title: Cardiac protein changes in ischaemic and dilated cardiomyopathy: a proteomic study of human left ventricular tissue.
abstract: 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.
authors.affiliation: Cardiocirculatory Unit, Research Center, Hospital Universitario La Fe, Valencia, Spain.
authors.forename: Esther
authors.initials: E
authors.lastname: Roselló-Lletí
authors.forename: Jana
authors.initials: J
authors.lastname: Alonso
authors.forename: Raquel
authors.initials: R
authors.lastname: Cortés
authors.forename: Luis
authors.initials: L
authors.lastname: Almenar
authors.forename: Luis
authors.initials: L
authors.lastname: Martínez-Dolz
authors.forename: Ignacio
authors.initials: I
authors.lastname: Sánchez-Lázaro
authors.forename: Francisca
authors.initials: F
authors.lastname: Lago
authors.forename: Inmaculada
authors.initials: I
authors.lastname: Azorín
authors.forename: Jose R González
authors.initials: JR
authors.lastname: Juanatey
authors.forename: Manuel
authors.initials: M
authors.lastname: Portolés
authors.forename: Miguel
authors.initials: M
authors.lastname: Rivera
mesh_terms: D000328:Adult; D015153:Blotting, Western; D002311:Cardiomyopathy, Dilated / Q000175:diagnosis* / Q000503:physiopathology*; D015536:Down-Regulation; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D024601:Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) / Q000235:genetics / Q000378:metabolism; D050884:HSP72 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006333:Heart Failure / Q000503:physiopathology; D006352:Heart Ventricles / Q000503:physiopathology; D006801:Humans; D008297:Male; D013058:Mass Spectrometry; D008856:Microscopy, Fluorescence; D008875:Middle Aged; D017202:Myocardial Ischemia / Q000175:diagnosis* / Q000503:physiopathology*; D020543:Proteome / Q000032:analysis*; D040901:Proteomics; D015854:Up-Regulation; D038203:alpha-Crystallin B Chain / Q000235:genetics / Q000378:metabolism
chemical_list: D050884:HSP72 Heat-Shock Proteins; D020543:Proteome; D038203:alpha-Crystallin B Chain; D024601:Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)