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Paul J Thornalley - One of the best experts on this subject based on the ideXlab platform.
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Glycation research in amino acids: a place to call home
Amino Acids, 2012Co-Authors: Naila Rabbani, Paul J ThornalleyAbstract:This is an introduction to a collection of review articles by leading investigators in the field of protein Glycation research, see following articles in this issue. With this we launch a section of this journal now established for presentation of research results, reviews and commentaries on protein Glycation and related topics. Glycation is the spontaneous, non-enzymatic reaction of protein with saccharides and saccharide derivatives. Although studied in the modern scientific era for over 100 years, its importance in the biology, medicine, food and nutrition, pharmacology and toxicology, and technological processing remains intriguingly undisclosed. In this section of amino acids, research on Glycation is a qualifier for publication. Glycation research now has a place to call home.
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Amino Acids Glycation Section.
Amino acids, 2011Co-Authors: Naila Rabbani, Paul J ThornalleyAbstract:It is a great pleasure and honour to present the following reviews on Glycation research to kick-off the new Glycation Section of Amino Acids. We start with an introduction to Glycation, describing in brief the history of Glycation research and its current standing in research across the scientific disciplines (Rabbani and Thornalley 2010a). There are then reviews on current issues of Glycation in food science: ‘Physiological relevance of dietary melanoidins’ by Morales et al. (2010), ‘Glycation products in infant formulas—chemical, analytical, and physiological aspects’ by Pischetsrieder and Henle (2010) and ‘Health effects of dietary Maillard reaction products—The results of ICARE and other studies’ by Tessier and BirlouezAragon (2010). New types of Glycation of current multidisciplinary interest are reviewed: ‘Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome’ Rabbani and Thornalley (2010b), ‘Enzymatic repair of early Glycation’ by Van Schaftingen et al. (2010), and ‘Advanced Glycation Endproducts: From Precursors to the Receptor RAGE’ by Ramasamy et al. (2010). There are then reviews on the current focus of Glycation in biomedical research. Four reviews focus on the important impact of Glycation in diabetes and related complications: ‘Lipid Glycation modifications in diabetes and atherosclerosis’ by Miyazawa et al. (2010), ‘Glycation and biomarkers of vascular complications of diabetes’ by Beisswenger (2010), ‘Glycation in diabetic nephropathy’ by Forbes and Cooper (2010), and ‘Earlyand advanced non-enzymatic Glycation in diabetic vascular complications and search for therapeutics’ by Schalkwijk and Miyata (2010). Finally, the compilation concludes with two reviews on the biomedical importance of Glycation in ageing-related disorders: ‘The Pathogenic Role of the Maillard Reaction in the Aging Eye’ by Nagaraj et al. (2010), and ‘Advanced Glycation endproducts and their pathogenic roles in neurological disorders’ by Munch et al. (2010). We thank all authors for their commitment and contributions to this compilation and we trust that this will be the start of an expanding and long-standing partnership of Amino Acids with Glycation research.
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advanced Glycation end products in extracellular matrix proteins contribute to the failure of sensory nerve regeneration in diabetes
Diabetes, 2009Co-Authors: Beatriz Duranjimenez, Paul J Thornalley, Naila Rabbani, Darin Dobler, Sarah Moffatt, Charles H Streuli, David R Tomlinson, Natalie J GardinerAbstract:OBJECTIVE: The goal of this study was to characterize Glycation adducts formed in both in vivo extracellular matrix (ECM) proteins of endoneurium from streptozotocin (STZ)-induced diabetic rats and in vitro by Glycation of laminin and fibronectin with methylglyoxal and glucose. We also investigated the impact of advanced Glycation end product (AGE) residue content of ECM on neurite outgrowth from sensory neurons. RESEARCH DESIGN AND METHODS: Glycation, oxidation, and nitration adducts of ECM proteins extracted from the endoneurium of control and STZ-induced diabetic rat sciatic nerve (3-24 weeks post-STZ) and of laminin and fibronectin that had been glycated using glucose or methylglyoxal were examined by liquid chromatography with tandem mass spectrometry. Methylglyoxal-glycated or unmodified ECM proteins were used as substrata for dissociated rat sensory neurons as in vitro models of regeneration. RESULTS: STZ-induced diabetes produced a significant increase in early Glycation N(epsilon)-fructosyl-lysine and AGE residue contents of endoneurial ECM. Glycation of laminin and fibronectin by methylglyoxal and glucose increased Glycation adduct residue contents with methylglyoxal-derived hydroimidazolone and N(epsilon)-fructosyl-lysine, respectively, of greatest quantitative importance. Glycation of laminin caused a significant decrease in both neurotrophin-stimulated and preconditioned sensory neurite outgrowth. This decrease was prevented by aminoguanidine. Glycation of fibronectin also decreased preconditioned neurite outgrowth, which was prevented by aminoguanidine and nerve growth factor. CONCLUSIONS: Early Glycation and AGE residue content of endoneurial ECM proteins increase markedly in STZ-induced diabetes. Glycation of laminin and fibronectin causes a reduction in neurotrophin-stimulated neurite outgrowth and preconditioned neurite outgrowth. This may provide a mechanism for the failure of collateral sprouting and axonal regeneration in diabetic neuropathy.
