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Proteomics and PUGNAcity will overcome questioning of insulin resistance induction by nonselective inhibition of O-GlcNAcase

Abstract : PTMs are the ultimate elements that perfect the existence and the activity of proteins. Owing to PTM, not less than 500 millions biological activities arise from approximately 20 000 protein-coding genes in human. Hundreds of PTM were characterized in living beings among which is a large variety of glycosylations. Many compounds have been developed to tentatively block each kind of glycosylation so as to study their biological functions but due to their complexity, many off-target effects were reported. Insulin resistance exemplifies this problem. Several independent groups described that inhibiting the removal of O-GlcNAc moieties using O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), a nonselective inhibitor of the nuclear and cytoplasmic O-GlcNAcase, induced insulin resistance both in vivo and ex vivo. The development of potent and highly selective O-GlcNAcase inhibitors called into question that elevated O-GlcNAcylation levels are responsible for insulin resistance; these compounds not recapitulating the insulin-desensitizing effect of PUGNAc. To tackle this intriguing problem, a South Korean group recently combined ATP-affinity chromatography and gel-assisted digestion to identify proteins, differentially expressed upon treatment of 3T3-L1 adipocytes with PUGNAc, involved in protein turnover and insulin signaling.
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https://hal.univ-lille.fr/hal-03173342
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Soumis le : jeudi 18 mars 2021 - 13:56:54
Dernière modification le : mardi 19 octobre 2021 - 11:33:30

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Vanessa Dehennaut, Tony Lefebvre. Proteomics and PUGNAcity will overcome questioning of insulin resistance induction by nonselective inhibition of O-GlcNAcase. Proteomics, 2013, Proteomics, 13 (20), pp.2944-2946. ⟨10.1002/pmic.201300363⟩. ⟨hal-03173342⟩

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