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Dadun > Depósito Académico > CIMA (Centro de Investigación Médica Aplicada) > Área de Terapia génica y Hepatología > Hepatología bioquímica > DA - CIMA - Terapia génica y Hepatología - Hepatología bioquímica - Artículos de revista >

Oxidation of specific methionine and tryptophan residues of apolipoprotein A-I in hepatocarcinogenesis
Autor(es) : Fernandez-Irigoyen, J. (Joaquín)
Santamaria, E. (Enrique)
Sesma, L. (Laura)
Muñoz, J. (Javier)
Riezu-Boj, J.I. (José Ignacio)
Caballeria, J. (Juan)
Lu, S.C. (Shelly C.)
Prieto, J. (Jesús)
Mato, J.M. (José María)
Avila, M.A. (Matías Antonio)
Corrales, F.J. (Fernando José)
Palabras clave : 2-D PAGE
Apolipoprotein A
Hepatocellular carcinoma
Mass spectrometry
Serum biomarkers
Fecha incorporación: 2005
Editorial : Wiley-VCH Verlag Berlin
Versión del editor: http://onlinelibrary.wiley.com/doi/10.1002/pmic.200500070/abstract
ISSN: 1615-9861
Cita: Fernandez-Irigoyen J, Santamaria E, Sesma L, Muñoz J, Riezu JI, Caballeria J, et al. Oxidation of specific methionine and tryptophan residues of apolipoprotein A-I in hepatocarcinogenesis. Proteomics 2005 Dec;5(18):4964-4972.
Resumen
Hepatocellular carcinoma (HCC) is the fifth most common neoplasm with more than 500 000 new cases diagnosed yearly. Although major risk factors of HCC are currently known, the identification of biological targets leading to an early diagnosis of the disease is considered one of the priorities of clinical hepatology. In this work we have used a proteomic approach to identify markers of hepatocarcinogenesis in the serum of a knockout mice deficient in hepatic AdoMet synthesis (MAT1A(-/-)), as well as in patients with HCC. Three isoforms of apolipoprotein A-I (Apo A-I) with different pI were identified in murine serum. Isoform 1 is up-regulated in the serum of MAT1A(-/-) mice much earlier than any histological manifestation of liver disease. Further characterization of the differential isoform by electrospray MS/MS revealed specific oxidation of methionine 85 and 216 to methionine sulfoxide while the sequence of the analogous peptides on isoforms 2 and 3 showed the nonoxidized methionine residues. Enrichment of an acidic isoform of Apo A-I was also assessed in the serum of hepatitis B virus patients who developed HCC. Specific oxidation of methionine 112 to methionine sulfoxide and tryptophans 50 and 108 to formylkinurenine were identified selectively in the up-regulated isoform. Although it is not clear at present whether the occurrence of these modifications has a causal role or simply reflects secondary epiphenomena, this selectively oxidized Apo A-I isoform may be considered as a pathological hallmark that may help to the understanding of the molecular pathogenesis of HCC.
Enlace permanente: http://hdl.handle.net/10171/21418
Aparece en las colecciones: DA - CUN - Medicina interna - Artículos de revista
DA - Medicina - Medicina Interna - Artículos de revista
DA - CIMA - Terapia génica y Hepatología - Virología - Artículos de revista
DA - CIMA - Unidad de Proteómica, Genómica y Bioinformática - Artículos de revista
DA - CIMA - Terapia génica y Hepatología - Hepatología bioquímica - Artículos de revista

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