scholarly journals Glyceraldehyde-Derived Advanced Glycation End Products Accumulate Faster Than Nε-(Carboxymethyl) Lysine

2017 ◽  
Vol 29 (4) ◽  
pp. 508
Author(s):  
Mami Yokota ◽  
Marie Sekita ◽  
Yuri Okano ◽  
Hitoshi Masaki ◽  
Masayoshi Takeuchi ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Carboxymethyl Lysine

Advanced glycation end-products associate with podocytopathy in type II diabetic patients

2021 ◽  
Author(s):  
Rajkishor Nishad ◽  
Tahaseen V Syed ◽  
Manga Motrapu ◽  
Rajesh Kavvuri ◽  
Kiranmayi Kodali ◽  
...  
Keyword(s):  
Kidney Disease ◽  
Kidney Function ◽  
Advanced Glycation End Products ◽  
Diabetic Patients ◽  
Type Ii ◽  
Advanced Glycation ◽  
Mesenchymal Transition ◽  
Glycation End Products ◽  
End Products ◽  
Carboxymethyl Lysine

Abstract Background The prevalence of diabetes reaches epidemic proportions, affecting the incidence of diabetic nephropathy (DN) and associated end-stage kidney disease (ESKD). Diabetes is the leading cause of ESKD since 30–40% of diabetic patients develop DN. Albuminuria and eGFR have been considered a surrogate outcome of chronic kidney disease, and the search for a biomarker that predicts progression to diabetic kidney disease is intense.Methods We analyzed the association of serum advanced glycation end-products (AGEs) index (AGI) with impaired kidney function in uncontrolled diabetic patients (type II, n = 130) with albuminuria ranging from (150 to 450 mg/day). The kidney biopsy specimens were also examined for the association of AGEs, particularly carboxymethyl lysine (CML) with kidney function. Further, we also assessed the effect of carboxymethyl lysine on glomerular injury and podocytopathy in experimental animals.Results We observed a strong correlation between AGI and impaired kidney function in miroalbuminuric patients with hyperglycemia. A significant association between CML levels and impaired kidney function was noticed. Administration of CML in mice showed heavy proteinuria and glomerular abnormalities. Reduced podocyte number observed in mice administered with CML could be attributed to the epithelial-mesenchymal transition (EMT) of podocytes. Conclusion Serum AGEs could be independently related to the podocyte injury vis-a-vis the risk of DN progression to ESKD in patients with microalbuminuria. AGEs or CML could be considered a prognostic marker to assess microalbuminuria progression to ESKD in diabetic patients.

Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats

2003 ◽  
Vol 31 (6) ◽  
pp. 1423-1425 ◽  
Author(s):  
N. Karachalias ◽  
R. Babaei-Jadidi ◽  
N. Ahmed ◽  
P.J. Thornalley
Keyword(s):  
Peripheral Neuropathy ◽  
Sciatic Nerve ◽  
Peripheral Nerve ◽  
Plasma Protein ◽  
Advanced Glycation End Products ◽  
Diabetic Rats ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Carboxymethyl Lysine

The accumulation of AGEs (advanced glycation end products) in diabetes mellitus has been implicated in the biochemical dysfunction associated with the chronic development of microvascular complications of diabetes – nephropathy, retinopathy and peripheral neuropathy. We investigated the concentrations of fructosyl-lysine and AGE residues in protein extracts of renal glomeruli, retina, peripheral nerve and plasma protein of streptozotocin-induced diabetic rats and normal healthy controls. Glycation adducts were determined by LC with tandem MS detection. In diabetic rats, the fructosyl-lysine concentration was increased markedly in glomeruli, retina, sciatic nerve and plasma protein. The concentrations of N∊-carboxymethyl-lysine and N∊-carboxyethyl-lysine were increased in glomeruli, sciatic nerve and plasma protein, and N∊-carboxymethyl-lysine also in the retina. Hydroimidazolone AGEs derived from glyoxal, methylglyoxal and 3-deoxylglucosone were major AGEs quantitatively. They were increased in the retina, nerve, glomeruli and plasma protein. AGE accumulation in renal glomeruli, retina, peripheral nerve and plasma proteins is consistent with a role for AGEs in the development of nephropathy, retinopathy and peripheral neuropathy in diabetes. High-dose therapy with thiamine and Benfotiamine suppressed the accumulation of AGEs, and is a novel approach to preventing the development of diabetic complications.

scholarly journals N ε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins

1997 ◽  
Vol 324 (2) ◽  
pp. 565-570 ◽  
Author(s):  
Mahtab U. AHMED ◽  
Elisabeth BRINKMANN FRYE ◽  
Thorsten P. DEGENHARDT ◽  
Suzanne R. THORPE ◽  
John W. BAYNES
Keyword(s):  
Advanced Glycation End Products ◽  
Human Lens ◽  
Advanced Glycation ◽  
Model Compounds ◽  
Lens Proteins ◽  
Glycation End Products ◽  
End Products ◽  
Lysine Residues ◽  
Carboxymethyl Lysine ◽  
Chemical Modification Of Proteins

