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Artykuły w czasopismach na temat "Glycation mediated diabetic"
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Canning, Paul, Josephine V. Glenn, Daniel K. Hsu, Fu-Tong Liu, Tom A. Gardiner i Alan W. Stitt. "Inhibition of Advanced Glycation and Absence of Galectin-3 Prevent Blood-Retinal Barrier Dysfunction during Short-Term Diabetes". Experimental Diabetes Research 2007 (2007): 1–10. http://dx.doi.org/10.1155/2007/51837.
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Breakdown of the inner blood-retinal barrier (iBRB) occurs early in diabetes and is central to the development of sight-threatening diabetic macular edema (DME) as retinopathy progresses. In the current study, we examined how advanced glycation end products (AGEs) forming early in diabetes could modulate vasopermeability factor expression in the diabetic retina and alter inter-endothelial cell tight junction (TJ) integrity leading to iBRB dysfunction. We also investigated the potential for an AGE inhibitor to prevent this acute pathology and examined a role of the AGE-binding protein galectin-3 (Gal-3) in AGE-mediated cell retinal pathophysiology. Diabetes was induced in C57/BL6 wild-type (WT) mice and in Gal-3−/−transgenic mice. Blood glucose was monitored and AGE levels were quantified by ELISA and immunohistochemistry. The diabetic groups were subdivided, and one group was treated with the AGE-inhibitor pyridoxamine (PM) while separate groups of WT and Gal-3−/−mice were maintained as nondiabetic controls. iBRB integrity was assessed by Evans blue assay alongside visualisation of TJ protein complexes via occludin-1 immunolocalization in retinal flat mounts. Retinal expression levels of the vasopermeability factor VEGF were quantified using real-time RT-PCR and ELISA. WT diabetic mice showed significant AGE -immunoreactivity in the retinal microvasculature and also showed significant iBRB breakdown (P<.005). These diabetics had higher VEGF mRNA and protein expression in comparison to controls (P<.01). PM-treated diabetics had normal iBRB function and significantly reduced diabetes-mediated VEGF expression. Diabetic retinal vessels showed disrupted TJ integrity when compared to controls, while PM-treated diabetics demonstrated near-normal configuration. Gal-3−/−mice showed significantly less diabetes-mediated iBRB dysfunction, junctional disruption, and VEGF expression changes than their WT counterparts. The data suggests an AGE-mediated disruption of iBRB via upregulation of VEGF in the diabetic retina, possibly modulating disruption of TJ integrity, even after acute diabetes. Prevention of AGE formation or genetic deletion of Gal-3 can effectively prevent these acute diabetic retinopathy changes.
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Muthenna, Puppala, Chandrasekhar Akileshwari i G. Bhanuprakash Reddy. "Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine". Biochemical Journal 442, nr 1 (27.01.2012): 221–30. http://dx.doi.org/10.1042/bj20110846.
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Non-enzymatic glycation is a complex series of reactions between reducing sugars and amino groups of proteins. Accumulation of AGEs (advanced glycation end-products) due to non-enzymatic glycation has been related to several diseases associated with aging and diabetes. The formation of AGEs is accelerated in hyperglycaemic conditions, which alters the structure and function of long-lived proteins, thereby contributing to long-term diabetic complications. The present study describes AGE inhibition and the mechanism of action of a new antiglycating agent, EA (ellagic acid), a flavonoid present in many dietary sources. Inhibition of AGE formation by EA was demonstrated with different proteins, namely eye lens TSP (total soluble protein), Hb (haemoglobin), lysozyme and BSA, using different glycating agents such as fructose, ribose and methylglyoxal by a set of complementary methods. These results suggest that the antiglycating action of EA seems to involve, apart from inhibition of a few fluorescent AGEs, predominantly inhibition of CEL [Nϵ-(carboxyethyl)lysine] through scavenging of the dicarbonyl compounds. Furthermore, MALDI–TOF-MS (matrix-assisted laser-desorption ionisation–time-of-flight MS) analysis confirms inhibition of the formation of CEL on lysozyme on in vitro glycation by EA. Prevention of glycation-mediated β-sheet formation in Hb and lysozyme by EA confirm its antiglycating ability. Inhibition of glycosylated Hb formation in human blood under ex vivo high-glucose conditions signifies the physiological antiglycating potential of EA. We have also determined the effectiveness of EA against loss of eye lens transparency through inhibition of AGEs in the lens organ culture system. These findings establish the antiglycating potential of EA and its in vivo utility in controlling AGE-mediated diabetic pathologies.
