Methylglyoxal Modification of mSin3A Links Glycolysis to Angiopoietin-2 Transcription
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منابع مشابه
Methylglyoxal Modification of mSin3A Links Glycolysis to Angiopoietin-2 Transcription
Methylglyoxal is a highly reactive dicarbonyl degradation product formed from triose phosphates during glycolysis. Methylglyoxal forms stable adducts primarily with arginine residues of intracellular proteins. The biologic role of this covalent modification in regulating cell function is not known. Here, we report that in retinal Müller cells, increased glycolytic flux causes increased methylgl...
متن کاملRETRACTED: Methylglyoxal Modification of mSin3A Links Glycolysis to Angiopoietin-2 Transcription
Dachun Yao, Tetsuya Taguchi, Takeshi Matsumura, Richard Pestell, Diane Edelstein, Ida Giardino, Guntram Suske, Naila Ahmed, Paul J. Thornalley, Vijay P. Sarthy, Hans-Peter Hammes, and Michael Brownlee* JDRF International Center for Diabetic Complications Research, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA Lombardi Cancer Center, Department of Oncology, G...
متن کاملMethylglyoxal, the dark side of glycolysis
Glucose is the main energy substrate for the brain. There is now extensive evidence indicating that the metabolic profile of neural cells with regard to glucose utilization and glycolysis rate is not homogenous, with a marked propensity for glycolytic glucose processing in astrocytes compared to neurons. Methylglyoxal, a highly reactive dicarbonyl compound, is inevitably formed as a by-product ...
متن کاملMethylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts.
Methylglyoxal (MG), an endogenous metabolite that increases in diabetes and is a common intermediate in the Maillard reaction (glycation), reacts with proteins and forms advanced glycation end products. In the present study, we identify a novel MG-arginine adduct and also characterize the structure of a major fluorescent adduct. In addition, we describe the immunochemical study on the MG-argini...
متن کاملBinding and Modification of Proteins by Methylglyoxal under Physiological Conditions
The physiological a-oxoaldehyde methylglyoxal binds and modifies arginine, lysine, and cysteine residues in proteins. The kinetics and mechanism of these reactions were investigated with Na-acetylamino acids and bovine serum albumin at pH 7.4 and 37 “C. The reaction of methylglyoxal with Na-acetylarginine involved the initial reversible formation of glycosylamine and 4,5-dihydroxy5-methylimidaz...
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ژورنال
عنوان ژورنال: Cell
سال: 2007
ISSN: 0092-8674
DOI: 10.1016/j.cell.2007.01.026