PubMed:7499266 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":160},"obj":"Sentence"},{"id":"T2","span":{"begin":161,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":419},"obj":"Sentence"},{"id":"T4","span":{"begin":420,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":888},"obj":"Sentence"},{"id":"T7","span":{"begin":889,"end":1118},"obj":"Sentence"},{"id":"T8","span":{"begin":1119,"end":1374},"obj":"Sentence"},{"id":"T9","span":{"begin":1375,"end":1611},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":160},"obj":"Sentence"},{"id":"T2","span":{"begin":161,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":419},"obj":"Sentence"},{"id":"T4","span":{"begin":420,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":888},"obj":"Sentence"},{"id":"T7","span":{"begin":889,"end":1118},"obj":"Sentence"},{"id":"T8","span":{"begin":1119,"end":1374},"obj":"Sentence"},{"id":"T9","span":{"begin":1375,"end":1611},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":21,"end":62},"obj":"protein"},{"id":"T2","span":{"begin":68,"end":93},"obj":"cell_line"},{"id":"T3","span":{"begin":119,"end":140},"obj":"protein"},{"id":"T4","span":{"begin":144,"end":159},"obj":"protein"},{"id":"T5","span":{"begin":161,"end":183},"obj":"protein"},{"id":"T6","span":{"begin":185,"end":195},"obj":"protein"},{"id":"T7","span":{"begin":269,"end":278},"obj":"protein"},{"id":"T8","span":{"begin":337,"end":352},"obj":"protein"},{"id":"T9","span":{"begin":535,"end":545},"obj":"protein"},{"id":"T10","span":{"begin":583,"end":598},"obj":"protein"},{"id":"T11","span":{"begin":652,"end":658},"obj":"protein"},{"id":"T12","span":{"begin":685,"end":725},"obj":"cell_line"},{"id":"T13","span":{"begin":727,"end":732},"obj":"cell_line"},{"id":"T14","span":{"begin":777,"end":792},"obj":"protein"},{"id":"T15","span":{"begin":835,"end":850},"obj":"protein"},{"id":"T16","span":{"begin":850,"end":863},"obj":"protein"},{"id":"T17","span":{"begin":876,"end":887},"obj":"cell_line"},{"id":"T18","span":{"begin":912,"end":921},"obj":"protein"},{"id":"T19","span":{"begin":1001,"end":1022},"obj":"protein"},{"id":"T20","span":{"begin":1036,"end":1042},"obj":"protein"},{"id":"T21","span":{"begin":1074,"end":1098},"obj":"protein"},{"id":"T22","span":{"begin":1102,"end":1117},"obj":"protein"},{"id":"T23","span":{"begin":1176,"end":1200},"obj":"protein"},{"id":"T24","span":{"begin":1204,"end":1219},"obj":"protein"},{"id":"T25","span":{"begin":1245,"end":1255},"obj":"protein"},{"id":"T26","span":{"begin":1318,"end":1333},"obj":"protein"},{"id":"T27","span":{"begin":1362,"end":1373},"obj":"cell_line"},{"id":"T28","span":{"begin":1408,"end":1420},"obj":"protein"},{"id":"T29","span":{"begin":1504,"end":1521},"obj":"protein"},{"id":"T30","span":{"begin":1525,"end":1540},"obj":"protein"},{"id":"T31","span":{"begin":1576,"end":1586},"obj":"protein"},{"id":"T32","span":{"begin":1587,"end":1610},"obj":"protein"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":18,"end":62},"obj":"NP"},{"id":"C2","span":{"begin":66,"end":93},"obj":"NP"},{"id":"C4","span":{"begin":115,"end":118},"obj":"NP"},{"id":"C5","span":{"begin":144,"end":159},"obj":"NP"},{"id":"C3","span":{"begin":115,"end":159},"obj":"NP"},{"id":"C6","span":{"begin":161,"end":196},"obj":"NP"},{"id":"C8","span":{"begin":337,"end":352},"obj":"NP"},{"id":"C7","span":{"begin":310,"end":352},"obj":"NP"},{"id":"C9","span":{"begin":354,"end":359},"obj":"NP"},{"id":"C10","span":{"begin":535,"end":545},"obj":"NP"},{"id":"C12","span":{"begin":650,"end":658},"obj":"NP"},{"id":"C13","span":{"begin":681,"end":725},"obj":"NP"},{"id":"C14","span":{"begin":727,"end":732},"obj":"NP"},{"id":"C15","span":{"begin":734,"end":738},"obj":"NP"},{"id":"C16","span":{"begin":777,"end":792},"obj":"NP"},{"id":"C11","span":{"begin":650,"end":792},"obj":"NP"},{"id":"C17","span":{"begin":876,"end":887