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TNF phosphorylates INSR. 20 / 20
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"A TNF-α stimulates lipolysis, increases the burden of free fatty acids (FFAs), and suppresses the production of adiponectin by phosphorylating and deactivating insulin receptor sites in adipose tissue and smooth muscle cells."
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"On the other hand it also has been reported that TNF α phosphorylates insulin receptor and had a central role in insulin resistance [9] ."
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"Although the precise mechanism of obesity-related insulin sensitivity remains unclear, it appears that within adipose tissue, TNFα phosphorylates and deactivates insulin receptor (IR) and insulin receptor substrate 1 (IRS-1) [ xref , xref ]."
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"This is true for TNF-alpha, which acts on the insulin receptor and prevents the dephosphorylation of insulin receptor substrates, thus blocking receptor signaling and preventing glucose entry into the cell (insulin resistance)."
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"Furthermore, TNF-α induced serine phosphorylation of IR and IRS-1, and these effects were completely precluded by pretreatment with inhibitors of p38 MAPK."
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"Thus, troglitazone or pioglitazone reverse the reduction in insulin receptor (IR) or IR substrate-1 phosphorylation caused by TNFα [22] ."
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"TNF-α can stimulate serine phosphorylation of the insulin receptor, which leads to insulin resistance [ xref ]."
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"some of the insulin resistance induced by the p60 TNF Moreover, staurosporin, a non specific inhibitor of pro- receptor; treatment of hepatoma cells and 3T3-L1 adipo- tein kinase C, did not abrogate t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In adipocytes, TNF-α suppresses the transcription of the adiponectin gene [27] and impairs insulin receptor phosphorylation and kinase pathways by activating NF-κB and c-Jun NH2-terminal kinase (JNK) signaling, thereby promoting IR [85]."
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"Infiltrated macrophages also secrete inflammatory cytokines especially tumor necrosis factor alpha (TNF-α) which modulates GLUT-4 and phosphorylates insulin receptor substrate-I to exhibit insulin resistance [9]."
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"In addition, the inhibition of IL-1β and TNFα in REC grown in high glucose decreased phosphorylated IRS-1 and cleaved caspase 3 levels, while increasing phosphorylation of the insulin receptor and Akt."
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"It is important to note that even a short-term systemic neutralization of TNF-α by V1q in ob/ob mice restored the expression of the InsR and phosphorylation of GSK3α at the wound site in vivo to level[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"TNF-α seems to be able to phosphorylate a serine residue on IRS-1 and, subsequently, to inhibit phosphorylation of either the insulin receptor or IRS-1."
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"In the same adipocytes or surrounding skeletal muscle cells, TNF-α may increase serine phosphorylation of the insulin receptor and also of IRS-1 and possibly other proteins that mediate intracellular[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Both TNF-α and IL-6 attenuate insulin signaling in the liver by inducing serine phosphorylation which blocks tyrosine phosphorylation of insulin receptor and insulin receptor substrates (IRS)-1 and 2."
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"Analysis of intestinal tissue in TNF-alpha-treated hamsters indicated impaired phosphorylation of insulin receptor-beta, insulin receptor substrate-1, Akt, and Shc and increased phosphorylation of p38, extracellular signal-related kinase-1/2, and Jun NH(2)-terminal kinase."
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rlimsp
"Pro-inflammatory cytokines, especially IL-6 and TNF-α, have been proposed to induce insulin resistance by the dysregulation of the insulin signaling pathway. These pro-inflammatory cytokines can phosphorylate the insulin receptor substrate-1-associated proteins along with the insulin receptor, resulting in the inhibition of the insulin binding and signaling (23)."
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"TNF-α promotes inhibitory phosphorylation of insulin receptor substrate (IRS) proteins, and enhances ceramide synthesis, adipocyte lipolysis and inhibits PPARγ expression ( xref ; xref )."
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"Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2."
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"Specifically, H. pylori infection raises the levels of TNF-α and IL-6, which disrupt insulin signaling by inhibiting the tyrosine phosphorylation of insulin receptor substrates while promoting their serine phosphorylation[3]."
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