678,"end":1723},"obj":"Protein"},{"id":"T38","span":{"begin":1724,"end":1725},"obj":"Protein"},{"id":"T39","span":{"begin":1762,"end":1770},"obj":"Protein"},{"id":"T40","span":{"begin":1784,"end":1789},"obj":"Protein"},{"id":"T41","span":{"begin":1813,"end":1823},"obj":"Protein"},{"id":"T42","span":{"begin":1876,"end":1881},"obj":"Protein"}],"text":"Phosphorylation and acetylation of histone H3 and autoregulation by early growth response 1 mediate interleukin 1beta induction of early growth response 1 transcription.\nOBJECTIVE: The transcription factor early growth response (EGR)-1 has been implicated as a key vascular phenotypic switch through its control of inducible transcription. EGR-1 autoregulation, and histone modification in the EGR-1 promoter, represent key mechanisms in EGR-1 control, but have not been explored.\nMETHODS AND RESULTS: We demonstrate that EGR-1 regulates its own transcription and that this involves histone H3 phosphorylation and acetylation. EGR-1 transactivates its promoter in smooth muscle cells exposed to interleukin (IL) 1beta through a novel cis-acting element (-211/-203). PD98059, which inhibits mitogen-activated protein kinase kinase/extracellular regulated kinase (MEK/ERK) attenuates IL-1beta-inducible phosphorylation of extracellular signal-regulated kinase 1/2 and mitogen and stress-activated protein kinases 1/2; and reduces levels of phosphorylated and acetylated histone H3. Histone deacetylase inhibition enhances EGR-1 transcription in response to cytokine. Conversely, suppression of histone modification with mitogen and stress-activated protein kinase 1/2 short interfering RNA, or the histone H3 acetyltransferase inhibitor Garcinol, inhibits IL-1beta-inducible EGR-1 transcription. EGR-1 interacts with the acetyltransferase p300. Acetylated H3 and phosphorylated H3 are enriched at the promoter of EGR-1; and EGR-1 is enriched at the promoters of tissue factor and plasminogen activator inhibitor 1 in response to IL-1beta, and attenuated by PD98059, Garcinol, and mitogen and stress-activated protein kinase 1/2 short interfering RNA.\nCONCLUSIONS: IL-1beta induction of EGR-1 transcription involves histone H3 phosphorylation, acetylation, and autoregulation by EGR-1."}
Allie
{"project":"Allie","denotations":[{"id":"SS1_20018936_2_0","span":{"begin":206,"end":227},"obj":"expanded"},{"id":"SS2_20018936_2_0","span":{"begin":229,"end":232},"obj":"abbr"},{"id":"SS1_20018936_6_0","span":{"begin":695,"end":706},"obj":"expanded"},{"id":"SS2_20018936_6_0","span":{"begin":708,"end":710},"obj":"abbr"},{"id":"SS1_20018936_7_0","span":{"begin":790,"end":860},"obj":"expanded"},{"id":"SS2_20018936_7_0","span":{"begin":862,"end":869},"obj":"abbr"}],"relations":[{"id":"AE1_20018936_2_0","pred":"abbreviatedTo","subj":"SS1_20018936_2_0","obj":"SS2_20018936_2_0"},{"id":"AE1_20018936_6_0","pred":"abbreviatedTo","subj":"SS1_20018936_6_0","obj":"SS2_20018936_6_0"},{"id":"AE1_20018936_7_0","pred":"abbreviatedTo","subj":"SS1_20018936_7_0","obj":"SS2_20018936_7_0"}],"text":"Phosphorylation and acetylation of histone H3 and autoregulation by early growth response 1 mediate interleukin 1beta induction of early growth response 1 transcription.\nOBJECTIVE: The transcription factor early growth response (EGR)-1 has been implicated as a key vascular phenotypic switch through its control of inducible transcription. EGR-1 autoregulation, and histone modification in the EGR-1 promoter, represent key mechanisms in EGR-1 control, but have not been explored.\nMETHODS AND RESULTS: We demonstrate that EGR-1 regulates its own transcription and that this involves histone H3 phosphorylation and acetylation. EGR-1 transactivates its promoter in smooth muscle cells exposed to interleukin (IL) 1beta through a novel cis-acting element (-211/-203). PD98059, which inhibits mitogen-activated protein kinase kinase/extracellular regulated kinase (MEK/ERK) attenuates IL-1beta-inducible phosphorylation of extracellular signal-regulated kinase 1/2 and mitogen and stress-activated protein kinases 1/2; and reduces levels of phosphorylated and acetylated histone H3. Histone deacetylase inhibition enhances EGR-1 transcription in response to cytokine. Conversely, suppression of histone modification with mitogen and stress-activated protein kinase 1/2 short interfering RNA, or the histone H3 acetyltransferase inhibitor Garcinol, inhibits IL-1beta-inducible EGR-1 transcription. EGR-1 interacts with the acetyltransferase p300. Acetylated H3 and phosphorylated H3 are enriched at the promoter of EGR-1; and EGR-1 is enriched at the promoters of tissue factor and plasminogen activator inhibitor 1 in response to IL-1beta, and attenuated by PD98059, Garcinol, and mitogen and stress-activated protein kinase 1/2 short interfering RNA.\nCONCLUSIONS: IL-1beta induction of EGR-1 transcription involves histone H3 phosphorylation, acetylation, and autoregulation by EGR-1."}