FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2029700855> ?p ?o ?g. }

• W2029700855 endingPage "4164" @default.
• W2029700855 startingPage "4158" @default.
• W2029700855 abstract "Nuclear factor κB (NF-κB), consisting of p50 and p65, is bound to a cytoplasmic retention protein, IκB, in a resting state, and the stimulation of cells with a variety of inflammatory stimuli induces the dissociation of NF-κB from IκB and the nuclear translocation of NF-κB, thereby activating several genes involved in inflammatory responses, such as interleukin (IL)-6, IL-8, and tumor necrosis factor α. In order to elucidate the precise mechanism of NF-κB activation, we have established lipopolysaccharide (LPS)-dependent NF-κB activation in a cell-free system using plasma membrane-enriched, cytosol, and nuclear fractions extracted from a human monocytic cell line, THP-1, by disruption with sonication followed by a differential centrifugation. The combination of plasma membrane-enriched fraction and cytosol was sufficient to activate NF-κB in a LPS/CD14-dependent manner only in the presence of ATP as judged by the binding of NF-κB to the IL-8 gene κB site on an electrophoretic mobility shift assay. LPS-dependent NF-κB activation was inhibited by protein kinase inhibitors, such as staurosporine, herbimycin A, tyrphostin, and genistein, but not mitogen-activated protein kinase substrate, cGMP-dependent protein kinase, cAMP-dependent protein kinase, protein kinase C, and calmodulin-dependent protein kinase II inhibitory peptides, suggesting that staurosporine-sensitive kinase(s) as well as tyrosine kinase(s) are involved in LPS-mediated NF-κB activation. In addition, LPS induced the phosphorylation of IκB-α, starting at 5 min after the stimulation in a cell-free system. Moreover, the phosphorylation was inhibited by herbimycin A and tyrphostin, but not staurosporine, suggesting that these protein kinase inhibitors act at distinct steps of signal transmission. Establishment of ligand-dependent activation of NF-κB in a cell-free system will facilitate identification of protein kinase(s) and its substrate(s) involved in LPS-mediated NF-κB activation. Nuclear factor κB (NF-κB), consisting of p50 and p65, is bound to a cytoplasmic retention protein, IκB, in a resting state, and the stimulation of cells with a variety of inflammatory stimuli induces the dissociation of NF-κB from IκB and the nuclear translocation of NF-κB, thereby activating several genes involved in inflammatory responses, such as interleukin (IL)-6, IL-8, and tumor necrosis factor α. In order to elucidate the precise mechanism of NF-κB activation, we have established lipopolysaccharide (LPS)-dependent NF-κB activation in a cell-free system using plasma membrane-enriched, cytosol, and nuclear fractions extracted from a human monocytic cell line, THP-1, by disruption with sonication followed by a differential centrifugation. The combination of plasma membrane-enriched fraction and cytosol was sufficient to activate NF-κB in a LPS/CD14-dependent manner only in the presence of ATP as judged by the binding of NF-κB to the IL-8 gene κB site on an electrophoretic mobility shift assay. LPS-dependent NF-κB activation was inhibited by protein kinase inhibitors, such as staurosporine, herbimycin A, tyrphostin, and genistein, but not mitogen-activated protein kinase substrate, cGMP-dependent protein kinase, cAMP-dependent protein kinase, protein kinase C, and calmodulin-dependent protein kinase II inhibitory peptides, suggesting that staurosporine-sensitive kinase(s) as well as tyrosine kinase(s) are involved in LPS-mediated NF-κB activation. In addition, LPS induced the phosphorylation of IκB-α, starting at 5 min after the stimulation in a cell-free system. Moreover, the phosphorylation was inhibited by herbimycin A and tyrphostin, but not staurosporine, suggesting that these protein kinase inhibitors act at distinct steps of signal transmission. Establishment of ligand-dependent activation of NF-κB in a cell-free system will facilitate identification of protein kinase(s) and its substrate(s) involved in LPS-mediated NF-κB activation." @default.
• W2029700855 created "2016-06-24" @default.
• W2029700855 creator A5005730268 @default.
• W2029700855 creator A5045762902 @default.
• W2029700855 creator A5052997534 @default.
• W2029700855 creator A5069419180 @default.
• W2029700855 creator A5076593822 @default.
• W2029700855 creator A5091494265 @default.
• W2029700855 date "1995-02-01" @default.
• W2029700855 modified "2023-09-30" @default.
• W2029700855 title "Establishment of Lipopolysaccharide-dependent Nuclear Factor κB Activation in a Cell-free System" @default.
• W2029700855 cites W1497553226 @default.
• W2029700855 cites W1510155660 @default.
• W2029700855 cites W1518046617 @default.
• W2029700855 cites W1519301821 @default.