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Highlights and hotspots of protein Glycation in end-stage renal disease.
Seminars in dialysis, 2009Co-Authors: Paul J Thornalley, Naila RabbaniAbstract:Analysis of tissues, plasma, urine, other body fluids, and dialysate for Glycation adducts has revealed the presence of two major forms: Glycation adduct residues of proteins and related glycated amino acids—called Glycation free adducts. The major effect on protein Glycation in uremia is loss of clearance of Glycation free adducts and their marked increase in plasma. Changes in Glycation adduct residue content of plasma protein in uremia is, in contrast, relatively modest. There is now doubt as to whether the concept of interaction of advanced Glycation endproduct (AGE)-modified proteins with putative AGE receptors can be sustained in vivo. A residual important feature of the receptor for AGEs may be decrease in expression of glyoxalase 1 of the antiGlycation defence by S100A12 protein leaving the vasculature vulnerable to dicarbonyl stress and related AGE formation. The dicarbonyl proteome, proteins susceptible to dicarbonyl Glycation at functional sites, is the likely mediator of Glycation damage in uremia. Glycation of type IV collagen with shedding of endothelial cells and Glycation of apolipoprotein B100 with increased atherogenicity of low density lipoprotein are two examples which may link protein Glycation to increased risk of cardiovascular disease in end-stage renal disease.
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Advanced Glycation end products in renal failure.
Journal of renal nutrition : the official journal of the Council on Renal Nutrition of the National Kidney Foundation, 2006Co-Authors: Paul J ThornalleyAbstract:Cellular and extracellular proteins suffer significant damage in vivo by Glycation. Physiological proteolysis of proteins damaged by Glycation forms Glycation free adducts that are released into plasma for urinary excretion. Inefficient elimination of these free adducts in uremia leads to their accumulation. In mild renal insufficiency, plasma Glycation free adducts accumulated as renal clearance declined. In patients with end-stage renal disease, plasma Glycation free adducts were increased up to 18-fold on peritoneal dialysis and up to 40-fold on hemodialysis. Glycation free adduct concentrations in peritoneal dialysate increased with dialysate dwell time, achieving concentrations in the dialysate higher than in plasma—suggesting that Glycation adduct formation may occur in the peritoneal cavity and active transport into the peritoneal cavity may occur. In hemodialysis, plasma Glycation free adducts equilibrated rapidly across the dialysis membrane, with both plasma and dialysate concentrations decreasing during a dialysis session. Therefore, protein Glycation free adducts normally excreted efficiently in urine show profound mishandling and accumulation in chronic renal failure. Their accumulation may impair vascular cell function and contribute to morbidity and mortality in renal disease.
Lu Zhang - One of the best experts on this subject based on the ideXlab platform.
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mechanisms of isoquercitrin attenuates ovalbumin Glycation investigation by spectroscopy spectrometry and molecular docking
Food Chemistry, 2020Co-Authors: Lu Zhang, Liang Xu, Zongcai Tu, Honghong WangAbstract:Abstract This research firstly investigated the inhibitory effect of isoquercitrin (ISQ) on Ovalbumin (OVA) Glycation. The mechanism was elucidated through the interaction between OVA and ISQ, and changes in Glycation sites and degree of each site as deduced by spectroscopy, spectrometry and molecular docking. ISQ significantly inhibited OVA Glycation by attenuating the conformational change induced by Glycation. It quenched the fluorescence of Trp via static mechanism, and exposed Trp residues to a more hydrophobic surroundings. Formation of OVA-ISQ complex was a endothermic processing driven by hydrophobic interactions, van der Waals forces and hydrogen bonds. LC-Orbitrap-MS/MS revealed that ISQ altered the location of Glycation and alleviated the Glycation degree of most sites. Molecular docking results indicated that ISQ inserted into the hydrophobic pocket of OVA with six hydrogen bonds and one π-π stacking formed between ISQ and the amino acid residues of OVA, leading to the altered Glycation activity of some sites.
