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Non Enzymatic Glycation

Lisanne C de Vos, Joop D Lefrandt, Robin P F Dullaart, Clark J Zeebregts, Andries J Smit
Patients with peripheral artery disease (PAD) suffer from widespread atherosclerosis. Partly due to the growing awareness of cardiovascular disease, the incidence of PAD has increased considerably during the past decade. It is anticipated that algorithms to identify high risk patients for cardiovascular events require being updated, making use of novel biomarkers. Advanced glycation end products (AGEs) are moieties formed non-enzymatically on long-lived proteins under influence of glycemic and oxidative stress reactions...
October 6, 2016: Atherosclerosis
Sarbani Ashe, Debasis Nayak, Manisha Kumari, Bismita Nayak
Advanced glycation end-products (AGEs) resulting from non-enzymatic glycation are one of the major factors involved in diabetes and its secondary complications and diseases. This necessitates our urge to discover new compounds that may be used as potential AGEs inhibitors without affecting the normal structure and function of biomolecules. In the present study, we investigated the inhibitory effects of AgNP (silver nanoparticles) on AGEs formation as well as their inhibitory effects on glycation mediated cell toxicity via ROS production and DNA damage...
October 17, 2016: ACS Applied Materials & Interfaces
Hossam M Abdallah, Hany M El-Bassossy, Gamal A Mohamed, Ali M El-Halawany, Khalid Z Alshali, Zainy M Banjar
Advanced glycation end-products (AGEs) are associated with a non-enzymatic reaction between the amino group of a protein and the carbonyl group of a sugar during hyperglycemia. The precipitation of AGEs in different tissues leads to many complications, such as endothelial dysfunction, cardiovascular complications, atherosclerosis, retinopathy, neuropathy, and Alzheimer's disease. Garcinia mangostana L. (Clusiaceae) (GM) was selected owing to the ability of its polar and non-polar fractions to inhibit AGE formation...
October 13, 2016: Journal of Natural Medicines
Kailash Prasad, Shuchita Tiwari
Advanced glycation end products (AGEs) are heterogeneous group of molecules formed from non-enzymatic reaction of reducing sugars with amino group of proteins, lipids, and nucleic acid. Interaction of AGEs with its cell-bound receptor (RAGE) results in generation of oxygen radicals, nuclear factor kappa-β, pro-inflammatory cytokines and cell adhesion molecules, and is involved in the pathophysiology of cardiovascular diseases (CVD). Circulating soluble forms of RAGE (sRAGE) and endo-secretory RAGE (esRAGE) compete with RAGE for ligand binding and function as a decoy...
October 6, 2016: Current Pharmaceutical Design
Adi Pinkas, Michael Aschner
Advanced glycation end-products (AGEs) are non-enzymatically glycated proteins, lipids and nucleic acids. These compounds both originate exogenously and are formed endogenously, and are associated, along with one of their receptors - RAGE, with a variety of pathologies and neurodegeneration. Some of their deleterious effects include affecting insulin signaling and FOXO-related pathways in both receptor-dependent and -independent manner. A potential ameliorating agent for these effects is insulin, which is being studied in several in vivo and in vitro models; one of these models is C...
October 5, 2016: Chemical Research in Toxicology
Masahiro Yamamoto, Toshitsugu Sugimoto
Diabetic patients have a higher fracture risk than expected by their bone mineral density (BMD). Poor bone quality is the most suitable and explainable cause for the elevated fracture risk in this population. Advanced glycation end products (AGEs), which are diverse compounds generated via a non-enzymatic reaction between reducing sugars and amine residues, physically affect the properties of the bone material, one of a component of bone quality, through their accumulation in the bone collagen fibers. On the other hand, these compounds biologically act as agonists for these receptors for AGEs (RAGE) and suppress bone metabolism...
October 4, 2016: Current Osteoporosis Reports
Ivana Sirangelo, Filomena M Vella, Gaetano Irace, Giuseppe Manco, Clara Iannuzzi
Superoxide dismutase 1 (SOD1) has been implicated with familial amyotrophic lateral sclerosis (fALS) through accumulation of protein amyloid aggregates in motor neurons of patients. Amyloid aggregates and protein inclusions are a common pathological feature of many neurological disorders in which protein aggregation seems to be directly related to neurotoxicity. Although, extensive studies performed on the aggregation process of several amyloidogenic proteins in vitro allowed the identification of many physiological factors involved, the molecular mechanisms underlying the formation of amyloid aggregates in vivo and in pathological conditions are still poorly understood...
