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Non Enzymatic Glycation

Annekatrin König, Hugo Vicente Miranda, Tiago Fleming Outeiro
 Parkinson's disease (PD) is a neurodegenerative disorder with complex etiology and variable pathology. While a subset of cases is associated with single-gene mutations, the majority originates from a combination of factors we do not fully understand. Thus, understanding the underlying causes of PD is indispensable for the development of novel therapeutics. Glycation, the non-enzymatic reaction between reactive dicarbonyls and amino groups, gives rise to a variety of different reaction products known as advanced glycation end products (AGEs)...
2018: Journal of Parkinson's Disease
Mariarosa Maietta, Raffaella Colombo, Federica Corana, Adele Papetti
Accumulation of advanced glycation end products (AGEs) in vivo is associated with many chronic disorders such as diabetes, renal failure, aging, and Alzheimer's disease. The aim of this study was to expand the knowledge about the functional properties of Origanum dictamnus L. beverage (Cretan tea) by an investigation about the inhibitory effects on the formation of AGEs and the capacity to trap dicarbonyl compounds. Dittany infusion was characterized for its polyphenolic composition by RP-HPLC-DAD-ESI/MS n and twenty compounds were detected...
February 12, 2018: Food & Function
Allisson Benatti Justino, Natália Carnevalli Miranda, Rodrigo Rodrigues Franco, Mário Machado Martins, Neide Maria da Silva, Foued Salmen Espindola
Annona muricata leaves are used in traditional medicine to manage diabetes mellitus and its complications. The aim of this study was to evaluate the potential in vitro antidiabetic properties of Annona muricata leaf by identifying its main phytochemical constituents and characterizing the phenolic-enriched fractions for their in vitro antioxidant capacity and inhibitory activities against glycoside and lipid hydrolases, advanced glycation end-product formation and lipid peroxidation. Ethanol extract of A. muricata leaf was subjected to a liquid-liquid partitioning and its fractions were used in enzymatic assays to evaluate their inhibitory potential against α-amylase, α-glucosidase and lipase, as well as their antioxidant (DPPH, ORAC, FRAP and Fe2+-ascorbate-induced lipid peroxidation assays) and anti-glycation (BSA-fructose, BSA-methylglyoxal and arginine-methylglyoxal models) capacities...
February 6, 2018: Biomedicine & Pharmacotherapy, Biomédecine & Pharmacothérapie
Ulrika Wendel, Nina Persson, Christian Risinger, Eva Bengtsson, Björn Nodin, Lena Danielsson, Charlotte Welinder, Gunilla Nordin Fredrikson, Bo Jansson, Ola Blixt
Advanced glycation end products are formed by non-enzymatic reactions between proteins and carbohydrates, causing irreversible lysine and arginine alterations that severely affect protein structure and function. The resulting modifications induce inflammation by binding to scavenger receptors. An increase in advanced glycation end products is observed in a number of diseases e.g. atherosclerosis and cancer. Since advanced glycation end products also are present in healthy individuals, their detection and quantification are of great importance for usage as potential biomarkers...
2018: PloS One
Corinne J Thomas, Timothy P Cleland, Grazyna E Sroga, Deepak Vashishth
Advanced glycation end-products (AGEs) are a category of post translational modification associated with the degradation of the structural properties of multiple different types of tissues. Typically, AGEs are the result of a series of post-translational modification reactions between sugars and proteins through a process known as non-enzymatic glycation (NEG). Increases in the rate of NEG of bone tissue are associated with type 2 diabetes and skeletal fragility. Current methods of assessing NEG and its impact on bone fracture risk involve measurement of pentosidine or total fluorescent AGEs (fAGEs)...
February 1, 2018: Bone
Camila Tiefensee Ribeiro, Juciano Gasparotto, Alexsander Alves Teixeira, Luis Valmor Cruz Portela, Viviane Noll Louzada Flores, José Claudio Fonseca Moreira, Daniel Pens Gelain
The receptor for advanced glycation endproducts (RAGE) is a multi-ligand receptor, which activation amplifies and perpetuates inflammatory reactions. RAGE activation also strongly stimulates the production of reactive oxygen species, leading an imbalance of redox cellular state. The extent of liver damage caused by inflammation is crucial to the systemic response during proinflammatory episodes. To investigate the role of RAGE in liver damage caused by systemic inflammation, we evaluated the effect of RAGE blocking in oxidative stress parameters induced by systemic LPS injection...
