Characteristic increase in nucleocytoplasmic protein glycosylation by O-GlcNAc in 3T3-L1 adipocyte differentiation

Ishihara, Katsunori; Takahashi, Isao; Tsuchiya, Yosuke; Hasegawa, Makoto; Kamemura, Kazuo

doi:10.1016/j.bbrc.2010.06.105

Cited by 36 publications

(40 citation statements)

References 37 publications

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“…However, in other systems it has been demonstrated that an increase in O-GlcNAcylation enhanced insulin signaling (52,53). In line with our data, it has also been shown that preadipocyte differentiation is induced through an increase in O-GlcNAc protein modification (54), whereas adipocyte differentiation can be blocked inhibiting the HBP (55). To our knowledge, no studies have been published regarding the regulation of O-GlcNAc incorporation in hypertrophic or articular chondrocytes.…”

Section: Discussionsupporting

confidence: 80%

The Increase in O-Linked N-Acetylglucosamine Protein Modification Stimulates Chondrogenic Differentiation Both in Vitro and in Vivo

Andrés-Bergós

Tardío

Larrañaga-Vera

et al. 2012

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 80%

The Increase in O-Linked N-Acetylglucosamine Protein Modification Stimulates Chondrogenic Differentiation Both in Vitro and in Vivo

Andrés-Bergós

Tardío

Larrañaga-Vera

et al. 2012

Journal of Biological Chemistry

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“…Furthermore, GFAT-1 siRNA and GFAT-1 inhibitors effectively prevented the formation of lipids in adipocytes. A previous report from Ishihara et al (2010) has demonstrated a global increase in O-GlcNAc-modified proteins during adipocyte differentiation. In addition, the patterns of O-GlcNAcylation between preadipocytes treated with thiamet G (a highly selective and potent inhibitor of O- differentiation (Li et al, 2009).…”

Section: Discussionmentioning

confidence: 96%

“…GlcNAcase) and differentiated adipocytes are clearly different, which indicates that some O-GlcNAcylated proteins have newly appeared in response to the induction of adipocyte differentiation (Ishihara et al, 2010). Ishihara et al also observed the DON-mediated inhibition of O-GlcNAcylation and LD formation.…”

mentioning

confidence: 93%

Suppression of Glutamine:Fructose‐6‐phosphate amidotransferase‐1 inhibits adipogenesis in 3T3‐L1 adipocytes

Hsieh

Lin

Hsieh

et al. 2011

Journal Cellular Physiology

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O-linked N-acetylglucosamine (O-GlcNAc) protein modification has been implicated in the regulation of signaling pathways, cell function, and gene expression. Glutamine:fructose-6-phosphate amidotransferase-1 (GFAT-1) is the rate-limiting enzyme in the hexosamine biosynthetic pathway (HBP), which generates the sugar nucleotide UDP-GlcNAc, where this nucleotide acts as the donor for O-GlcNAc modification. In this study, we determined whether GFAT-1 regulates adipogenesis in adipocytes. 3T3-L1 preadipocytes were differentiated using medium containing high glucose, insulin, dexamethasone, and isobutylmethylxanthine. Cells were harvested 4, 8, and 12 h and 1, 2, 3, 4, 6, and 8 days after the initiation of differentiation. Global level of O-GlcNAc modification increased 4 h after induction and persisted for 8 days of observation. GFAT-1 mRNA and protein expression was also upregulated beginning 4 h after induction. Pharmacological inhibition of GFAT-1 or GFAT-1 siRNA treatment blocked the increase in O-GlcNAcylation and the formation of lipid droplets in adipocytes. GFAT-1 may regulate the expression of C/EBPβ, PPARγ, SREBP-1, fatty acid synthase, S3-12, perilipin, or adipophilin during adipogenesis. Our results suggest that GFAT-1 plays a critical role in modulating adipogenesis via the regulation of protein O-GlcNAcylation in adipocytes.

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“…The activity of Runx2, a critical transcription factor for osteogenesis, was shown to be regulated by O-GlcNAc modification using the reporter assay system (Nagel and Ball, 2014;Nagel et al, 2013). In addition to osteogenesis, mouse 3T3-L1 preadipocytes also exhibit a drastic increase in global OGlcNAc levels during adipogenesis (Ishihara et al, 2010). O-GlcNAc modified proteins that increased in abundance during adipogenesis include vimentin, Nup62, and ewing sarcoma protein (EWS).…”

Section: O-glcnacylation Enzymes In the Nucleus Cytosol And Mitochomentioning

confidence: 98%

Intracellular and extracellular O-linked N-acetylglucosamine in the nervous system

Ogawa

Sawaguchi

Kamemura

et al. 2015

Experimental Neurology

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Characteristic increase in nucleocytoplasmic protein glycosylation by O-GlcNAc in 3T3-L1 adipocyte differentiation

Cited by 36 publications

References 37 publications

The Increase in O-Linked N-Acetylglucosamine Protein Modification Stimulates Chondrogenic Differentiation Both in Vitro and in Vivo

The Increase in O-Linked N-Acetylglucosamine Protein Modification Stimulates Chondrogenic Differentiation Both in Vitro and in Vivo

Suppression of Glutamine:Fructose‐6‐phosphate amidotransferase‐1 inhibits adipogenesis in 3T3‐L1 adipocytes

Intracellular and extracellular O-linked N-acetylglucosamine in the nervous system

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