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Activation of PPARgamma negatively regulates O-GlcNAcylation of Sp1.

Abstract：

:O-GlcNAcylation is a kind of post-translational modification and many nuclear and cytoplasmic proteins are O-GlcNAcylated. In this study, we demonstrated that thiazolidinediones (TZDs), which are used as insulin sensitizer, specifically inhibited the O-GlcNAcylation of Sp1 but did not affect the O-GlcNAcylation of the total proteins in cell culture systems and mouse models. This effect was mediated by peroxisome proliferator activated receptor gamma (PPARgamma) activation and probably by synthesis of a specific protein induced by PPARgamma activation. In addition, we demonstrated that the O-GlcNAcylation sites in the zinc-finger domain were involved in the transcriptional activation of Sp1 and that rosiglitazone, a member of TZDs, affected Sp1 transcriptional activity partially by regulating the O-GlcNAcylation level of these sites. Considering the role of hexosamine biosynthesis pathway in hyperglycemia-induced insulin resistance and Sp1 in the hyperglycemia-induced gene expression, the regulation of Sp1 O-GlcNAcylation by TZDs may help to explain the function of TZDs as a treatment for insulin resistance and diabetes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Chung SS,Kim JH,Park HS,Choi HH,Lee KW,Cho YM,Lee HK,Park KS

doi

10.1016/j.bbrc.2008.05.096

subject

Has Abstract

pub_date

2008-08-08 00:00:00

pages

713-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)01023-1

journal_volume

372

pub_type

杂志文章

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