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investigation into allergenicity reduction and Glycation sites of glycated β lactoglobulin with ultrasound pretreatment by high resolution mass spectrometry
Food Chemistry, 2018Co-Authors: Guangxian Liu, Tao Huang, Wenhua Yang, Hui Wang, Lu Zhang, Jun LiuAbstract:Abstract Ultrasound treatment could change the conformation of β-lactoglobulin (β-Lg) and improve the Glycation reaction in aqueous solution under neutral condition. However, the effect of ultrasound pretreatment on Glycation of β-Lg with pentose at dry-state remains ambiguous, and the relationship between Glycation and allergenicity of β-Lg with ultrasound pretreatment is unclear. This study aimed to evaluate the effect of ultrasound pretreatment on Glycation and allergenicity of β-Lg. Markedly decreased allergenicity of β-Lg was observed after Glycation with ribose before and after ultrasound pretreatment with the minimum found at 400 W. Orbitrap LC–MS/MS showed that the Glycation degree of some peptides in glycated β-Lg with and without ultrasound pretreatment were different although the content of free amino group and molecular mass were insignificantly different. Therefore, ultrasound pretreatment promoted the reduction in allergenicity by improving the Glycation extent of some Glycation sites although it hardly enhanced the whole Glycation degree of β-Lg.
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the reduction in the ige binding ability of β lactoglobulin by dynamic high pressure microfluidization coupled with Glycation treatment revealed by high resolution mass spectrometry
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Yuan Chen, Tao Huang, Hui Wang, Lu Zhang, Zongcai Tu, Qiuting Zhang, Juanjuan Pang, Ping YangAbstract:Our previous study indicated that pretreatment by dynamic high-pressure microfluidization (DHPM) and Glycation with galactose was a promising method for decreasing the immunoglobulin E (IgE)-binding ability of β-lactoglobulin (β-LG). In this work, the conformational alteration of β-LG subjected to DHPM and Glycation treatment was investigated in relation to IgE-binding ability by orbitrap mass spectrometry. After DHPM pretreatment, lower IgE-binding ability of glycated β-LG was observed with increasing pressures. Prior to DHPM pretreatment, 11 glycated sites were identified, while the number of Glycation sites was increased to 12 after pretreatment. However, there was no significant difference of the Glycation sites at the pressures of 50, 100, and 200 MPa, respectively. Average degree of substitution per peptide molecule of β-LG (DSP) was investigated to assess the degree of Glycation per Glycation site. All of the samples pretreated by DHPM exhibited a higher Glycation level than those without DHPM pret...
Hui Wang - One of the best experts on this subject based on the ideXlab platform.
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Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry
2019Co-Authors: Yipeng Yang, Guangxian Liu, Hui WangAbstract:Glycation between ovalbumin (OVA) and different monoses under mild dry heating at 37 °C was studied. The content of free amino groups decreased dramatically, and the conformational changes based on fluorescence and circular dichroism spectra were evident in glycated OVA. The glycated sites and the average degree of substitution per peptide molecule per site were determined using liquid chromatography high-resolution mass spectrometry. Lysine and arginine were the predominant glyaction sites, in which Lys207 was a relatively reactive site for Glycation in all of the conjugates. In general, the extent of Glycation of aldose was higher, and its alterations on the steric layouts of protein were more drastic than those of ketose. The configuration of hydroxyl groups at C-4 in sugar epimers might be important for the Glycation reactivity and conformational modification in the glycated proteins. These insights would have important implications for the creation of sweetened food products with desirable structures and excellent quality control
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investigation into allergenicity reduction and Glycation sites of glycated β lactoglobulin with ultrasound pretreatment by high resolution mass spectrometry
Food Chemistry, 2018Co-Authors: Guangxian Liu, Tao Huang, Wenhua Yang, Hui Wang, Lu Zhang, Jun LiuAbstract:Abstract Ultrasound treatment could change the conformation of β-lactoglobulin (β-Lg) and improve the Glycation reaction in aqueous solution under neutral condition. However, the effect of ultrasound pretreatment on Glycation of β-Lg with pentose at dry-state remains ambiguous, and the relationship between Glycation and allergenicity of β-Lg with ultrasound pretreatment is unclear. This study aimed to evaluate the effect of ultrasound pretreatment on Glycation and allergenicity of β-Lg. Markedly decreased allergenicity of β-Lg was observed after Glycation with ribose before and after ultrasound pretreatment with the minimum found at 400 W. Orbitrap LC–MS/MS showed that the Glycation degree of some peptides in glycated β-Lg with and without ultrasound pretreatment were different although the content of free amino group and molecular mass were insignificantly different. Therefore, ultrasound pretreatment promoted the reduction in allergenicity by improving the Glycation extent of some Glycation sites although it hardly enhanced the whole Glycation degree of β-Lg.
