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Alterations in nonenzymatic biochemistry in uremia: Origin and significance of “carbonyl stress” in long-term uremic complications

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TLDR
Uremia may be described as a state of carbonyl overload or "carbonyl stress" resulting from either increased oxidation of carbohydrates and lipids (oxidative stress) or inadequate detoxification or inactivation of reactive carbonyL compounds derived from both carbohydrates andlipids by oxidative and nonoxidatives.
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This article is published in Kidney International.The article was published on 1999-02-01 and is currently open access. It has received 518 citations till now. The article focuses on the topics: Pentosidine & Uremia.

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Mechanisms, Pathophysiology, and Therapy of Arterial Stiffness

TL;DR: A number of lifestyle changes and therapies that reduce arterial stiffness are presented, including weight loss, exercise, salt reduction, alcohol consumption, and neuroendocrine-directed therapies, such as those targeting the renin-angiotensin aldosterone system, natriuretic peptides, insulin modulators, as well as novel therapies that target advanced glycation end products.
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Endothelial dysfunction in diabetes

TL;DR: Correcting the principal mediators of hyperglycaemia‐induced endothelial dysfunction may be activation of protein kinase C, increased activity of the polyol pathway, non‐enzymatic glycation and oxidative stress, as well as administration of ACE inhibitors and folate has been shown to improve endothelium‐dependent vasodilation in diabetes.
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The elephant in uremia: Oxidant stress as a unifying concept of cardiovascular disease in uremia

TL;DR: The hypothesis that increased oxidative stress and its sequalae is a major contributor to increased atherosclerosis and cardiovascular morbidity and mortality found in uremia is proposed and it is proposed that retained uremic solutes such as beta-2 microglobulin, advanced glycosylated end products, cysteine, and homocysteine further contribute to the pro-atherogenic milieu of Uremia.
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Protein carbonylation in human diseases.

TL;DR: Rapid recent progress in the identification of carbonylated proteins should provide new diagnostic (possibly pre-symptomatic) biomarkers for oxidative damage, and yield basic information to aid the establishment an efficacious antioxidant therapy.
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N ε-(Carboxymethyl)Lysine Adducts of Proteins Are Ligands for Receptor for Advanced Glycation End Products That Activate Cell Signaling Pathways and Modulate Gene Expression

TL;DR: It is demonstrated here that physiologically relevant CML modifications of proteins engage cellular RAGE, thereby activating key cell signaling pathways such as NF-κB and modulating gene expression, and triggers processes intimately linked to accelerated vascular and inflammatory complications that typify disorders in which inflammation is an established component.
References
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Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes.

TL;DR: This review provides a comprehensive summary on the chemical properties of 4-hydroxyalkenals and malonaldehyde, the mechanisms of their formation and their occurrence in biological systems and methods for their determination, as well as the many types of biological activities described so far.
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Role of Oxidative Stress in Development of Complications in Diabetes

TL;DR: Structural characterization of the cross-links and other products accumulating in collagen in diabetes is needed to gain a better understanding of the relationship between oxidative stress and the development of complications in diabetes.
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Protein oxidation and aging

TL;DR: The importance of protein oxidation in aging is supported by the observation that levels of oxidized proteins increase with animal age and may reflect age-related increases in rates of ROS generation, decreases in antioxidant activities, or losses in the capacity to degrade oxidized protein.
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Advanced oxidation protein products as a novel marker of oxidative stress in uremia

TL;DR: The measurement of AOPP is proposed as a reliable marker to estimate the degree of oxidant-mediated protein damage in uremic patients and to predict the potential efficacy of therapeutic strategies aimed at reducing such an oxidative stress.
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Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins.

TL;DR: RAGE is a new member of the immunoglobulin superfamily of cell surface molecules and shares significant homology with MUC 18, NCAM, and the cytoplasmic domain of CD20 and could potentially mediate cellular effects of this class of glycosylated proteins.
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