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Rehman, Shahnawaz, Mohammad Faisal, Abdulrahman A. Alatar i Saheem Ahmad. "Physico-chemical Changes Induced in the Serum Proteins Immunoglobulin G and Fibrinogen Mediated by Methylglyoxal". Current Protein & Peptide Science 21, nr 9 (11.12.2020): 916–23. http://dx.doi.org/10.2174/1389203720666190618095719.
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Background: Non-enzymatic glycation of proteins plays a significant role in the pathogenesis of secondary diabetic complications via the formation of advanced glycation end products (AGEs) and increased oxidative stress. Methylglyoxal (MG), a highly reactive dicarbonyl of class α-oxoaldehyde that generates during glucose oxidation and lipid peroxidation, contributes to glycation. Objective: This comparative study focuses on methylglyoxal induced glycoxidative damage suffered by immunoglobulin G (IgG) and fibrinogen, and to unveil implication of structural modification of serum proteins in diabetes-associated secondary complications. Methods: The methylglyoxal induced structural alterations in IgG and fibrinogen were analyzed by UVvis, fluorescence, circular dichroism and Fourier transform infrared (FT-IR) spectroscopy. Ketoamine moieties, carbonyl contents, 5-Hydroxymethylfurfural (HMF) and malondyaldehyde were also quantified. Free lysine and arginine estimation, detection of non-fluorogenic carboxymethyllysine (CML) and fibril formation were confirmed by thioflavin T (ThT) assay. Results: Structural alterations, increased carbonyl contents and ketoamines were reported in MG glycated IgG and fibrinogen against their native analogues. Conclusion: The experiment results validate structural modifications, increased oxidative stress and AGEs formation. Thus, we can conclude that IgG-AGEs and Fib-AGEs formed during MG induced glycation of IgG and fibrinogen could impede normal physiology and might initiates secondary complications in diabetic patients.
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Furtak, Kh Ye, H. Ya Hachkova i N. O. Sybirna. "The effect of Galega officinalis L. extract on the content of the advanced glycation end products and their receptors in rat leukocytes under experimental diabetes mellitus". Studia Biologica 15, nr 4 (grudzień 2021): 49–58. http://dx.doi.org/10.30970/sbi.1504.672.
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Background. Diabetes mellitus intensifies non-enzymatic glycosylation (glycation) of biomolecules under conditions of chronic hyperglycemia and facilitates accumulation of advanced glycation end products. Disorders of the cells of various tissues are caused by binding of advanced glycation end products to the corresponding receptors, the level of receptors for advanced glycation end products increases under conditions of hyperglycemia. The interaction between receptors for advanced glycation end products and advanced glycation end products leads to the formation of excessive reactive oxygen species, changes in intracellular signaling, gene expression, increased secretion of pro-inflammatory cytokines and contributes to the development of diabetic complications. The search for factors of natural origin that will slow down the development of specific complications of diabetes, determines the feasibility of studies of the corrective ability of biologically active substances isolated from medicinal plants for the process of glycation of proteins in diabetes. Materials and methods. Experimental diabetes mellitus was induced by intraperitoneal administration of streptozotocin. Separation of blood leukocytes was performed in Ficoll density gradient. To determine the extent of advanced glycation end products and receptor for advanced glycation end products in leukocyte immunoperoxidase labeling was performed. Results. A decrease in the content of advanced glycation end products in leukocytes under conditions of experimental diabetes mellitus was found. The obtained data indicate a possible contravention of glucose uptake by leukocytes in the studied pathology. At the same time, an increase in exposure to the receptor for advanced glycation end products leukocyte membranes in response to chronic hyperglycemia has been demonstrated. The ability of alkaloid free fraction of Galega officinalis extract to reduce the content of receptors for end products of glycation on the membranes of immunocompetent cells in diabetic animals has been confirmed, which may be due to the presence of biologically active substances with hypoglycemic action in its composition. Conclusion. Corrective effect of alkaloid free fraction of Galega officinalis L. extract on the content of receptor for advanced glycation end products in diabetes mellitus is mediated by its normalizing effect on carbohydrate metabolism.
