scholarly journals Role of advanced glycation end products (AGEs) and its receptor (RAGE)-mediated diabetic vascular complications

2019 ◽  
Vol 6 (5) ◽  
Author(s):  
Diwesh Chawla ◽  
Ashok Kumar Tripathi
Keyword(s):  
Advanced Glycation End Products ◽  
Vascular Complications ◽  
Advanced Glycation ◽  
Diabetic Vascular Complications ◽  
Glycation End Products ◽  
End Products

Role of methylglyoxal adducts in the development of vascular complications in diabetes mellitus

2003 ◽  
Vol 31 (6) ◽  
pp. 1400-1402 ◽  
Author(s):  
M. Bourajjaj ◽  
C.D.A. Stehouwer ◽  
V.W.M. van Hinsbergh ◽  
C.G. Schalkwijk
Keyword(s):  
Diabetes Mellitus ◽  
Advanced Glycation End Products ◽  
Vascular Complications ◽  
Advanced Glycation ◽  
Exact Role ◽  
Dicarbonyl Compound ◽  
Diabetic Vascular Complications ◽  
Glycation End Products ◽  
End Products

Various theories have been proposed to explain the hyperglycaemia-induced pathogenesis of vascular complications of diabetes, including detrimental effects of AGEs (advanced glycation end products) on vascular tissues. Increased formation of the very reactive dicarbonyl compound MGO (methylglyoxal), one of the side-products of glycolysis, and MGO-derived AGEs seem to be implicated in the development of diabetic vascular complications. Although the exact role of MGO and MGO adducts in the development of vascular complications is unknown, receptor-mediated activation of vascular cells by the MGO–arginine adduct hydroimidazolone, as well as intracellular modifications of protein by MGO, seem to be involved. The aim of this mini-review is to assess to what extent MGO is related to vascular complications in diabetes.

Elevated endogenous secretory receptor for advanced glycation end products (esRAGE) levels are associated with circulating soluble RAGE levels in diabetic children

2017 ◽  
Vol 30 (1) ◽  
Author(s):  
Reiko Saito ◽  
Shunsuke Araki ◽  
Yukiyo Yamamoto ◽  
Koichi Kusuhara
Keyword(s):  
Advanced Glycation End Products ◽  
Vascular Complications ◽  
Soluble Form ◽  
Advanced Glycation ◽  
Diabetic Vascular Complications ◽  
Soluble Rage ◽  
Control Serum ◽  
Glycation End Products ◽  
End Products ◽  
Diabetic Children

AbstractBackground:Advanced glycation end products (AGEs) and the receptor for AGE (RAGE) play an important role in the development of diabetic vascular complications. This study aimed at investigating the relationship between the soluble form of RAGE (sRAGE), endogenous secretory RAGE (esRAGE), and pentosidine in childhood diabetes.Methods:The study included 18 children with type 1 diabetes mellitus (T1DM), 10 with type 2 DM (T2DM), and 22 age-matched, non-diabetic children (control).Results:Serum sRAGE levels in the T1DM (2557.7 pg/mL) were significantly higher than both T2DM (1956.4 pg/mL) and control (1658.5 pg/mL). The circulating levels of esRAGE in T1DM and T2DM children were similar, but significantly higher than those of control. Serum pentosidine levels in the T1DM group were positively correlated with serum sRAGE and esRAGE levels, but not with anthropometric or biochemical measurements. The duration of diabetes and esRAGE levels were independent predictors of the circulating sRAGE levels.Conclusions:Unlike adults, children with diabetes exhibit high circulating esRAGE levels, and both sRAGE and esRAGE levels are correlated with pentosidine levels. These results suggest that circulating sRAGE and esRAGE in children may be surrogate markers for progressive glucose toxicity in pediatric patients with childhood-onset diabetes.

scholarly journals Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury

2003 ◽  
Vol 370 (3) ◽  
pp. 1097-1109 ◽  
Author(s):  
Hideto YONEKURA ◽  
Yasuhiko YAMAMOTO ◽  
Shigeru SAKURAI ◽  
Ralica G. PETROVA ◽  
Md. Joynal ABEDIN ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Advanced Glycation End Products ◽  
Splice Variants ◽  
Vascular Complications ◽  
Full Length ◽  
Vascular Endothelial ◽  
Advanced Glycation ◽  
Diabetic Vascular Complications ◽  
Glycation End Products ◽  
End Products

The binding of advanced glycation end-products (AGE) to the receptor for AGE (RAGE) is known to deteriorate various cell functions and is implicated in the pathogenesis of diabetic vascular complications. In the present study, we show that the cellular constituents of small vessels, endothelial cells (EC) and pericytes express novel splice variants of RAGE mRNA coding for the isoforms that lack the N-terminal V-type immunoglobulin-like domain (N-truncated) or the C-terminal transmembrane domain (C-truncated), as well as the known full-length mRNA. The ratio of the expression of the three variants was different between EC and pericytes; the content of the C-truncated form was highest in EC, whereas the full-length form was the most abundant in pericytes. Transfection experiments with COS-7 cells demonstrated that those variant mRNAs were translated into proteins as deduced; C-truncated RAGE was efficiently secreted into the culture media, and N-truncated RAGE was located mainly on the plasma membrane. The three isoforms were also detected in primary cultured human EC and pericytes. Further, full-length and C-truncated forms of RAGE bound to an AGE-conjugated column, whereas N-truncated RAGE did not. The AGE induction of extracellular-signal-related kinase phosphorylation and vascular endothelial growth factor in EC and of the growth and cord-like structure formation of EC was abolished completely by C-truncated RAGE, indicating that this endogenous secretory receptor (endogenous secretory RAGE) is cytoprotective against AGE. The results may contribute to our understanding of the molecular basis for the diversity of cellular responses to AGE and for individual variations in the susceptibility to diabetic vascular complications.

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