},"obj":"NP"},{"id":"C18","span":{"begin":912,"end":927},"obj":"NP"},{"id":"C20","span":{"begin":1026,"end":1042},"obj":"NP"},{"id":"C19","span":{"begin":995,"end":1042},"obj":"NP"},{"id":"C22","span":{"begin":1102,"end":1117},"obj":"NP"},{"id":"C21","span":{"begin":1070,"end":1117},"obj":"NP"},{"id":"C24","span":{"begin":1204,"end":1219},"obj":"NP"},{"id":"C23","span":{"begin":1172,"end":1219},"obj":"NP"},{"id":"C25","span":{"begin":1362,"end":1373},"obj":"NP"},{"id":"C26","span":{"begin":1404,"end":1420},"obj":"NP"},{"id":"C28","span":{"begin":1525,"end":1540},"obj":"NP"},{"id":"C27","span":{"begin":1500,"end":1540},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-pron","subj":"C4","obj":"C1"},{"id":"R2","pred":"coref-ident","subj":"C8","obj":"C5"},{"id":"R3","pred":"coref-relat","subj":"C9","obj":"C7"},{"id":"R4","pred":"coref-ident","subj":"C10","obj":"C6"},{"id":"R5","pred":"coref-ident","subj":"C13","obj":"C2"},{"id":"R6","pred":"coref-appos","subj":"C14","obj":"C13"},{"id":"R7","pred":"coref-relat","subj":"C15","obj":"C12"},{"id":"R8","pred":"coref-ident","subj":"C16","obj":"C8"},{"id":"R9","pred":"coref-ident","subj":"C11","obj":"C1"},{"id":"R10","pred":"coref-ident","subj":"C17","obj":"C13"},{"id":"R11","pred":"coref-ident","subj":"C18","obj":"C16"},{"id":"R12","pred":"coref-ident","subj":"C19","obj":"C3"},{"id":"R13","pred":"coref-ident","subj":"C22","obj":"C18"},{"id":"R14","pred":"coref-ident","subj":"C24","obj":"C22"},{"id":"R15","pred":"coref-ident","subj":"C23","obj":"C21"},{"id":"R16","pred":"coref-ident","subj":"C25","obj":"C17"},{"id":"R17","pred":"coref-ident","subj":"C26","obj":"C20"},{"id":"R18","pred":"coref-ident","subj":"C28","obj":"C24"},{"id":"R19","pred":"coref-ident","subj":"C27","obj":"C23"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":160},"obj":"Sentence"},{"id":"S2","span":{"begin":161,"end":279},"obj":"Sentence"},{"id":"S3","span":{"begin":280,"end":419},"obj":"Sentence"},{"id":"S4","span":{"begin":420,"end":615},"obj":"Sentence"},{"id":"S5","span":{"begin":616,"end":793},"obj":"Sentence"},{"id":"S6","span":{"begin":794,"end":888},"obj":"Sentence"},{"id":"S7","span":{"begin":889,"end":1118},"obj":"Sentence"},{"id":"S8","span":{"begin":1119,"end":1374},"obj":"Sentence"},{"id":"S9","span":{"begin":1375,"end":1611},"obj":"Sentence"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":21,"end":62},"obj":"protein_molecule"},{"id":"T2","span":{"begin":68,"end":93},"obj":"cell_line"},{"id":"T3","span":{"begin":119,"end":140},"obj":"protein_domain_or_region"},{"id":"T4","span":{"begin":144,"end":159},"obj":"protein_molecule"},{"id":"T5","span":{"begin":161,"end":183},"obj":"protein_molecule"},{"id":"T6","span":{"begin":185,"end":195},"obj":"protein_molecule"},{"id":"T7","span":{"begin":214,"end":223},"obj":"cell_component"},{"id":"T8","span":{"begin":269,"end":278},"obj":"protein_molecule"},{"id":"T9","span":{"begin":312,"end":333},"obj":"other_name"},{"id":"T10","span":{"begin":337,"end":346},"obj":"protein_molecule"},{"id":"T11","span":{"begin":396,"end":418},"obj":"other_name"},{"id":"T12","span":{"begin":469,"end":487},"obj":"lipid"},{"id":"T13","span":{"begin":489,"end":492},"obj":"lipid"},{"id":"T14","span":{"begin":535,"end":545},"obj":"protein_molecule"},{"id":"T15","span":{"begin":583,"end":592},"obj":"protein_molecule"},{"id":"T16","span":{"begin":652,"end":658},"obj":"protein_family_or_group"},{"id":"T17","span":{"begin":662,"end":675},"obj":"cell_component"},{"id":"T18","span":{"begin":685,"end":688},"obj":"lipid"},{"id":"T19","span":{"begin":727,"end":732},"obj":"cell_line"},{"id":"T20","span":{"begin":777,"end":792},"obj":"protein_molecule"},{"id":"T21","span":{"begin":794,"end":797},"obj":"lipid"},{"id":"T22","span":{"begin":835,"end":844},"obj":"protein_molecule"},{"id":"T23","span":{"begin":850,"end":863},"obj":"protein