A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease

Zhang, Qibin; Ames, Jennifer M.; Smith, Richard D.; Baynes, John W.; Metz, Thomas O.

doi:10.1021/pr800858h

Cited by 332 publications

(298 citation statements)

References 142 publications

(338 reference statements)

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“…Moreover, a variety of other pathways such as autoxidation of glucose, or ascorbate and lipid peroxidation, can also lead to AGE formation. The yields of these pathways usually are dicarbonyl intermediates, for example MGO, GO, 3-deoxyglucosone, glycolaldehyde, 1-deoxyglucosone [7] and free radicals [8]. Reaction of glyoxal or methylglyoxal with free lysine groups of proteins gives rise to the formation of AGEs such as CML, carboxyethyllysine or methylglyoxal lysine dimer [9].…”

Section: The Mechanisms Of Inhibition Of Advanced Glycation End Produmentioning

confidence: 99%

The Mechanisms of Inhibition of Advanced Glycation End Products Formation through Polyphenols in Hyperglycemic Condition

et al. 2015

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Glycation, the non-enzymatic binding of glucose to free amino groups of an amino acid, yields irreversible heterogeneous compounds known as advanced glycation end products. Those products play a significant role in diabetic complications. In the present article we briefly discuss the contribution of advanced glycation end products to the pathogenesis of diabetic complications, such as atherosclerosis, diabetic retinopathy, nephropathy, neuropathy, and wound healing. Then we mention the various mechanisms by which polyphenols inhibit the formation of advanced glycation end products. Finally, recent supporting documents are presented to clarify the inhibitory effects of polyphenols on the formation of advanced glycation end products. Phytochemicals apply several antiglycation mechanisms, including glucose metabolism, amelioration of oxidative stress, scavenging of dicarbonyl species, and up/down-regulation of gene expression. To utilize polyphenols in order to remedy diabetic complications, we must explore, examine and clarify the action mechanisms of the components of polyphenols.

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Section: The Mechanisms Of Inhibition Of Advanced Glycation End Produmentioning

confidence: 99%

The Mechanisms of Inhibition of Advanced Glycation End Products Formation through Polyphenols in Hyperglycemic Condition

et al. 2015

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“…The Maillard reaction (MR) encompasses a complex network of reactions and the chemistry concerned has been reviewed by many authors over the last 60 years (e.g., Hodge 1953;Zhang et al 2009). In summary, the MR involves the reaction between the carbonyl group of a reducing sugar with a free amino group, typically the ε-amino group of lysine residues in protein.…”

Section: Chemistry Of the Maillard Reaction (Mr)mentioning

confidence: 99%

Dietary Maillard Reaction Products: Implications for Human Health and Disease

Ames¹

2009

Czech J. Food Sci.

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When foods are heat processed, the sugars and lipids react with the proteins they contain via the Maillard and related reactions to form a wide range of products. As a result, the sensory, safety, nutritional and health-promoting attributes of the foods are affected. Reaction products include advanced glycation/lipoxidation endproducts (AGE/ALEs), acrylamide and heterocyclic amines (HAA), all of which may impact on human health and disease. Furthermore, some Maillard reaction products affect the growth of colonic bacteria and thermally-induced modification of dietary protein can affect allergenicity. This paper briefly reviews aspects of the Maillard reaction in food related to human health.

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“…AGE accumulation is involved in the development of chronic diseases as vascular complications of diabetes and in the development of inflammation in atherosclerosis as well (Zhang et al 2009). Moreover, this accumulation plays a pathological role in the development of atherosclerosis by cross-linking collagen in vessel walls, producing stiffness of blood vessels, oxidizing low density lipoprotein and increasing inflammation through the receptor for AGE (RAGE) (Sims et al 1996, Zieman & Kass 2004.…”

Section: Introductionmentioning

confidence: 99%

Key structural and functional differences between early and advanced glycation products

Paradela-Dobarro

Rodiño-Janeiro

Alonso

et al. 2016

Journal of Molecular Endocrinology

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Most of the studies on advanced glycation end products (AGE) have been carried out with uncharacterized mixtures of AGE, so the observed effects cannot be linked to defined structures. Therefore, we analysed the structural differences between glycated human serum albumin (gHSA), a low glycated protein, and AGE-human serum albumin (AGE-HSA), a high glycated protein, and we compared their effects on endothelial functionality. Specifically, we characterized glycation and composition on both early and advanced stage glycation products of gHSA and AGE-HSA by using the MALDI-TOF-mass spectrometry assay. Furthermore, we studied the effects of both types of glycation products on reactive oxygen species (ROS) production and in the expression of vascular and intercellular cell adhesion molecules (VCAM-1 and ICAM-1) on human umbilical endothelial cells (HUVEC). We also measured the adhesion of peripheral blood mononuclear cells (PBMC) to HUVEC. Low concentrations of gHSA enhanced long-lasting ROS production in HUVEC, whereas lower concentrations of AGE-HSA caused the anticipation of the induced extracellular ROS production. Both gHSA and AGE-HSA up-regulated the expression of VCAM-1 and ICAM-1 at mRNA levels. Nevertheless, only AGE-HSA increased protein levels and enhanced the adhesion of PBMC to HUVEC monolayers. Functional differences were observed between gHSA and AGE-HSA, causing the latter an anticipation of the pro-oxidant effects in comparison to gHSA. Moreover, although both molecules induced genetic up-regulation of adhesion molecules in HUVEC, only the high glycated protein functionally increased mononuclear cell adhesion to endothelial monolayers. These observations could have important clinical consequences in the development of diabetic vascular complications.

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A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease

Cited by 332 publications

References 142 publications

The Mechanisms of Inhibition of Advanced Glycation End Products Formation through Polyphenols in Hyperglycemic Condition

The Mechanisms of Inhibition of Advanced Glycation End Products Formation through Polyphenols in Hyperglycemic Condition

Dietary Maillard Reaction Products: Implications for Human Health and Disease

Key structural and functional differences between early and advanced glycation products

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