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Ahmad, Saheem, Sultan Alouffi, Saif Khan, Mahvish Khan, Rihab Akasha, Jalaluddin Mohammad Ashraf, Mohd Farhan, Uzma Shahab i Mohd Yasir Khan. "Physicochemical Characterization of In Vitro LDL Glycation and Its Inhibition by Ellagic Acid (EA): An In Vivo Approach to Inhibit Diabetes in Experimental Animals". BioMed Research International 2022 (19.01.2022): 1–15. http://dx.doi.org/10.1155/2022/5583298.
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Hundreds of millions of people around the globe are afflicted by diabetes mellitus. The alteration in glucose fixation process might result into hyperglycaemia and could affect the circulating plasma proteins to undergo nonenzymatic glycation reaction. If it is unchecked, it may lead to diabetes with increase in advanced glycation end products (AGEs). Therefore, the present study was designed to inhibit the diabetes and glycation by using natural antioxidant “ellagic acid” (EA). In this study, we explored the antidiabetes and antiglycation potential of EA in both in vitro (EA at micromolar concentration) and in vivo systems. The EA concentrations of 10 and 20 mg kg-1B.W./day were administered orally for 25 days to alloxan-induced diabetic rats, a week after confirmation of stable diabetes in animals. Intriguingly, EA supplementation in diabetic rats reversed the increase in fasting blood sugar (FBS) and hemoglobin A1c (HbA1c) level. EA also showed an inhibitory role against glycation intermediates including dicarbonyls, as well as AGEs, investigated in a glycation mixture with in vitro and in vivo animal plasma samples. Additionally, EA treatment resulted in inhibition of lipid peroxidation-mediated malondialdehyde (MDA) and conjugated dienes (CD). Furthermore, EA exhibited an antioxidant property, increased the level of plasma glutathione (GSH), and also helped to decrease histological changes evaluated by histoimmunostaining of animal kidney tissues. The results from our investigation clearly indicates the antiglycative property of EA, suggesting EA as an adequate inhibitor of glycation and diabetes, which can be investigated further in preclinical settings for the treatment and management of diabetes-associated complications.
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Ahmad, Saheem, Mohd Sajid Khan, Sultan Alouffi, Saif Khan, Mahvish Khan, Rihab Akashah, Mohammad Faisal i Uzma Shahab. "Gold Nanoparticle-Bioconjugated Aminoguanidine Inhibits Glycation Reaction: An In Vivo Study in a Diabetic Animal Model". BioMed Research International 2021 (13.05.2021): 1–10. http://dx.doi.org/10.1155/2021/5591851.
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Proteins undergo glycation resulting in the generation of advanced glycation end products (AGEs) that play a central role in the onset and advancement of diabetes-associated secondary complications. Aminoguanidine (AG) acts as an antiglycating agent by inhibiting AGE generation by blocking reactive carbonyl species (RCS) like, methylglyoxal (MGO). Previous studies on antiglycating behavior of AG gave promising results in the treatment of diabetes-associated microvascular complications, but it was discontinued as it was found to be toxic at high concentrations (>10 mmol/L). The current article aims at glycation inhibition by conjugating gold nanoparticles (Gnp) with less concentration of AG (0.5-1.0 mmol/L). The HPLC results showed that AG-Gnp fairly hampers the formation of glycation adducts. Moreover, the in vivo studies revealed AG-Gnp mediated inhibition in the production of total-AGEs and - N ε -(carboxymethyl)lysine (CML) in the diabetic rat model. This inhibition was found to be directly correlated with the antioxidant parameters, blood glucose, insulin, and glycosylated hemoglobin levels. Furthermore, the histopathology of AG-Gnp-treated rats showed good recovery in the damaged pancreatic tissue as compared to diabetic rats. We propose that this approach might increase the efficacy of AG at relatively low concentrations to avoid toxicity and might facilitate to overcome the hazardous actions of antiglycating drugs.