2016: Frontiers in Molecular Biosciences
Mercedes Rodriguez-Teja, Claudia Breit, Mitchell Clarke, Kamil Talar, Kai Wang, Mohammad A Mohammad, Sage Pickwell, Guillermina Etchandy, Graeme J Stasiuk, Justin Sturge
Here we describe a protocol that can be used to study the biophysical microenvironment related to increased thickness and stiffness of the basement membrane (BM) during age-related pathologies and metabolic disorders (e.g. cancer, diabetes, microvascular disease, retinopathy, nephropathy and neuropathy). The premise of the model is non-enzymatic crosslinking of reconstituted BM (rBM) matrix by treatment with glycolaldehyde (GLA) to promote advanced glycation endproduct (AGE) generation via the Maillard reaction...
2016: Journal of Visualized Experiments: JoVE
Mitsuru Saito, Keishi Marumo
Chronic obstructive pulmonary disease(COPD)is a chronic inflammatory disease associated with an increase of fracture risk. Bone strength is determined by bone mass and quality.Bone quality is thought to encompass the structural and material properties of bone. Bone collagen crosslinking plays important roles in bone strength. The quantitative and qualitative deterioration of lysyl oxidase control and non enzymatic cross-links(advanced glycation end products, AGEs, pentosidine)of collagen in patients with osteoporotic femoral neck fracture and diabetes, and COPD might be affected by increased oxidative stress and glycation...
2016: Clinical Calcium
Saheem Ahmad, Mohammed Farhan
Non-enzymatic protein glycosylation is the addition of free carbonyls to the free amino groups of proteins, amino acids, lipoproteins and nucleic acids resulting in the formation of early glycation products. The early glycation products are also known as Maillard reaction which undergoes dehydration, cyclization and rearrangement to form advanced glycation end-products (AGEs). By and large the researchers in the past have also established that glycation and the AGEs are responsible for most type of metabolic disorders, including diabetes mellitus, cancer, neurological disorders and aging...
2016: Advances in Neurobiology
Thomas A Collier, Anthony Nash, Helen L Birch, Nora H de Leeuw
Covalently cross-linked advanced glycation end products (AGE) are among the major post-translational modifications to proteins as a result of non-enzymatic glycation. The formation of AGEs has been shown to have adverse effects on the properties of the collagenous tissue; they are even linked to a number of age related disorders. Little is known about the sites at which these AGEs form or why certain sites within the collagen are energetically more favourable than others. In this study we have used a proven fully atomistic molecular dynamics approach to identify six sites where the formation of the intra-molecular 3-deoxyglucosone-derived imidazolium cross-link (DOGDIC) is energetically favourable...
November 2016: Biophysical Chemistry
Kei-Ichiro Kitamura, Tadashi Andoh, Wakana Okesaku, Yuya Tazaki, Kazuhiro Ogai, Kayo Sugitani, Isao Kobayashi, Nobuo Suzuki, Wenxi Chen, Mika Ikegame, Atsuhiko Hattori
Increased risk of fracture associated with type 2 diabetes has been a topic of recent concern. Fracture risk is related to a decrease in bone strength, which can be affected by bone metabolism and the quality of the bone. To investigate the cause of the increased fracture rate in patients with diabetes through analyses of bone metabolism and bone matrix protein properties, we used goldfish scales as a bone model for hyperglycemia. Using the scales of seven alloxan-treated and seven vehicle-treated control goldfish, we assessed bone metabolism by analyzing the activity of marker enzymes and mRNA expression of marker genes, and we measured the change in molecular weight of scale matrix proteins with SDS-PAGE...
September 16, 2016: Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
Renaat Coopman, Thijs Van de Vyver, Antoine Sadiki Kishabongo, Philippe Katchunga, Elisabeth H Van Aken, Justin Cikomola, Tinne Monteyne, Marijn M Speeckaert, Joris R Delanghe
OBJECTIVES: Although HbA1c is a good diagnostic tool for diabetes, the precarity of the health system and the costs limit the use of this biomarker in developing countries. Fingernail clippings contain ±85% of keratins, which are prone to glycation. Nail keratin glycation may reflect the average glycemia over the last months. We explored if attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) can be used as a non-invasive tool for assessing glycation in diabetes...
September 3, 2016: Clinical Biochemistry
Michael Hellwig, Sophia Witte, Thomas Henle
The Maillard reaction is important for beer color and flavor, but little is known about the occurrence of individual glycated amino acids in beer. Therefore, seven Maillard reaction products (MRPs), namely, fructosyllysine, maltulosyllysine, pyrraline, formyline, maltosine, MG-H1, and argpyrimidine, were synthesized and quantitated in different types of beer (Pilsner, dark, bock, wheat, and nonalcoholic beers) by HPLC-ESI-MS/MS in the multiple reaction monitoring mode through application of the standard addition method...