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the reduction in the ige binding ability of β lactoglobulin by dynamic high pressure microfluidization coupled with Glycation treatment revealed by high resolution mass spectrometry
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Yuan Chen, Tao Huang, Hui Wang, Lu Zhang, Zongcai Tu, Qiuting Zhang, Juanjuan Pang, Ping YangAbstract:Our previous study indicated that pretreatment by dynamic high-pressure microfluidization (DHPM) and Glycation with galactose was a promising method for decreasing the immunoglobulin E (IgE)-binding ability of β-lactoglobulin (β-LG). In this work, the conformational alteration of β-LG subjected to DHPM and Glycation treatment was investigated in relation to IgE-binding ability by orbitrap mass spectrometry. After DHPM pretreatment, lower IgE-binding ability of glycated β-LG was observed with increasing pressures. Prior to DHPM pretreatment, 11 glycated sites were identified, while the number of Glycation sites was increased to 12 after pretreatment. However, there was no significant difference of the Glycation sites at the pressures of 50, 100, and 200 MPa, respectively. Average degree of substitution per peptide molecule of β-LG (DSP) was investigated to assess the degree of Glycation per Glycation site. All of the samples pretreated by DHPM exhibited a higher Glycation level than those without DHPM pret...
Jun Liu - One of the best experts on this subject based on the ideXlab platform.
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investigation into allergenicity reduction and Glycation sites of glycated β lactoglobulin with ultrasound pretreatment by high resolution mass spectrometry
Food Chemistry, 2018Co-Authors: Guangxian Liu, Tao Huang, Wenhua Yang, Hui Wang, Lu Zhang, Jun LiuAbstract:Abstract Ultrasound treatment could change the conformation of β-lactoglobulin (β-Lg) and improve the Glycation reaction in aqueous solution under neutral condition. However, the effect of ultrasound pretreatment on Glycation of β-Lg with pentose at dry-state remains ambiguous, and the relationship between Glycation and allergenicity of β-Lg with ultrasound pretreatment is unclear. This study aimed to evaluate the effect of ultrasound pretreatment on Glycation and allergenicity of β-Lg. Markedly decreased allergenicity of β-Lg was observed after Glycation with ribose before and after ultrasound pretreatment with the minimum found at 400 W. Orbitrap LC–MS/MS showed that the Glycation degree of some peptides in glycated β-Lg with and without ultrasound pretreatment were different although the content of free amino group and molecular mass were insignificantly different. Therefore, ultrasound pretreatment promoted the reduction in allergenicity by improving the Glycation extent of some Glycation sites although it hardly enhanced the whole Glycation degree of β-Lg.
Tao Huang - One of the best experts on this subject based on the ideXlab platform.
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investigation into allergenicity reduction and Glycation sites of glycated β lactoglobulin with ultrasound pretreatment by high resolution mass spectrometry
Food Chemistry, 2018Co-Authors: Guangxian Liu, Tao Huang, Wenhua Yang, Hui Wang, Lu Zhang, Jun LiuAbstract:Abstract Ultrasound treatment could change the conformation of β-lactoglobulin (β-Lg) and improve the Glycation reaction in aqueous solution under neutral condition. However, the effect of ultrasound pretreatment on Glycation of β-Lg with pentose at dry-state remains ambiguous, and the relationship between Glycation and allergenicity of β-Lg with ultrasound pretreatment is unclear. This study aimed to evaluate the effect of ultrasound pretreatment on Glycation and allergenicity of β-Lg. Markedly decreased allergenicity of β-Lg was observed after Glycation with ribose before and after ultrasound pretreatment with the minimum found at 400 W. Orbitrap LC–MS/MS showed that the Glycation degree of some peptides in glycated β-Lg with and without ultrasound pretreatment were different although the content of free amino group and molecular mass were insignificantly different. Therefore, ultrasound pretreatment promoted the reduction in allergenicity by improving the Glycation extent of some Glycation sites although it hardly enhanced the whole Glycation degree of β-Lg.
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the reduction in the ige binding ability of β lactoglobulin by dynamic high pressure microfluidization coupled with Glycation treatment revealed by high resolution mass spectrometry
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Yuan Chen, Tao Huang, Hui Wang, Lu Zhang, Zongcai Tu, Qiuting Zhang, Juanjuan Pang, Ping YangAbstract:Our previous study indicated that pretreatment by dynamic high-pressure microfluidization (DHPM) and Glycation with galactose was a promising method for decreasing the immunoglobulin E (IgE)-binding ability of β-lactoglobulin (β-LG). In this work, the conformational alteration of β-LG subjected to DHPM and Glycation treatment was investigated in relation to IgE-binding ability by orbitrap mass spectrometry. After DHPM pretreatment, lower IgE-binding ability of glycated β-LG was observed with increasing pressures. Prior to DHPM pretreatment, 11 glycated sites were identified, while the number of Glycation sites was increased to 12 after pretreatment. However, there was no significant difference of the Glycation sites at the pressures of 50, 100, and 200 MPa, respectively. Average degree of substitution per peptide molecule of β-LG (DSP) was investigated to assess the degree of Glycation per Glycation site. All of the samples pretreated by DHPM exhibited a higher Glycation level than those without DHPM pret...
