tailieunhanh - Báo cáo khoa học: Yeast protein glycation in vivo by methylglyoxal Molecular modification of glycolytic enzymes and heat shock proteins

Protein glycation by methylglyoxal is a nonenzymatic post-translational modification whereby arginine and lysine side chains form a chemically heterogeneous group of advanced glycation end-products. Methylglyoxal-derived advanced glycation end-products are involved in pathologies such as diabetes and neurodegenerative diseases of the amyloid type. | ỊFEBS Journal Yeast protein glycation in vivo by methylglyoxal Molecular modification of glycolytic enzymes and heat shock proteins Ricardo A. Gomes1 Hugo Vicente Miranda1 Marta Sousa Silva1 Goncalo Graca2 Ana V. Coelho2 3 Antonio E. Ferreira1 Carlos Cordeiro1 and Ana Ponces Freire1 1 Centro de Quimica e Bioquimica Departamento de Quimica e Bioquimica Faculdade de Ciencias da Universidade de Lisboa Portugal 2 Laboratorio de Espectrometria de Massa do Instituto deTecnologia Quimica e Biologica Universidade Nova de Lisboa Oeiras Portugal 3 Departamento de Quimica da Universidade de Evora Portugal Keywords kinetic modeling methylglyoxal peptide mass fingerprint protein glycation yeast Correspondence C. Cordeiro Centro de Quimica e Bioquimica Departamento de Quimica e Bioquimica Faculdade de Ciencias da Universidade de Lisboa Edificio C8 Lisboa Portugal Fax 351 217500088 Tel 351 217500929 E-mail cacordeiro@ Website http enzimol Received 28 June 2006 revised 14 September 2006 accepted 2 October 2006 doi Protein glycation by methylglyoxal is a nonenzymatic post-translational modification whereby arginine and lysine side chains form a chemically heterogeneous group of advanced glycation end-products. Methylglyoxalderived advanced glycation end-products are involved in pathologies such as diabetes and neurodegenerative diseases of the amyloid type. As methylglyoxal is produced nonenzymatically from dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate during glycolysis its formation occurs in all living cells. Understanding methylglyoxal glycation in model systems will provide important clues regarding glycation prevention in higher organisms in the context of widespread human diseases. Using Saccharomy-ces cerevisiae cells with different glycation phenotypes and MALDI-TOF peptide mass fingerprints we identified enolase 2 as the primary methylglyoxal glycation target in yeast. Two other glycolytic enzymes are also

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