# Interleukin-1α inhibits insulin signaling with phosphorylating insulin receptor substrate-1 on serine residues in 3T3-L1 adipocytes
> He J.

URL kanonis: https://discover.unhas.ac.id/publications/interleukin-1-inhibits-insulin-signaling-with-phosphorylating-insulin-receptor-s
Jurnal / Konferensi: Molecular Endocrinology
Tahun terbit: 2006
DOI: https://doi.org/10.1210/me.2005-0107
ISSN: 08888809
Citations: 94

## Authors
- He J.

## Abstract
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.

## Keywords
- Insulin receptor
- Insulin receptor substrate
- Phosphorylation
- Tyrosine phosphorylation
- IRS1
- IRS2
- Biology
- Insulin resistance
- Protein kinase B
- Kinase
- Proinflammatory cytokine
- Insulin
- Internal medicine
- Endocrinology
- Cell biology
- Medicine
- Immunology
- Inflammation

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Sumber: Discover Unhas — RIMS Universitas Hasanuddin.
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