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Kuchurka, О. М., М. O. Chaban, O. V. Dzydzan, I. V. Brodyak i N. O. Sybirna. "Leukocytes in type 1 diabetes mellitus: the changes they undergo and induce". Studia Biologica 16, nr 1 (11.04.2022): 47–66. http://dx.doi.org/10.30970/sbi.1601.674.
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As leukocytes represent cellular and humoral immunity at the same time, they are a vital part of every immune process. This also stands for autoimmune processes and disorders, such as diabetes, specifically type 1 diabetes mellitus. Diabetes mellitus is one of the most widespread autoimmune diseases. Development of type 1 diabetes mellitus is mediated through complicated mechanisms of intercellular communication where leukocytes function as the key element, being both effectors and regulators. However, the immunocompetent cells are also affected by diabetic alterations, powered by chronic hyperglycemia. For example, the products of non-enzymatic interaction of glucose or other reducing sugars with either proteins or lipids, called advanced glycation end products, are associated with the development of long-term negative changes in diabetes. By binding to the receptors for advanced glycation end-products, they trigger the signaling pathways involved in expression of pro-inflammatory genes, which results in diabetic complications. As long as diabetes mellitus remains a global healthcare issue and several details of its pathogenesis are still to be discovered, it is important to analyze and investigate the peculiarities of alterations in leukocytes under type 1 diabetes mellitus, particularly the ones caused by advanced glycation end-products and their receptors.
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Ramesh, Pranav, Jian L. Yeo, Emer M. Brady i Gerry P. McCann. "Role of inflammation in diabetic cardiomyopathy". Therapeutic Advances in Endocrinology and Metabolism 13 (styczeń 2022): 204201882210835. http://dx.doi.org/10.1177/20420188221083530.
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The prevalence of type 2 diabetes (T2D) has reached a pandemic scale. Systemic chronic inflammation dominates the diabetes pathophysiology and has been implicated as a causal factor for the development of vascular complications. Heart failure (HF) is regarded as the most common cardiovascular complication of T2D and the diabetic diagnosis is an independent risk factor for HF development. Key molecular mechanisms pivotal to the development of diabetic cardiomyopathy include the NF-κB pathway and renin–angiotensin–aldosterone system, in addition to advanced glycation end product accumulation and inflammatory interleukin overexpression. Chronic myocardial inflammation in T2D mediates structural and metabolic changes, including cardiomyocyte apoptosis, impaired calcium handling, myocardial hypertrophy and fibrosis, all of which contribute to the diabetic HF phenotype. Advanced cardiovascular magnetic resonance imaging (CMR) has emerged as a gold standard non-invasive tool to delineate myocardial structural and functional changes. This review explores the role of chronic inflammation in diabetic cardiomyopathy and the ability of CMR to identify inflammation-mediated myocardial sequelae, such as oedema and diffuse fibrosis.
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Muthenna, P., C. Akileshwari, Megha Saraswat i G. Bhanuprakash Reddy. "Inhibition of advanced glycation end-product formation on eye lens protein by rutin". British Journal of Nutrition 107, nr 7 (25.08.2011): 941–49. http://dx.doi.org/10.1017/s0007114511004077.
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Formation of advanced glycation end products (AGE) plays a key role in the several pathophysiologies associated with ageing and diabetes, such as arthritis, atherosclerosis, chronic renal insufficiency, Alzheimer's disease, nephropathy, neuropathy and cataract. This raises the possibility of inhibition of AGE formation as one of the approaches to prevent or arrest the progression of diabetic complications. Previously, we have reported that some common dietary sources such as fruits, vegetables, herbs and spices have the potential to inhibit AGE formation. Flavonoids are abundantly found in fruits, vegetables, herbs and spices, and rutin is one of the commonly found dietary flavonols. In the present study, we have demonstrated the antiglycating potential and mechanism of action of rutin using goat eye lens proteins as model proteins. Under in vitro conditions, rutin inhibited glycation as assessed by SDS-PAGE, AGE-fluorescence, boronate affinity chromatography and immunodetection of specific AGE. Further, we provided insight into the mechanism of inhibition of protein glycation that rutin not only scavenges free-radicals directly but also chelates the metal ions by forming complexes with them and thereby partly inhibiting post-Amadori formation. These findings indicate the potential of rutin to prevent and/or inhibit protein glycation and the prospects for controlling AGE-mediated diabetic pathological conditions in vivo.
