Linked Life Data

16150868

Source:http://linkedlifedata.com/resource/pubmed/id/16150868

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-12-28
pubmed:abstractText
Proinflammatory cytokines are recently reported to inhibit insulin signaling causing insulin resistance. IL-1alpha is also one of the proinflammatory cytokines; however, it has not been clarified whether IL-1alpha may also cause insulin resistance. Here, we investigated the effects of IL-1alpha treatment on insulin signaling in 3T3-L1 adipocytes. IL-1alpha treatment up to 4 h did not alter insulin-stimulated insulin receptor tyrosine phosphorylation, whereas tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and the association with phosphatidylinositol 3-kinase were partially inhibited with the maximal inhibition in around 15 min. IRS-1 was transiently phosphorylated on some serine residues around 15 min after IL-1alpha stimulation, when several serine kinases, IkappaB kinase, c-Jun-N-terminal kinase, ERK, and p70S6K were activated. Chemical inhibitors for these kinases inhibited IL-1alpha-induced serine phosphorylation of IRS-1. Tyrosine phosphorylation of IRS-1 was recovered only by the IKK inhibitor or JNK inhibitor, suggesting specific involvement of these two kinases. Insulin-stimulated Akt phosphorylation and 2-deoxyglucose uptake were not inhibited only by IL-1alpha. Interestingly, Akt phosphorylation was synergistically inhibited by IL-1alpha in the presence of IL-6. Taken together, short-term IL-1alpha treatment transiently causes insulin resistance at IRS-1 level with its serine phosphorylation. IL-1alpha may suppress insulin signaling downstream of IRS-1 in the presence of other cytokines, such as IL-6.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
114-24
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:16150868-3T3-L1 Cells, pubmed-meshheading:16150868-Adipocytes, pubmed-meshheading:16150868-Animals, pubmed-meshheading:16150868-Enzyme Activation, pubmed-meshheading:16150868-Insulin, pubmed-meshheading:16150868-Insulin Receptor Substrate Proteins, pubmed-meshheading:16150868-Insulin Resistance, pubmed-meshheading:16150868-Interleukin-1, pubmed-meshheading:16150868-Interleukin-6, pubmed-meshheading:16150868-Mice, pubmed-meshheading:16150868-Oncogene Protein v-akt, pubmed-meshheading:16150868-Phosphatidylinositol 3-Kinases, pubmed-meshheading:16150868-Phosphoproteins, pubmed-meshheading:16150868-Phosphorylation, pubmed-meshheading:16150868-Protein-Serine-Threonine Kinases, pubmed-meshheading:16150868-Serine, pubmed-meshheading:16150868-Signal Transduction, pubmed-meshheading:16150868-Tyrosine
pubmed:year
2006
pubmed:articleTitle
Interleukin-1alpha inhibits insulin signaling with phosphorylating insulin receptor substrate-1 on serine residues in 3T3-L1 adipocytes.
pubmed:affiliation
The First Department of Internal Medicine, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't