scholarly journals Advanced glycation end products and diabetic complications: A General overview

HORMONES ◽  
2005 ◽  
Vol 4 (1) ◽  
pp. 28-37 ◽  
Author(s):  
Melpomeni Peppa ◽  
Helen Vlassara
Keyword(s):  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Advanced Glycation ◽  
General Overview ◽  
Glycation End Products ◽  
End Products

scholarly journals Advanced Glycation End Products: Formation, Role in Diabetic Complications, and Potential in Clinical Applications

2020 ◽  
Author(s):  
Rujman Khan ◽  
Xin Yee Ooi ◽  
Matthew Parvus ◽  
Laura Valdez ◽  
Andrew Tsin
Keyword(s):  
Diabetic Retinopathy ◽  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Tanshinone Iia ◽  
Future Research ◽  
Advanced Glycation ◽  
Reactive Aldehydes ◽  
Glycation End Products ◽  
End Products ◽  
Lysine Residues

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.

Monocyte CD147 is induced by advanced glycation end products and high glucose concentration: possible role in diabetic complications

2010 ◽  
Vol 299 (5) ◽  
pp. C1212-C1219 ◽  
Author(s):  
W. Bao ◽  
D. Min ◽  
S. M. Twigg ◽  
N. A. Shackel ◽  
F. J. Warner ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
High Glucose ◽  
Transmembrane Protein ◽  
Soluble Form ◽  
Dependent Manner ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Cd147 Expression

CD147 is a highly glycosylated transmembrane protein that is known to play a role in regulation of many protein families. It has the unique ability to maintain functional activity in both the membrane bound state and in the soluble form. CD147 is known to play a role in regulation of matrix metalloproteinase (MMP) expression, but whether its expression is affected by the diabetic milieu is not known, and its role in regulation of monocyte MMPs in this environment has not been investigated. Therefore, in this study we investigated the effect of advanced glycation end products (AGEs) and high glucose (HG; 25 mM), on monocyte CD147 expression. Culture of THP-1 monocytes in the presence of AGEs or HG significantly increased CD147 at the gene and protein level. THP-1 cell results were confirmed using freshly isolated monocytes from human volunteers. The effect of AGEs and HG on CD147 expression was also mimicked by addition of proinflammatory cytokines. Addition of AGEs or HG also increased expression of monocyte MMP-1 and MMP-9 but not MMP-2. This increase in MMPs was significantly attenuated by inhibition of CD147 using either a small interfering RNA or an anti-CD147 antibody. Inhibition of NF-κB or addition of antibodies to either TNF-α or the receptor for AGE (RAGE) each significantly prevented in a dose-dependent manner the induction of CD147 gene and protein by AGE and also decreased MMP-1 and MMP-9. This novel result shows that AGEs can induce monocyte CD147 expression, an effect mediated by inflammatory pathways and RAGE. Because MMPs play a role in monocyte migration, inhibition of their regulator CD147 may assist in the prevention of diabetic complications, particularly those where monocyte infiltration is an early initiating event.

Increased Serum Levels of Advanced Glycation End Products in NIDDM Patients With Diabetic Complications

Diabetes Care ◽  
1998 ◽  
Vol 21 (6) ◽  
pp. 1027-1027 ◽  
Author(s):  
Y. Ono ◽  
S. Aoki ◽  
K. Ohnishi ◽  
T. Yasuda ◽  
K. Kawano ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Serum Levels ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Niddm Patients

scholarly journals Advanced Glycation End Products Activate a Chymase-Dependent Angiotensin II–Generating Pathway in Diabetic Complications

Circulation ◽  
2006 ◽  
Vol 113 (10) ◽  
pp. 1353-1360 ◽  
Author(s):  
Vijay Koka ◽  
Wansheng Wang ◽  
Xiao Ru Huang ◽  
Shokei Kim-Mitsuyama ◽  
Luan D. Truong ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Increased serum levels of advanced glycation end-products and diabetic complications

1998 ◽  
Vol 41 (2) ◽  
pp. 131-137 ◽  
Author(s):  
Yuri Ono ◽  
Shin Aoki ◽  
Katsunori Ohnishi ◽  
Takuzi Yasuda ◽  
Katsumi Kawano ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Serum Levels ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

scholarly journals Advanced Glycation End Products and Diabetic Complications

2014 ◽  
Vol 18 (1) ◽  
pp. 1 ◽  
Author(s):  
Varun Parkash Singh ◽  
Anjana Bali ◽  
Nirmal Singh ◽  
Amteshwar Singh Jaggi
Keyword(s):  
Advanced Glycation End Products ◽  
Diabetic Complications ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products
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