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Thornalley, P. J., A. C. McLellan, T. W. C. Lo, J. Benn i P. H. Sönksen. "Negative Association between Erythrocyte Reduced Glutathione Concentration and Diabetic Complications". Clinical Science 91, nr 5 (1.11.1996): 575–82. http://dx.doi.org/10.1042/cs0910575.
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1. Multiple logistic regression analysis of biochemical and clinical variables in diabetic patients was performed to identify those associated with the presence of diabetic complications (retinopathy, neuropathy and nephropathy). 2. The presence of diabetic complications correlated positively with duration of diabetes and patient age and negatively with the concentration of reduced glutathione in erythrocytes. Individually, retinopathy, neuropathy and nephropathy correlated with duration of diabetes, but retinopathy also correlated positively with haemoglobin A1c in diabetic patients. In insulin-dependent patients, the concentration of methylglyoxal was also in the logistic model for retinopathy and diabetic complications, but the logistic regression coefficient was not significant. 3. Multiple linear regression analysis indicated that erythrocyte reduced glutathione concentration correlated negatively with d-lactate concentration and positively with duration of diabetes in insulin-dependent patients and correlated negatively with glucose concentration in non-insulin-dependent diabetic patients. 4. In non-diabetic subjects, erythrocyte glyoxalase I activity correlated positively with methylglyoxal concentration. There was no similar correlation in diabetic patients. In insulin-dependent patients, methylglyoxal concentration correlated positively with duration of diabetes. 5. Glyoxal and methylglyoxal are detoxified by the glyoxalase system with reduced glutathione as co-factor. The concentration of reduced glutathione may be decreased by oxidative stress and by decreased in situ glutathione reductase activity in diabetes mellitus. A reduced concentration of reduced glutathione may predispose diabetic patients to oxidative damage and to α-oxoaldehyde-mediated glycation by decreasing the in situ glyoxalase I activity. Recent studies of vascular endothelial cells in vitro have suggested that α-oxoaldehydes detoxified by glyoxalase I are the major precursors of advanced glycation end products implicated in the development of diabetic complications. The role of these factors in the development of diabetic complications and the prospective prevention of diabetic complications by supplementation of reduced glutathione and/or α-oxoaldehyde-scavenging agents now deserve investigation.
Rozprawy doktorskie na temat "Glycation mediated diabetic"
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Al-Turkistani, Abdul Rasheed. "Low densitiy lipoprotein glycation mediated modifications in diabetic atherosclerosis". Thesis, University of Leicester, 1999. http://hdl.handle.net/2381/29590.
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Evidence suggests a role for glycation and glycoxidative changes in damaged tissues and plasma components. LDL modified as a result of glucoxidation stress, is potentially atherogenic, and is implicated in the accelerated atherosclerosis associated with diabetic complications. The purpose of this thesis is to investigate and establish the importance of glycoxidative changes to LDL and its role in the chemical complications associated with diabetes. LDL was chemically modified in vitro with glyoxal (dicarbonyl aldehyde) to produce a crosslinked structure (glyoxalated) LDL. The complex produced (glyoxalated LDL) was used for the production of specific antibodies. Anti-glyoxalated LDL antibody was employed in specific and sensitive ELISA assays to measure the levels of glyoxalated LDL in human plasma. Levels of glyoxalated LDL measured in diabetics were generally up to 20% higher (n = 182, P <0.001) when compared to non-diabetics, reference and hyperlipidemic groups. An anti-glyoxalated LDL autoantibody ELISA assay was developed to assess the immunological importance of glyoxalated LDL and similar crosslinked structures in human plasma. Diabetics with poor glycaemic control demonstrated a 22% increase in anti-glyoxalated LDL autoantibodies (n = 39, P <0.0001) compared to reference groups, where less than a 3% increase was detected in hyperlipidemic non-diabetic subjects (n = 33, P <0.08). Unlike glycated haemoglobin, no significant age relationship was detected. Although glyoxal is a common product of glucose and lipoprotein autoxidation, levels of glyoxalated LDL and anti-glyoxalated LDL autoantibodies measured in diabetics, hyperlipidemic and reference groups, suggest a direct relationship between hyperglycaemia and the presence of glyoxal mediated crosslinks on human LDL. Glyoxalated LDL measured with these specific immunochemical assays may predict the possible complications associated with diabetes better than glycated haemoglobin because it appears not to have a direct relationship with age at high concentrations observed in diabetics.
