Characteristic increase in nucleocytoplasmic protein glycosylation by O-GlcNAc in 3T3-L1 adipocyte differentiation.
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| Abstract |
O-Linked beta-N-acetylglucosaminylation (O-GlcNAcylation) of nucleocytoplasmic proteins is a ubiquitous post-translational modification in multicellular organisms studied so far. Since aberrant O-GlcNAcylation has a link with insulin resistance, it is important to establish the status of O-GlcNAcylation in differentiation of mesenchymal cells such as preadipocytes. In this study, we found a differentiation-dependent drastic increase in the level of O-GlcNAcylation in mouse 3T3-L1 preadipocytes. The occurrence of the increase in O-GlcNAcylation, which correlated with the expression of C/EBPalpha, was in part due to increased expression of O-GlcNAc transferase. In addition to the well-known O-GlcNAcylated proteins such as nucleoporins and vimentin, pyruvate carboxylase, long chain fatty acid-CoA ligase 1, and Ewing sarcoma protein were identified as the proteins which are heavily O-GlcNAcylated with the adipocyte differentiation. Both adipocyte differentiation and the differentiation-dependent increase in O-GlcNAcylation were blocked by 6-diazo-5-oxo-norleucine. These results suggest that O-GlcNAcylation particilates, at least in part, in adipogenesis.
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| Authors | Katsunori Ishihara, Isao Takahashi, Yuichi Tsuchiya, Makoto Hasegawa, Kazuo Kamemura |
| Journal | Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 398 Issue 3 Pg. 489-94 (Jul 30 2010) ISSN: 1090-2104 [Electronic] United States |
| PMID | 20599697 (Publication Type: Journal Article) |
| Copyright | Copyright 2010 Elsevier Inc. All rights reserved. |
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