Cardiac protein changes in ischaemic and dilated cardiomyopathy: A proteomic study of human left ventricular tissue

The development of heart failure (HF) is characterized by progressive alteration of left ventricle structure and function. Previous works on proteomic analysis in cardiac tissue from patients with HF remain scant. The purpose of our study was to use a proteomic approach to investigate variations in...

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Detalles Bibliográficos
Autores: Roselló-LLetí, Esther, Alonso Lorenzo, Jana, Cortés, Raquel, Almenar, Luis, Martínez-Dolz, Luis, Sánchez-Lázaro, Ignacio, Lago Paz, Francisca, Azorín, Inmaculada, González Juanatey, José Ramón, Portolés, Manuel, Rivera, Miguel
Tipo de recurso: artículo
Fecha de publicación:2012
País:España
Institución:Servizo Galego de Saúde (SERGAS)
Repositorio:RUNA. Repositorio da Consellería de Sanidade e Sergas
OAI Identifier:oai:runa.sergas.gal:20.500.11940/4739
Acceso en línea:http://hdl.handle.net/20.500.11940/4739
Access Level:acceso abierto
Palabra clave:Cardiomyopathy, Dilated
Electrophoresis, Gel, Two-Dimensional
Heart Failure
Myocardial Ischemia
Proteome
Cardiomiopatía Dilatada
Electroforesis en Gel Bidimensional
Insuficiencia Cardíaca
Isquemia Miocárdica
Proteoma
Descripción
Sumario:The development of heart failure (HF) is characterized by progressive alteration of left ventricle structure and function. Previous works on proteomic analysis in cardiac tissue from patients with HF remain scant. The purpose of our study was to use a proteomic approach to investigate variations in protein expression of left ventricle tissue from patients with ischaemic (ICM) and dilated cardiomyopathy (DCM). Twenty-four explanted human hearts, 12 from patients with ICM and 12 with DCM undergoing cardiac transplantation and six non-diseased donor hearts (CNT) were analysed by 2DE. Proteins of interest were identified by mass spectrometry and validated by Western blotting and immunofluorescence. We encountered 35 differentially regulated spots in the comparison CNT versus ICM, 33 in CNT versus DCM, and 34 in ICM versus DCM. We identified glyceraldehyde 3-phophate dehydrogenase up-regulation in both ICM and DCM, and alpha-crystallin B down-regulation in both ICM and DCM. Heat shock 70 protein 1 was up-regulated only in ICM. Ten of the eleven differentially regulated proteins common to both aetiologies are interconnected as a part of a same network. In summary, we have shown by proteomics analysis that HF is associated with changes in proteins involved in the cellular stress response, respiratory chain and cardiac metabolism. Although we found altered expression of eleven proteins common to both ischaemic and dilated aetiology, we also observed different proteins altered in both groups. Furthermore, we obtained that seven of these eleven proteins are involved in cell death and apoptosis processes, and therefore in HF progression.