O-GlcNAc modification is associated with insulin sensitivity in the whole blood of healthy young adult males

Myslicki, Jason P.; Shearer, Jane; Hittel, Dustin S.; Hughey, Curtis C.; Belke, Darrell D.

doi:10.1186/1758-5996-6-96

Cited by 20 publications

(6 citation statements)

References 20 publications

(28 reference statements)

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“…Both N-glycans and O-glycans play an important role in the functions of the glycoprotein involved in various cell recognition signals and pathological situations [13,[18][19][20][21][22][23], so they are potentially potent and reliable biomarkers of various diseases. Because of the large number of biological processes in which glycans participate, it is not surprising that defects in the synthesis of glycans can be the direct cause of numerous diseases and, therefore, markers of the disease [5].…”

Section: E Gclinical Importance Of Glycoproteinsmentioning

confidence: 99%

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Fuertes-Martín

Correig

Vallvé

et al. 2020

JCM

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Several studies suggest that variations in the concentration of plasma glycoproteins can influence cellular changes in a large number of diseases. In recent years, proton nuclear magnetic resonance (1H-NMR) has played a major role as an analytical tool for serum and plasma samples. In recent years, there is an increasing interest in the characterization of glycoproteins through 1H-NMR in order to search for reliable and robust biomarkers of disease. The objective of this review was to examine the existing studies in the literature related to the study of glycoproteins from an analytical and clinical point of view. There are currently several techniques to characterize circulating glycoproteins in serum or plasma, but in this review, we focus on 1H-NMR due to its great robustness and recent interest in its translation to the clinical setting. In fact, there is already a marker in H-NMR representing the acetyl groups of the glycoproteins, GlycA, which has been increasingly studied in clinical studies. A broad search of the literature was performed showing a general consensus that GlycA is a robust marker of systemic inflammation. The results also suggested that GlycA better captures systemic inflammation even more than C-reactive protein (CRP), a widely used classical inflammatory marker. The applications reviewed here demonstrated that GlycA was potentially a key biomarker in a wide range of diseases such as cancer, metabolic diseases, cardiovascular risk, and chronic inflammatory diseases among others. The profiling of glycoproteins through 1H-NMR launches an encouraging new paradigm for its future incorporation in clinical diagnosis.

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Section: E Gclinical Importance Of Glycoproteinsmentioning

confidence: 99%

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Fuertes-Martín

Correig

Vallvé

et al. 2020

JCM

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“…A study by Myslicki et al used human whole blood samples to measure O-GlcNAc ( 34 ). They found no correlation between whole blood O-GlcNAc and aerobic capacity (VO 2peak ) in healthy males, however, their samples were collected only from resting individuals.…”

Section: Discussionmentioning

confidence: 99%

Protein O-GlcNAc Modification Increases in White Blood Cells After a Single Bout of Physical Exercise

et al. 2018

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BackgroundProtein O-linked N-acetylglucosamine (O-GlcNAc) is a dynamic posttranslational modification influencing the function of many intracellular proteins. Recently it was revealed that O-GlcNAc regulation is modified under various stress states, including ischemia and oxidative stress. Aside from a few contradictory studies based on animal models, the effect of exercise on O-GlcNAc is unexplored.PurposeTo evaluate O-GlcNAc levels in white blood cells (WBC) of human volunteers following physical exercise.MethodsYoung (age 30 ± 5.2), healthy male volunteers (n = 6) were enlisted for the study. Blood parameters including metabolites, ions, “necro”-enzymes, and cell counts were measured before and after a single bout of exercise (2-mile run). From WBC samples, we performed western blots to detect O-GlcNAc modified proteins. The distribution of O-GlcNAc in WBC subpopulations was assessed by flow cytometry.ResultsElevation of serum lactic acid (increased from 1.3 ± 0.4 to 6.9 ± 1.7 mM), creatinine (from 77.5 ± 6.3 U/L to 102.2 ± 7.0 μM), and lactate dehydrogenase (from 318.5 ± 26.2 to 380.5 ± 33.2 U/L) confirmed the effect of exercise. WBC count also significantly increased (from 6.6 ± 1.0 to 8.4 ± 1.4 G/L). The level of O-GlcNAc modified proteins in WBCs showed significant elevation after exercise (85 ± 51%, p < 0.05). Flow cytometry revealed that most of this change could be attributed to lymphocytes and monocytes.ConclusionOur results indicate that short-term exercise impacts the O-GlcNAc status of WBCs. O-GlcNAc modification could be a natural process by which physical activity modulates the immune system. Further research could elucidate the role of O-GlcNAc during exercise and validate O-GlcNAc as a biomarker for fitness assessment.

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“…Measurement of O-GlcNAc levels in human patients could report about important information. A few studies already attempted to use O-GlcNAc analysis to predict the extent of metabolic dysfunction and the complications of diabetes [ 157 , 158 ]. On the other hand, intervening in O-GlcNAc regulation by specific OGT and OGA inhibitors could significantly improve the outcome of some diseases.…”

Section: Discussionmentioning

confidence: 99%

The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport

Fisi

Miseta

Nagy

2017

Oxidative Medicine and Cellular Longevity

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O-linked N-acetylglucosamine (O-GlcNAc) is a posttranslational modification that is increasingly recognized as a signal transduction mechanism. Unlike other glycans, O-GlcNAc is a highly dynamic and reversible process that involves the addition and removal of a single N-acetylglucosamine molecule to Ser/Thr residues of proteins. UDP-GlcNAc—the direct substrate for O-GlcNAc modification—is controlled by the rate of cellular metabolism, and thus O-GlcNAc is dependent on substrate availability. Serving as a feedback mechanism, O-GlcNAc influences the regulation of insulin signaling and glucose transport. Besides nutrient sensing, O-GlcNAc was also implicated in the regulation of various physiological and pathophysiological processes. Due to improvements of mass spectrometry techniques, more than one thousand proteins were detected to carry the O-GlcNAc moiety; many of them are known to participate in the regulation of metabolites, ions, or protein transport across biological membranes. Recent studies also indicated that O-GlcNAc is involved in stress adaptation; overwhelming evidences suggest that O-GlcNAc levels increase upon stress. O-GlcNAc elevation is generally considered to be beneficial during stress, although the exact nature of its protective effect is not understood. In this review, we summarize the current data regarding the oxidative stress-related changes of O-GlcNAc levels and discuss the implications related to membrane trafficking.

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O-GlcNAc modification is associated with insulin sensitivity in the whole blood of healthy young adult males

Cited by 20 publications

References 20 publications

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Protein O-GlcNAc Modification Increases in White Blood Cells After a Single Bout of Physical Exercise

The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport

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