_family_or_group"},{"id":"T24","span":{"begin":876,"end":887},"obj":"cell_line"},{"id":"T25","span":{"begin":912,"end":921},"obj":"protein_molecule"},{"id":"T26","span":{"begin":932,"end":955},"obj":"other_name"},{"id":"T27","span":{"begin":965,"end":983},"obj":"peptide"},{"id":"T28","span":{"begin":1001,"end":1022},"obj":"protein_domain_or_region"},{"id":"T29","span":{"begin":1036,"end":1042},"obj":"protein_molecule"},{"id":"T30","span":{"begin":1046,"end":1049},"obj":"amino_acid_monomer"},{"id":"T31","span":{"begin":1054,"end":1057},"obj":"amino_acid_monomer"},{"id":"T32","span":{"begin":1074,"end":1098},"obj":"protein_domain_or_region"},{"id":"T33","span":{"begin":1102,"end":1111},"obj":"protein_molecule"},{"id":"T34","span":{"begin":1146,"end":1153},"obj":"peptide"},{"id":"T35","span":{"begin":1176,"end":1200},"obj":"protein_domain_or_region"},{"id":"T36","span":{"begin":1204,"end":1213},"obj":"protein_molecule"},{"id":"T37","span":{"begin":1233,"end":1236},"obj":"lipid"},{"id":"T38","span":{"begin":1245,"end":1255},"obj":"protein_molecule"},{"id":"T39","span":{"begin":1288,"end":1303},"obj":"other_name"},{"id":"T40","span":{"begin":1318,"end":1327},"obj":"protein_molecule"},{"id":"T41","span":{"begin":1339,"end":1355},"obj":"other_name"},{"id":"T42","span":{"begin":1362,"end":1373},"obj":"cell_line"},{"id":"T43","span":{"begin":1408,"end":1420},"obj":"protein_family_or_group"},{"id":"T44","span":{"begin":1461,"end":1464},"obj":"lipid"},{"id":"T45","span":{"begin":1481,"end":1496},"obj":"other_name"},{"id":"T46","span":{"begin":1504,"end":1521},"obj":"protein_domain_or_region"},{"id":"T47","span":{"begin":1525,"end":1534},"obj":"protein_molecule"},{"id":"T48","span":{"begin":1576,"end":1586},"obj":"protein_molecule"},{"id":"T49","span":{"begin":1587,"end":1602},"obj":"protein_molecule"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":68,"end":73},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":700,"end":705},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":214,"end":223},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005737"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":74,"end":83},"obj":"Cell"},{"id":"T3","span":{"begin":706,"end":715},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0001054"}],"text":"Identification of an I kappa B alpha-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on I kappa B alpha.\nNuclear factor kappa B (NF-kappa B) is stored in the cytoplasm as an inactive form through interaction with I kappa B. Stimulation of cells leads to a rapid phosphorylation of I kappa B alpha, which is presumed to be important for the subsequent degradation. We have recently reported the establishment of a lipopolysaccharide (LPS)-dependent cell-free activation system of NF-kappa B in association with the induction of I kappa B alpha phosphorylation. In this study, we have identified a kinase in cell extracts from the LPS-stimulated human monocytic cell line, THP-1, that specifically binds and phosphorylates I kappa B alpha. LPS stimulation transiently enhanced the I kappa B alpha-bound kinase activity in THP-1 cells. Mutational analyses of I kappa B alpha and competition experiments with the synthetic peptides identified major phosphorylation sites by the bound kinase as Ser and Thr residues in the C-terminal acidic domain of I kappa B alpha. Moreover, we show that the peptide, corresponding to the C-terminal acidic domain of I kappa B alpha, blocked the LPS-induced NF-kappa B activation as well as inducible phosphorylation of endogenous I kappa B alpha in a cell-free system using THP-1 cells. These results suggested that the bound kinase is involved in the signaling pathway of LPS by inducing the phosphorylation of the C-terminal region of I kappa B alpha and subsequent dissociation of the NF-kappa B.I kappa B alpha complex."}