Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin.
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TLDR
The formation of methylglyoxal-modified proteins involves glycoxidation leading to advanced glycation end product-like fluorescence and is expected to be increased in diabetes mellitus and may be linked to the development of diabetic complications.About:
This article is published in Journal of Biological Chemistry.The article was published on 1994-12-23 and is currently open access. It has received 691 citations till now. The article focuses on the topics: Methylglyoxal & Bovine serum albumin.read more
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Advanced glycation end products: sparking the development of diabetic vascular injury.
TL;DR: Because of the emerging evidence about the adverse effects of AGEs on the vasculature of patients with diabetes, a number of different therapies to inhibit A GEs are under investigation.
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Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose.
TL;DR: Alpha-Oxoaldehydes were formed in early glycation from the degradation of glucose and Schiff's base adduct, which suggests that short periods of hyperglycaemia, as occur in impaired glucose tolerance, may be sufficient to increase the concentrations of alpha-oxoaldeHydes in vivo.
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Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response.
TL;DR: Necrosis occurs in both physiological and pathophysiological processes, and is capable of killing tumour cells that have developed strategies to evade apoptosis, so detailed knowledge of necrosis may be exploited in therapeutic strategies.
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N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins.
Mahtab U. Ahmed,Elisabeth Brinkmann Frye,Thorsten P. Degenhardt,Suzanne R. Thorpe,John W. Baynes +4 more
TL;DR: Levels of CML and CEL are proposed to 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.
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Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): An overview of their mechanisms of formation
TL;DR: The aim of the present review is to group the main AGEs and ALEs and to describe, for each of them, the precursors and mechanisms of formation.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Relation between Complications of Type I Diabetes Mellitus and Collagen-Linked Fluorescence
Vincent M. Monnier,Vasanth Vishwanath,Kay E. Frank,Craig A. Elmets,Paul J Dauchot,Robert R. Kohn +5 more
TL;DR: The data suggest that there is an overall correlation between the severity of diabetic complications and cumulative glycemia over many years.
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The Reaction of Phenylglyoxal with Arginine Residues in Proteins
TL;DR: Phenylglyoxal (14C-labeled, if desired) may be useful for modification of accessible arginine residues in proteins and may be potentially useful for reversible coverage of arginin residues so that tryptic hydrolysis can take place at lysine residues only.
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Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications.
TL;DR: The glyoxalase system was characterized in blood samples from patients with insulin-dependent diabetes mellitus, patients with non-insulin-dependent Diabetes mellitus and 21 normal healthy control subjects.