January 22, 2018: Journal of Biochemistry
Hee Jung Kang, Haneulnari Lee, Eun Mi Park, Jong-Min Kim, Jun-Seop Shin, Chung-Gyu Park
BACKGROUND: The development of a precise and easy-to-use tool for monitoring islet graft function is important in clarifying the causes of graft loss, identifying appropriate therapy, and ensuring graft survival in the nonhuman primate (NHP) model of porcine islet transplantation (PITx). Glycated albumin (GA) is an indicator of intermediate-term changes in blood glucose control and is useful in clinical diabetes management. The validity of GA for monitoring graft function in NHP recipients of PITx was evaluated using a retrospective analysis of cohort samples...
January 23, 2018: Xenotransplantation
Lorella Marinucci, Stefania Balloni, Katia Fettucciari, Maria Bodo, Vincenzo N Talesa, Cinzia Antognelli
Nicotine contained in cigarette smoke contributes to the onset of several diseases, including osteoporosis, whose emerging pathogenic mechanism is associated with osteoblasts apoptosis. Scanty information is available on the molecular mechanisms of nicotine on osteoblasts apoptosis and, consequently, on an important aspect of the pathogenesis of smokers-related osteoporosis. Glyoxalase 1 (Glo1) is the detoxification enzyme of methylglyoxal (MG), a major precursor of advanced glycation end products (AGEs), potent pro-apoptotic agents...
January 17, 2018: Free Radical Biology & Medicine
Mohd Adnan Khan, Zarina Arif, Mohd Asad Khan, Moinuddin, Khursheed Alam
Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins' structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and biophysical changes in human IgG under normal and high glucose after introducing methylglyoxal into the assay mixture. This non-enzymatic reaction mainly engaged lysine residues as indicated by TNBS results. The UV results showed hyperchromicity in modified-IgG samples while fluorescence data supported AGEs formation during the course of reaction...
2018: PloS One
Behdad Pouran, Parisa R Moshtagh, Vahid Arbabi, Jessica Snabel, Reinout Stoop, Jeffrey Ruberti, Jos Malda, Amir A Zadpoor, Harrie Weinans
An important aspect in cartilage ageing is accumulation of advanced glycation end products (AGEs) after exposure to sugars. Advanced glycation results in crosslinks formation between the collagen fibrils in articular cartilage, hampering their flexibility and making cartilage more brittle. In the current study, we investigate whether collagen crosslinking after exposure to sugars depends on the stretching condition of the collagen fibrils. Healthy equine cartilage specimens were exposed to L-threose sugar and placed in hypo-, iso- or hyper-osmolal conditions that expanded or shrank the tissue and changed the 3D conformation of collagen fibrils...
January 15, 2018: Journal of Orthopaedic Research: Official Publication of the Orthopaedic Research Society
Richard Kehm, Jeannette König, Kerstin Nowotny, Tobias Jung, Stephanie Deubel, Sabrina Gohlke, Tim Julius Schulz, Annika Höhn
Aged tissues usually show a decreased regenerative capacity accompanied by a decline in functionality. During aging pancreatic islets also undergo several morphological and metabolic changes. Besides proliferative and regenerative limitations, endocrine cells lose their secretory capacity, contributing to a decline in functional islet mass and a deregulated glucose homeostasis. This is linked to several features of aging, such as induction of cellular senescence or the formation of modified proteins, such as advanced glycation end products (AGEs) - the latter mainly examined in relation to hyperglycemia and in disease models...
May 2018: Redox Biology
Saima Rasheed, Sara S Sánchez, Sammer Yousuf, Stella M Honoré, M Iqbal Choudhary
Drug repositioning or repurposing, i.e. identifying new indications for existing drugs, has gained increasing attention in the recent years. This approach enables the scientists to discover "new targets" for known drugs in a cost and time efficient manner. Glycation, the non-enzymatic reaction of sugars with proteins or nucleic acids to form early glycation (Amadori or fructosamine) products, is a key molecular basis of diabetic complications. Inhibiting the process of non-enzymatic protein glycation is one of the key strategies to prevent glycation-mediated diabetic complications...
2018: PloS One
Lakshmishri Ramachandra Bhat, Srinivasan Vedantham, Uma Maheswari Krishnan, John Bosco Balaguru Rayappan
Methylglyoxal (MG) is a predominant precursor for advanced glycation end products (AGEs) due to its protein glycation reactions, which are the major causes of diabetic complications. MG is explored as a significant biomarker towards the prediction of diabetic complications. With this background, a non-enzymatic electrochemical biosensor has been developed to detect MG in human blood plasma samples. Microwave synthesized V2O5 nanoplates were used as interface material in the fabrication of modified gold (Au) working electrode for electrochemical MG biosensor...
