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Advanced glycation end products and the kidney

American Journal of Physiology-Renal Physiology, 2005
Advanced glycation end products (AGEs) are a heterogeneous group of protein and lipids to which sugar residues are covalently bound. AGE formation is increased in situations with hyperglycemia (e.g., diabetes mellitus) and is also stimulated by oxidative stress, for example in uremia.
Jürgen M, Bohlender   +3 more
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Advanced Glycation End Products Inhibitor

2010
Early intensive glycemic control in both type 1 and type 2 diabetes mellitus retards in the long term the development and progression of microvascular complications such as diabetic nephropathy, even despite a worsening glycemic control. This phenomenon is a so-called metabolic memory or legacy effect, partly ascribed to the advanced glycation end ...
Takashi Dan   +2 more
openaire   +1 more source

Advanced Glycation End Products and Insulin Resistance

Current Pharmaceutical Design, 2008
Non-enzymatic modification of proteins by reducing sugars, a process that is also known as Maillard reaction, leads to the formation of advanced glycation end products (AGEs) in vivo. There is a growing body of evidence that formation and accumulation of AGEs progress during normal aging, and at an extremely accelerated rate under diabetes, thus being ...
Hiroyuki, Unoki, Sho-ichi, Yamagishi
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Role of dietary advanced glycation end products

Current Opinion in Lipidology, 2017
Refereed/Peer ...
Peter, Clifton, Jennifer, Keogh
openaire   +3 more sources

Advanced Glycation End Products and Diabetic Nephropathy

American Journal of Therapeutics, 2005
Chronic hyperglycemia and oxidative stress in diabetes results in the formation and accumulation advanced glycation end products (AGEs). AGEs have a wide range of chemical, cellular, and tissue effects that contribute to the development of microvascular complications. In particular, AGEs appear to have a key role in the diabetic nephropathy.
Merlin C, Thomas   +2 more
openaire   +2 more sources

Advanced glycation end products and diabetic complications

Expert Opinion on Investigational Drugs, 2002
Diabetic complications are major cause of morbidity and mortality in patients with diabetes. While the precise pathogenic mechanism(s) underlying conditions such as diabetic retinopathy, diabetic nephropathy and increased risk of atherosclerosis remain ill-defined, it is clear that hyperglycaemia is a primary factor that initiates and promotes ...
Stitt, Alan, Jenkins, A.J., Cooper, M.E.
openaire   +3 more sources

Advanced Glycation End Products in Renal Failure

Journal of Renal Nutrition, 2006
Cellular and extracellular proteins suffer significant damage in vivo by glycation. Physiological proteolysis of proteins damaged by glycation forms glycation free adducts that are released into plasma for urinary excretion. Inefficient elimination of these free adducts in uremia leads to their accumulation.
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Advanced Glycation End Products and Cardiovascular Disease

Current Diabetes Reviews, 2008
Cardiovascular disease (CVD) is the leading cause of mortality worldwide. Advanced glycation end products [AGEs] seem to play an important role for the development and/or progression of CVD mainly through induction of oxidative stress and inflammation.
Melpomeni, Peppa, Sotirios A, Raptis
openaire   +2 more sources

Advanced Glycation End Products

Circulation, 2006
Advanced glycation end products (AGEs) are proteins or lipids that become glycated after exposure to sugars. AGEs are prevalent in the diabetic vasculature and contribute to the development of atherosclerosis. The presence and accumulation of AGEs in many different cell types affect extracellular and intracellular structure and function.
Alison, Goldin   +3 more
openaire   +2 more sources

Mass spectrometry of advanced glycation end products

2005
Mass spectrometry, in particular matrix assisted laser desorption/ionisation, is a powerful analytical tool in studies devoted to protein non-enzymatic glycation. It has been firstly tested on in vitro glycated proteins, and looking at the reliable results so obtained, on in vivo glycated proteins in population of healthy, well-controlled and badly ...
LAPOLLA, ANNUNZIATA, BASSO E., TRALDI P.
openaire   +4 more sources

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