pubmed-article:11399523 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0021753 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0022131 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C1120843 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0017725 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C2261486 | lld:lifeskim |
pubmed-article:11399523 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:11399523 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:11399523 | pubmed:dateCreated | 2001-6-11 | lld:pubmed |
pubmed-article:11399523 | pubmed:abstractText | The cytokine interleukin-1 beta (IL-1 beta) is cytotoxic to rat pancreatic beta-cells and has been implicated in the pathogenesis of insulin-dependent diabetes mellitus. IL-1 beta causes expression of inducible nitric oxide synthase (iNOS) and production of nitric oxide (NO). NO may be the mediator of the cytotoxic effect of IL-1 beta in rat islets and beta-cell lines. Glucose has been shown to modulate the effects of IL-1 beta on accumulated insulin release and potentiate NO production in rat islets, but the biochemical mechanism is unknown. IL-1 beta activates the mitogen-activated protein kinases (MAPK) extracellular signal-regulated kinase 1 and 2 (ERK1/2), p38 and c-jun NH2-terminal kinase (JNK) in rat islets and beta-cells. Glucose may modulate MAPK activity although contrasting data have been published. The aim of this study was to investigate whether glucose potentiated IL-1 beta-induced p38 and ERK1/2 activity in rat islets. It was shown that glucose alone increased the phosphorylation of the MAPK substrates Elk-1 and activating transcription factor 2 (ATF2). D-glucose potentiated the p38 activity induced by a low concentration of IL-1 beta, whereas no effect was seen at high concentrations of IL-1 beta. Inhibition of p38 activity prevented IL-1 beta-induced nitrite production in the presence of D-glucose. We conclude that IL-1 beta-induced NO production in the presence of glucose is signalled by the p38 pathway. | lld:pubmed |
pubmed-article:11399523 | pubmed:language | eng | lld:pubmed |
pubmed-article:11399523 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11399523 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11399523 | pubmed:issn | 1148-5493 | lld:pubmed |
pubmed-article:11399523 | pubmed:author | pubmed-author:AndersenN ANA | lld:pubmed |
pubmed-article:11399523 | pubmed:author | pubmed-author:Mandrup-Pouls... | lld:pubmed |
pubmed-article:11399523 | pubmed:author | pubmed-author:SprinkelA MAM | lld:pubmed |
pubmed-article:11399523 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11399523 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:11399523 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11399523 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11399523 | pubmed:pagination | 331-9 | lld:pubmed |
pubmed-article:11399523 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:meshHeading | pubmed-meshheading:11399523... | lld:pubmed |
pubmed-article:11399523 | pubmed:articleTitle | Glucose potentiates interleukin-1 beta (IL-1 beta)-induced p38 mitogen-activated protein kinase activity in rat pancreatic islets of Langerhans. | lld:pubmed |
pubmed-article:11399523 | pubmed:affiliation | Steno Diabetes Center, 2 Niels Steensens vej, DK-2820 Gentofte, Denmark. | lld:pubmed |
pubmed-article:11399523 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11399523 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11399523 | lld:pubmed |