Części książek na temat "Glycation mediated diabetic"
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Nakamura, Akio, i Ritsuko Kawahrada. "Advanced Glycation End Products and Oxidative Stress in a Hyperglycaemic Environment". W Fundamentals of Glycosylation [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97234.
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Protein glycation is the random, nonenzymatic reaction of sugar and protein induced by diabetes and ageing; this process is quite different from glycosylation mediated by the enzymatic reactions catalysed by glycosyltransferases. Schiff bases form advanced glycation end products (AGEs) via intermediates, such as Amadori compounds. Although these AGEs form various molecular species, only a few of their structures have been determined. AGEs bind to different AGE receptors on the cell membrane and transmit signals to the cell. Signal transduction via the receptor of AGEs produces reactive oxygen species in cells, and oxidative stress is responsible for the onset of diabetic complications. This chapter introduces the molecular mechanisms of disease onset due to oxidative stress, including reactive oxygen species, caused by AGEs generated by protein glycation in a hyperglycaemic environment.
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Khan, Rujman, Xin Yee Ooi, Matthew Parvus, Laura Valdez i Andrew Tsin. "Advanced Glycation End Products: Formation, Role in Diabetic Complications, and Potential in Clinical Applications". W The Eye and Foot in Diabetes. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.89408.
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Hyperglycemic conditions and disruptions to glucose-regulating pathways lead to increased formation of highly reactive aldehydes, methylglyoxal and glyoxal, which react with certain arginine and lysine residues in proteins to form advanced glycation end products (AGEs). These AGEs damage the integrity of the retinal vasculature predominantly through two mechanisms: non-receptor-mediated damage, which pertains to the interaction with extracellular matrix and its functional properties, and receptor-mediated damage through AGE interactions with their receptors (RAGE) on pericytes and Muller cells. Damage occurring between AGE and RAGE potentially generates reactive oxygen species, inflammatory cytokines, and growth factors. Both mechanisms result in increased permeability of endothelial tight junctions, and this increased permeability can lead to leaking and eventually ischemia. Once this ischemia becomes significant, neovascularization can occur, the hallmark of proliferative diabetic retinopathy. Current pharmaceutical studies have shown the potential of AGE inhibitors, such as aminoguanidine, in decreasing AGE production, thus minimizing its effects in hyperglycemic conditions. Other pharmaceutical interventions, such as Tanshinone IIA, aim to protect cells from the impacts of AGEs. Future research will not only continue to understand the properties of AGEs and their effects on diabetes and diabetic complications like diabetic retinopathy but will also explore how they impact other diseases.
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Ravi, Ramya, i Bharathidevi Subramaniam Rajesh. "Advanced glycation end product induced endothelial dysfunction through ER stress: Unravelling the role of Paraoxonase 2". W Updates on Endoplasmic Reticulum [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.106018.
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Hyperglycemia accelerates the formation of advanced glycation end products (AGEs). AGEs are a heterogeneous group of compounds generated by non-enzymatic glycation of proteins or lipids with glucose through Amadori rearrangement and its accumulation increases with aging in diabetes. AGEs augments ROS generation, diminishes the antioxidant defense of the cells, decreases mitochondrial membrane potential, ATP production, and elevates the levels of mitochondrial fission protein (Drp1) and mitophagic proteins (Parkin and PTEN) leading to dysfunction of mitochondria. In this chapter, we have discussed how AGEs trigger the endoplasmic reticulum stress and inflammation and mediate endothelial dysfunction in diabetes and also have discussed the role played by endogenous Paraoxonase 2 (PON2) in mitigating endothelial dysfunction by inhibiting the adverse effects of AGE.