Advanced glycation end-products and glycoxidation products, such as Nϵ-(carboxymethyl)lysine (CML) and pentosidine, accumulate in long-lived tissue proteins with age and are implicated in the aging of tissue proteins and in the development of pathology in diabetes, atherosclerosis and other diseases. In this paper we describe a new advanced glycation end-product, Nϵ-(carboxyethyl)lysine (CEL), which is formed during the reaction of methylglyoxal with lysine residues in model compounds and in the proteins RNase and collagen. CEL was also detected in human lens proteins at a concentration similar to that of CML, and increased with age in parallel with the concentration of CML. Although CEL was formed in highest yields during the reaction of methylglyoxal and triose phosphates with lysine and protein, it was also formed in reactions of pentoses, ascorbate and other sugars with lysine and RNase. We propose that levels of CML and CEL and their ratio to one another in tissue proteins and in urine will provide an index of glyoxal and methylglyoxal concentrations in tissues, alterations in glutathione homoeostasis and dicarbonyl metabolism in disease, and sources of advanced glycation end-products in tissue proteins in aging and disease.

scholarly journals Leptin and advanced glycation end products receptor (RAGE) in tuberculosis patients

PLoS ONE ◽  
2021 ◽  
Vol 16 (7) ◽  
pp. e0254198
Author(s):  
Tássia Kirchmann Lazzari ◽  
Erika Cavalheiro ◽  
Sandra Eugênia Coutinho ◽  
Lívia Fontes da Silva ◽  
Denise Rossato Silva
Keyword(s):  
Weight Loss ◽  
Advanced Glycation End Products ◽  
Inverse Correlation ◽  
Advanced Glycation ◽  
Serum Leptin ◽  
Soluble Rage ◽  
Glycation End Products ◽  
End Products ◽  
Carboxymethyl Lysine ◽  
Control Study

Introduction The pathogenesis of consumptive syndrome of tuberculosis (TB) is largely unknown. Leptin concentrations may be high because of the host’s inflammatory response, contributing to weight loss in patients with TB. The receptor for advanced glycation end products (RAGE) is also associated with weight loss in patients with TB and is related to enhanced mortality. The objective of this study was to evaluate the association between leptin and AGE/RAGE. Methods Case-control study. Leptin, AGE (carboxymethyl lysine, CML) and soluble RAGE (sRAGE) were measured from blood samples by ELISA. Results We included in the study 34 patients with TB and 34 controls. We found an inverse correlation between serum leptin levels and sRAGE, only in cases (r = -0.609, p < 0.0001). sRAGE levels were lower in patients with TB who died as compared with patients who survive (21.90 ± 4.24 pg/mL vs 66.14 ± 29.49 pg/mL; p = 0.045). Leptin levels were higher in patients with TB who died as compared with patients who survive (14.11 [7.48–14.11] ng/mL vs 3.08 [0.54–6.34] ng/mL; p = 0.028). Conclusions We identified lower sRAGE levels and higher leptin levels in patients with TB who died as compared with patients who survive. In addition, an inverse and significant correlation between serum leptin and sRAGE levels was demonstrated. Future studies, with a larger sample size and in different settings, including not only hospitalized patients, are needed to confirm these findings.

Frequency of Autoantibodies Against 3-Deoxyglucosone H1 Protein in Type 2 Diabetes

2020 ◽  
Vol 8 (3) ◽  
pp. 135-143
Author(s):  
Jalaluddin M. ASHRAF ◽  
Shahnawaz REHMAN
Keyword(s):  
Advanced Glycation End Products ◽  
Autoimmune Response ◽  
Diabetic Patients ◽  
Advanced Glycation ◽  
Contributing Factors ◽  
Strong Binding ◽  
Glycation End Products ◽  
End Products ◽  
Carboxymethyl Lysine

Introduction: Advanced glycation end-products (AGEs) are contributing factors to diabetes complications. The antigenic nature of AGEs established the theory of incessant accumulation of AGEs can incite an autoimmune response in a diabetic patient. Glycating agents like 3-deoxyglucosone are increased in diabetic patients, leading to the high formation of AGEs aggravating the pathophysiological conditions in diabetes. We aimed to study the immunogenicity of glycated histone H1 protein and AGEs (N-carboxymethyl-lysine and pentosidine) as well as detection of autoantibodies in the sera of type 2 diabetic subjects. Materials and Methods: Female rabbits were injected with native H1 and glycated-H1 to discern its immunogenicity. Diabetic subjects’ sera were also scanned for the detection of autoantibodies against glycated-H1 and AGEs using immunochemical assay technique. Results: Glycated-H1 was highly immunogenic, unlike the native analog. Diabetic sera showed 48% (72 of 150 samples) significantly strong binding with glycated-H1, further sera also showed 40% (60 of 150 samples), and 36% (54 of 150 samples) strong binding with CML, and pentosidine, respectively. Conclusion: The findings support modified H1 as well AGEs are highly immunogenic in nature. The presence of autoantibodies against glycated-H1 and AGEs may be utilized in the assessment of diabetes or its complications. Keywords: immunogenicity, 3-deoxyglucosone, advanced glycation end-products, diabetes

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