December 23, 2017: Biosensors & Bioelectronics
Heather B Hunt, Jared C Pearl, David R Diaz, Karen B King, Eve Donnelly
Type 2 diabetes mellitus (T2DM) increases fracture risk for a given bone mineral density, which suggests that T2DM changes bone tissue properties independently of bone mass. In this study, we assessed the effects of hyperglycemia on bone tissue compositional properties, enzymatic collagen crosslinks, and advanced glycation endproducts (AGEs) in the KK-Ay murine model of T2DM using Fourier transform infrared imaging and high-performance liquid chromatography. Compared to KK-aa littermate controls (n = 8), proximal femoral bone tissue of KK-Ay mice (n = 14) exhibited increased collagen maturity, increased mineral content, and less heterogeneous mineral properties...
December 27, 2017: Journal of Bone and Mineral Research: the Official Journal of the American Society for Bone and Mineral Research
Marius Cristian NeamŢu, Elena Taina Avramescu, Iulia Rahela Marcu, Adina Turcu-Ştiolică, Mihail Virgil Boldeanu, Oana Maria NeamŢu, Ştefania Tudorache, Rucsandra Elena Dănciulescu Miulescu
Insulin-like growth factor (IGF) family is made up of two polypeptides, IGF-I and IGF-II, six specific binding proteins (IGFBPs 1-6) and specific receptors. IGF-I is involved in the regulation of growth and cellular proliferation and has a similar structure to insulin. The major IGF transport function is attributed to IGFBP-3. Some studies have highlighted the association between IGF and diabetes. The aims of this study were to analyze the correlation between IGF with glycemic control, glomerular filtration rate (GFR), blood pressure, hematological changes or body mass index (BMI) in patients with type 2 diabetes mellitus (T2DM)...
2017: Romanian Journal of Morphology and Embryology, Revue Roumaine de Morphologie et Embryologie
Alena Soboleva, Rico Schmidt, Maria Vikhnina, Tatiana Grishina, Andrej Frolov
Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer's disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation...
December 12, 2017: International Journal of Molecular Sciences
Tyler Rhinesmith, Thomas Turkette, Robert Root-Bernstein
The causes of insulin resistance are not well-understood in either type 1 or type 2 diabetes. Insulin (INS) is known to undergo rapid non-enzymatic covalent conjugation to glucose or other sugars (glycation). Because the insulin receptor (IR) has INS-like regions associated with both glucose and INS binding, we hypothesize that hyperglycemic conditions may rapidly glycate the IR, chronically interfering with INS binding. IR peptides were synthesized spanning IR- associated INS-binding regions. Glycation rates of peptides under hyperglycemic conditions were followed over six days using matrix assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry...
December 2, 2017: International Journal of Molecular Sciences
Di Zhao, Thao T Le, Lotte Bach Larsen, Lin Li, Dan Qin, Guoying Su, Bing Li
α-Dicarbonyl compounds, which are widely found in common consumed food, are one of the precursors of advanced glycation end products (AGEs). In this study, the effect of glycation derived from glyoxal (GO), methylglyoxal (MGO) or butanedione (BU) on the in vitro digestibility of β-casein (β-CN) and β-lactoglobulin (β-Lg) was investigated. Glycation from α-dicarbonyl compounds reduced the in vitro digestibility of studied proteins in both gastric and intestinal stage. In addition, glycation substantially altered the peptides released through gastric and gastrointestinal digestion, as detected by liquid chromatography electrospray-ionization tandem mass spectrometry (LC-ESI-MS/MS)...
December 2017: Food Research International
R Li, R Rajan, W C V Wong, D G Reid, M J Duer, V J Somovilla, N Martinez-Saez, G J L Bernardes, R Hayward, C M Shanahan
Non-enzymatic glycation of extracellular matrix with (U-13 C5 )-d-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH3 -CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes.
December 14, 2017: Chemical Communications: Chem Comm
Alena Soboleva, Maria Vikhnina, Tatiana Grishina, Andrej Frolov
Glycation is a non-enzymatic post-translational modification of proteins, formed by the reaction of reducing sugars and α-dicarbonyl products of their degradation with amino and guanidino groups of proteins. Resulted early glycation products are readily involved in further transformation, yielding a heterogeneous group of advanced glycation end products (AGEs). Their formation is associated with ageing, metabolic diseases, and thermal processing of foods. Therefore, individual glycation adducts are often considered as the markers of related pathologies and food quality...
November 28, 2017: International Journal of Molecular Sciences
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