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Possible Interaction: Acetylglucosamine and Insulin

drug:

Insulin

Research Papers that Mention the Interaction

These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
Molecular & cellular proteomics : MCP  •  2009  |  View Paper
O-GlcNAc regulates cellular responses to hormones such as insulin , initiates a protective response to stress, modulates a cell's capacity to grow and divide, and regulates gene transcription.
Journal of cellular biochemistry  •  2006  |  View Paper
Related to insulin action, work by others has suggested that O-GlcNAc elevation may inhibit the anti-apoptotic action of insulin.
Glycobiology  •  2016  |  View Paper
Insulin stimulates both the biosynthesis of transcription factor Sp1 and its O-linked N-acetylglucosaminylation (O-GlcNAcylation), which promotes nuclear localization of Sp1 and its ability to transactivate calmodulin (CaM) gene transcription.
Diabetes  •  2004  |  View Paper
Insulin increased the amount of cytosolic N - and O-linked GlcNAc by 56% from 362 +/- 30 to 564 +/- 45 dpm/microg protein .
Metabolism: clinical and experimental  •  1998  |  View Paper
Glucose, alpha-ketoisocaproate, and N-acetylglucosamine all initiate insulin release and stimulate cyclic AMP efflux and cyclic AMP accumulation.
Bioscience reports  •  1982  |  View Paper
Lectins that interact with galactose (Ricinus communis I, RCAI), mannose, Lens culinaris agglutinin (LCA), Concanavalin A (Con A) or N-acetylglucosamine (wheat-germ agglutinin, WGA) decreased insulin binding by 43, 57, 59 and 85% respectively.
Molecular and Cellular Endocrinology  •  1981  |  View Paper