Article Publish Status: FREE
Abstract Title:

High glucose induces mitochondrial dysfunction independently of protein O-GlcNAcylation.

Abstract Source:

Biochem J. 2015 Apr 1 ;467(1):115-26. PMID: 25627821

Abstract Author(s):

Sujith Dassanayaka, Ryan D Readnower, Joshua K Salabei, Bethany W Long, Allison L Aird, Yu-Ting Zheng, Senthilkumar Muthusamy, Heberty T Facundo, Bradford G Hill, Steven P Jones

Article Affiliation:

Sujith Dassanayaka


Diabetes is characterized by hyperglycaemia and perturbations in intermediary metabolism. In particular, diabetes can augment flux through accessory pathways of glucose metabolism, such as the hexosamine biosynthetic pathway (HBP), which produces the sugar donor for theβ-O-linked-N-acetylglucosamine (O-GlcNAc) post-translational modification of proteins. Diabetes also promotes mitochondrial dysfunction. Nevertheless, the relationships among diabetes, hyperglycaemia, mitochondrial dysfunction and O-GlcNAc modifications remain unclear. In the present study, we tested whether high-glucose-induced increases in O-GlcNAc modifications directly regulate mitochondrial function in isolated cardiomyocytes. Augmentation of O-GlcNAcylation with high glucose (33 mM) was associated with diminished basal and maximal cardiomyocyte respiration, a decreased mitochondrial reserve capacity and lower Complex II-dependent respiration (P<0.05); however, pharmacological or genetic modulation of O-GlcNAc modifications under normal or high glucose conditions showed few significant effects on mitochondrial respiration, suggesting that O-GlcNAc does not play a major role in regulating cardiomyocyte mitochondrial function. Furthermore, an osmotic control recapitulated high-glucose-induced changes to mitochondrial metabolism (P<0.05) without increasing O-GlcNAcylation. Thus, increased O-GlcNAcylation is neither sufficient nor necessary for high-glucose-induced suppression of mitochondrial metabolism in isolated cardiomyocytes.

Study Type : Human In Vitro

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