Formation of α-Aminoadipic and γ-Glutamic Semialdehydes in Proteins by the Maillard Reaction
| Autor: | Yayoi Kurota, Mitsugu Akagawa, Daisuke Sasaki, Kyozo Suyama |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Glycation End Products
Advanced Amidines Deamination Reductive amination General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound symbols.namesake Glutamates History and Philosophy of Science Glycation Humans Serum Albumin Chromatography General Neuroscience Methylglyoxal Proteins Serum Albumin Bovine Oxidative deamination Ascorbic acid Maillard Reaction Maillard reaction Biochemistry chemistry Carcinogens symbols Acid hydrolysis 2-Aminoadipic Acid Mutagens |
| Zdroj: | Annals of the New York Academy of Sciences. 1043:129-134 |
| ISSN: | 0077-8923 |
| DOI: | 10.1196/annals.1333.016 |
| Popis: | Recent research has demonstrated that nonenzymatic glycation (the Maillard reaction) lead to the formation of carbonyl groups and advanced glycation end products (AGEs) in proteins. Such oxidative modifications are a major contributing factor to diabetic complications and aging. alpha-Aminoadipic semialdehyde (AAS) and gamma-glutamic semialdehyde (GGS) have been identified as the major carbonyl products in oxidized proteins both in vitro and in vivo. AAS is an oxidative deamination product of lysine residue, while GGS originates from arginine and proline residues. To evaluate oxidative damage to proteins by the Maillard reaction, we developed a method of detecting AAS and GGS by high-performance liquid chromatography (HPLC). The aldehydic residues in proteins were derivatized by reductive amination with NaCNBH3 and p-aminobenzoic acid (ABA), a fluorescence regent. After acid hydrolysis of the ABA-derivatized protein, ABA-AAS and ABA-GGS were measured by fluorometric HPLC. Thus, AAS and GGS could be detected in various proteins such as human plasma protein using the present method. Accumulation of both aldehydic residues was observed in oxidized proteins by reactive oxygen species. Furthermore, AAS and GGS were markedly formed in the incubation of BSA with ascorbic acid. The formation of both aldehydic residues was also observed in the incubation of BSA with 100 mM glucose or 1.0 mM methylglyoxal in the absence and presence of 100 microM Fe3+ for 2 weeks. These results suggest that the Maillard reaction can contribute to the formation of AAS and GGS in vivo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text