Truong, Nhat Quang

Vickers, Abigail

English

Liberty University Digital Commons

 Abstract Title – O-GlcNAcylation and Activity of Succinate Dehydrogenase Program of Study – Biochemistry and Molecular Biology Presentation Type – Physical Poster Subtype – Basic Mentor(s) and Mentor Email – Dr. Pei Zhang (pzhang@liberty.edu) Student name(s) and email(s) – Abigail Vickers (ahvickers@liberty.edu) and Nhat Truong (ntruong1@liberty.edu)   This presentation will look at how O-GlcNAcylation affects the activity of succinate dehydrogenase and how it may be involved in metabolic diseases such as diabetes and obesity. O-linked N-acetylglucosamine Transferase (OGT) is an enzyme that glycosylates proteins on serine and threonine residues. O-GlcNAcylation has been shown to play a prominent regulatory role in a variety of cellular processes, and aberrant O-GlcNAc signaling has been implicated in human diseases such as obesity and Type II diabetes (1). High glucose levels have been shown to increase O-GlcNAcylation, which has been connected to diabetes (2). One way in which excess O-GlcNAcylation may be involved in diabetes is by causing decreased metabolic function. O-GlcNAcylation has been shown to occur on complexes I, III, and IV of the electron transport chain in the mitochondria, and as glucose levels and O-GlcNAcylation increased, mitochondrial function was impaired (3). This presentation will explore whether this type of modification has effects on a principal mitochondrial enzyme, succinate dehydrogenase (SDH), which is involved both in catalyzing the conversion of succinate to fumarate in the TCA cycle and is a part of complex II in the electron transport chain. Key O-GlcNAcylation sites on SDH were mutated, then transfected into Hela cells. An enzymatic assay was performed to examine the effects of O-GlcNAcylation on SDH activity by using the reduction of DCPIP. The SDH with a double mutation appeared to have decreased activity, suggesting that some O-GlcNAcylation is required for the function of SDH.  References 1. X. Yang, K. Qian, Protein O-GlcNAcylation: emerging mechanisms and functions. Nature reviews. Molecular cell biology 18, 452-465 (2017). 2. J. Ma, G. W. Hart, Protein O-GlcNAcylation in diabetes and diabetic complications. Expert review of proteomics 10, 365-380 (2013). 3. Y. Hu, J. Suarez, E. Fricovsky, H. Wang, B. T. Scott, S. A. Trauger, W. Han, Y. Hu, M. O. Oyeleye, W. H. Dillmann, Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. Journal of biological chemistry 284, 547–555 (2009).   

O-GlcNAcylation and Activity of Succinate Dehydrogenase

https://digitalcommons.liberty.edu/cgi/viewcontent.cgi?article=1233&amp;context=research_symp

O-GlcNAcylation and Activity of Succinate Dehydrogenase

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