• W2029700855 cites W1544122331 @default.
• W2029700855 cites W1561376991 @default.
• W2029700855 cites W1573683888 @default.
• W2029700855 cites W1592606160 @default.
• W2029700855 cites W1595516692 @default.
• W2029700855 cites W1605123818 @default.
• W2029700855 cites W1622015823 @default.
• W2029700855 cites W1636221253 @default.
• W2029700855 cites W1667463872 @default.
• W2029700855 cites W1671728707 @default.
• W2029700855 cites W1911781926 @default.
• W2029700855 cites W1968235120 @default.
• W2029700855 cites W1993243592 @default.
• W2029700855 cites W2015469705 @default.
• W2029700855 cites W2027152576 @default.
• W2029700855 cites W2031850022 @default.
• W2029700855 cites W2039088937 @default.
• W2029700855 cites W2053111401 @default.
• W2029700855 cites W2057093252 @default.
• W2029700855 cites W2061903251 @default.
• W2029700855 cites W2079773459 @default.
• W2029700855 cites W2088094960 @default.
• W2029700855 cites W2089478514 @default.
• W2029700855 cites W2105415988 @default.
• W2029700855 cites W2118991962 @default.
• W2029700855 cites W2123884323 @default.
• W2029700855 cites W2128584338 @default.
• W2029700855 cites W2146746046 @default.
• W2029700855 cites W2164701257 @default.
• W2029700855 cites W2176220887 @default.
• W2029700855 doi "https://doi.org/10.1074/jbc.270.8.4158" @default.
• W2029700855 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7876168" @default.
• W2029700855 hasPublicationYear "1995" @default.
• W2029700855 type Work @default.
• W2029700855 sameAs 2029700855 @default.
• W2029700855 citedByCount "80" @default.
• W2029700855 countsByYear W20297008552012 @default.
• W2029700855 countsByYear W20297008552013 @default.
• W2029700855 countsByYear W20297008552014 @default.
• W2029700855 countsByYear W20297008552017 @default.
• W2029700855 countsByYear W20297008552021 @default.
• W2029700855 crossrefType "journal-article" @default.
• W2029700855 hasAuthorship W2029700855A5005730268 @default.
• W2029700855 hasAuthorship W2029700855A5045762902 @default.
• W2029700855 hasAuthorship W2029700855A5052997534 @default.
• W2029700855 hasAuthorship W2029700855A5069419180 @default.
• W2029700855 hasAuthorship W2029700855A5076593822 @default.
• W2029700855 hasAuthorship W2029700855A5091494265 @default.
• W2029700855 hasBestOaLocation W20297008551 @default.
• W2029700855 hasConcept C137361374 @default.
• W2029700855 hasConcept C153911025 @default.
• W2029700855 hasConcept C184235292 @default.
• W2029700855 hasConcept C185592680 @default.
• W2029700855 hasConcept C2779033064 @default.
• W2029700855 hasConcept C2779084600 @default.
• W2029700855 hasConcept C55493867 @default.
• W2029700855 hasConcept C86803240 @default.
• W2029700855 hasConcept C90934575 @default.
• W2029700855 hasConcept C95444343 @default.
• W2029700855 hasConcept C97029542 @default.
• W2029700855 hasConceptScore W2029700855C137361374 @default.
• W2029700855 hasConceptScore W2029700855C153911025 @default.
• W2029700855 hasConceptScore W2029700855C184235292 @default.
• W2029700855 hasConceptScore W2029700855C185592680 @default.
• W2029700855 hasConceptScore W2029700855C2779033064 @default.
• W2029700855 hasConceptScore W2029700855C2779084600 @default.
• W2029700855 hasConceptScore W2029700855C55493867 @default.
• W2029700855 hasConceptScore W2029700855C86803240 @default.
• W2029700855 hasConceptScore W2029700855C90934575 @default.
• W2029700855 hasConceptScore W2029700855C95444343 @default.
• W2029700855 hasConceptScore W2029700855C97029542 @default.
• W2029700855 hasIssue "8" @default.
• W2029700855 hasLocation W20297008551 @default.
• W2029700855 hasOpenAccess W2029700855 @default.
• W2029700855 hasPrimaryLocation W20297008551 @default.
• W2029700855 hasRelatedWork W1589866689 @default.
• W2029700855 hasRelatedWork W1987938799 @default.
• W2029700855 hasRelatedWork W2034683990 @default.
• W2029700855 hasRelatedWork W2059352797 @default.
• W2029700855 hasRelatedWork W2059557436 @default.
• W2029700855 hasRelatedWork W2073743870 @default.
• W2029700855 hasRelatedWork W2079012692 @default.
• W2029700855 hasRelatedWork W2086175308 @default.

• next