Results 41 to 50 of about 37,721 (216)

Skin advanced glycation end-products evaluation in infants according to the type of feeding and mother’s smoking habits

open access: yesSAGE Open Medicine, 2016
Objectives: This study was conducted to assess whether formula-fed infants had increased skin advanced glycation end-products compared with breastfed ones.
Giovanni Federico   +3 more
doaj   +1 more source

Increased concentration of two different advanced glycation end-products detected by enzyme immunoassays with new monoclonal antibodies in sera of patients with rheumatoid arthritis

open access: yesBMC Musculoskeletal Disorders, 2010
Background Levels of pentosidine (representative of advanced glycation end-products) in sera of patients with rheumatoid arthritis are increased when compared with sera of other diagnoses or healthy controls.
Vilím Vladimír   +2 more
doaj   +1 more source

Diphlorethohydroxycarmalol Attenuates Methylglyoxal-Induced Oxidative Stress and Advanced Glycation End Product Formation in Human Kidney Cells

open access: yesOxidative Medicine and Cellular Longevity, 2018
Diabetic nephropathy is the leading cause of end-stage renal disease in patients with diabetes mellitus. Oxidative stress has been shown to play an important role in pathogeneses of renal damage in diabetic patients.
Seon-Heui Cha   +3 more
semanticscholar   +1 more source

Toxicity of advanced glycation end products (Review)

open access: yesBiomedical Reports, 2021
Advanced glycation end-products (AGEs) are proteins or lipids glycated nonenzymatically by glucose, or other reducing sugars and their derivatives, such as glyceraldehyde, glycolaldehyde, methyloglyoxal and acetaldehyde. There are three different means of AGE formation: i) Maillard reactions, the polyol pathway and lipid peroxidation.
openaire   +5 more sources

The Advanced Glycation End Product, N-(Carboxymethyl)lysine, Is a Product of both Lipid Peroxidation and Glycoxidation Reactions (*)

open access: yesJournal of Biological Chemistry, 1996
N-(Carboxymethyl)lysine (CML) is an advanced glycation end product formed on protein by combined nonenzymatic glycation and oxidation (glycoxidation) reactions.
M. Fu   +5 more
semanticscholar   +1 more source

Role of Hyperglycemia-Induced Advanced Glycation End Product (AGE) Accumulation in Atherosclerosis

open access: yesAnnals of Vascular Diseases, 2018
There is a growing body of evidence that cumulative hyperglycemic exposure plays a central role in the development and progression of atherosclerotic cardiovascular disease in diabetic patients.
S. Yamagishi, T. Matsui
semanticscholar   +1 more source

Polymorphisms of the receptor for advanced glycation end products and glyoxalase I and long-term outcome in patients with breast cancer

open access: yesTumor Biology, 2017
Receptor for advanced glycation end products and glyoxalase I metabolizing advanced glycation end product precursors may play important role in the pathogenesis and progression of cancer.
Petra Tesarova   +3 more
doaj   +1 more source

Activation of NLRP3 Inflammasome Promotes Foam Cell Formation in Vascular Smooth Muscle Cells and Atherogenesis Via HMGB1

open access: yesJournal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2018
Background This study aimed at investigating whether NLRP3 (the Nod like receptor family, pyrin domain‐containing 3 protein) inflammasome activation induced HMGB1 (high mobility group box‐1 protein) secretion and foam cell formation in human vascular ...
Rui Wang   +9 more
doaj   +1 more source

Advanced glycation end (AGE) product modification of laminin downregulates Kir4.1 in retinal Müller cells. [PDF]

open access: yesPLoS ONE, 2018
Diabetic retinopathy (DR) is a major cause of adult blindness. Retinal Müller cells maintain water homeostasis and potassium concentration via inwardly rectifying Kir4.1 channels.
Kayla Thompson   +5 more
doaj   +1 more source

Mdia1 is Crucial for Advanced Glycation End Product-Induced Endothelial Hyperpermeability

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: Disruption of endothelial barrier integrity in response to advanced glycation end products (AEGs) stimulation contributes to vasculopathy associated with diabetes mellitus. Mammalian diaphanous-related formin (mDia1) has been reported to
Xiaoyan Zhou   +7 more
doaj   +1 more source

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