September 28, 2016: Journal of Agricultural and Food Chemistry
Mohd Shahnawaz Khan, Nayyar Rabbani, Shams Tabrez, Badar Islam, Ajmaluddin Malik, Anwar Ahmed, Mohammad A Alsenaidy, Abdulrahman M Al-Senaidy
The non-enzymatic reaction (glycation) of reducing sugars with proteins has received increased interest in dietary and therapeutic research lately. In the present work, the impact of glycation on structural alterations of camel serum albumin (CSA) by different glucose metabolites was studied. Glycation of CSA was evaluated by specific fluorescence of advanced glycation end-products (AGEs) and determination of available amino groups. Further, conformational changes in CSA during glycation were also studied using 8-analino 1-nephthlene sulfonic acid (ANS) binding assay, circular dichroism (CD) and thermal analysis...
August 31, 2016: Protein and Peptide Letters
Thomas B Parsons, Weston B Struwe, Joseph Gault, Keisuke Yamamoto, Thomas A Taylor, Ritu Raj, Kim Wals, Shabaz Mohammed, Carol V Robinson, Justin L P Benesch, Benjamin G Davis
Glycosylation patterns in antibodies critically determine biological and physical properties but their precise control is a significant challenge in biology and biotechnology. We describe herein the optimization of an endoglycosidase-catalyzed glycosylation of the best-selling biotherapeutic Herceptin, an anti-HER2 antibody. Precise MS analysis of the intact four-chain Ab heteromultimer reveals nonspecific, non-enzymatic reactions (glycation), which are not detected under standard denaturing conditions. This competing reaction, which has hitherto been underestimated as a source of side products, can now be minimized...
February 12, 2016: Angewandte Chemie
G M Campbell, S Tiwari, A-K Picke, C Hofbauer, M Rauner, M M Morlock, L C Hofbauer, C-C Glüer
Type 2 diabetes mellitus increases skeletal fragility; however, the contributing mechanisms and optimal treatment strategies remain unclear. We studied the effects of diabetes and insulin therapy on non-enzymatic glycation (NEG), cortical porosity (Ct.Po) and biomechanics of the bone tissue in Zucker Diabetic Fatty (ZDF) rats. Eleven-week old ZDF diabetic and non-diabetic rats were given insulin to achieve glycaemic control or vehicle seven days per week over twelve weeks (insulin dose adapted individually 0...
October 2016: Bone
Lenka Michalcová, Zdeněk Glatz
Diabetes is one of the most widespread diseases characterized by a deficiency in the production of insulin or its ineffectiveness. As a result, the increased concentrations of glucose in the blood lead not only to damage to many of the body's systems but also cause the nonenzymatic glycation of plasma proteins affecting their drug binding. Since the binding ability influences its pharmacokinetics and pharmacodynamics, this is a very important issue in the development of new drugs and personalized medicine. In this study, capillary electrophoresis-frontal analysis was used to evaluate the affinities between human serum albumin or its glycated form and the first generation of sulfonylurea antidiabetics, since their inadequate concentration may induce hypoglycaemia or on the contrary hyperglycaemia...
September 2016: Journal of Separation Science
Yuki Ogasawara, Ryo Tanaka, Shin Koike, Yasue Horiuchi, Mitsuhiro Miyashita, Makoto Arai
Methylglyoxal (MG) is a highly reactive dicarbonyl compound that promotes the non-enzymatic glycation of proteins to yield irreversible advanced glycated end products, leading to the cross-linking or degradation of proteins. The physiological relevance of MG currently remains unclear because its metabolic behavior has not yet been elucidated in detail. Although several labeling methods that require a HPLC system have been developed and used to measure MG, a standard method to analyze the content of MG in biological samples has not been established...
September 1, 2016: Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Alexandra K Pastino, Todd M Greco, Rommel A Mathias, Ileana M Cristea, Jean E Schwarzbauer
Advanced glycation endproducts (AGEs) are a heterogeneous group of compounds that form via non-enzymatic glycation of proteins throughout our lifespan and at a higher rate in certain chronic diseases such as diabetes. AGEs contribute to the progression of fibrosis, in part by stimulating cellular pathways that affect gene expression. Long-lived ECM proteins are targets for non-enzymatic glycation but the question of whether the AGE-modified ECM leads to excess ECM accumulation and fibrosis remains unanswered...
July 14, 2016: Matrix Biology: Journal of the International Society for Matrix Biology
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