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Tumor necrosis factor (TNF) interferes with insulin signaling through the p55 TNF receptor death domain.

Abstract：

:Tumor necrosis factor (TNF) contributes to insulin resistance by binding to the 55kDa TNF receptor (TNF-R55), resulting in serine phosphorylation of proteins such as insulin receptor (IR) substrate (IRS)-1, followed by reduced tyrosine phosphorylation of IRS-1 through the IR and, thereby, diminished IR signal transduction. Through independent receptor domains, TNF-R55 activates a neutral (N-SMase) and an acid sphingomyelinase (A-SMase), that both generate the sphingolipid ceramide. Multiple candidate kinases have been identified that serine-phosphorylate IRS-1 in response to TNF or ceramide. However, due to the fact that the receptor domain of TNF-R55 mediating inhibition of the IR has not been mapped, it is currently unknown whether TNF exerts these effects with participation of N-SMase or A-SMase. Here, we identify the death domain of TNF-R55 as responsible for the inhibitory effects of TNF on tyrosine phosphorylation of IRS-1, implicating ceramide generated by A-SMase as a downstream mediator of inhibition of IR signaling.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Csehi SB,Mathieu S,Seifert U,Lange A,Zweyer M,Wernig A,Adam D

doi

10.1016/j.bbrc.2005.01.140

subject

Has Abstract

pub_date

2005-04-01 00:00:00

pages

397-405

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)00205-6

journal_volume

329

pub_type

杂志文章

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