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oai:repisalud.isciii.es:20.500.12105/52562024-09-27T10:11:42Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19607

00925njm 22002777a 4500 dc Martin-Rojas, Tatiana author Mourino-Alvarez, Laura author Alonso-Orgaz, Sergio author Rosello-Lleti, Esther author Calvo, Enrique author Fernando Lopez-Almodovar, Luis author Rivera, Miguel author Padial, Luis R. author Lopez, Juan Antonio author de la Cuesta, Fernando author Barderas, Maria G author 2015 Degenerative aortic stenosis (AS) is the most common worldwide cause of valve replacement. The aortic valve is a thin, complex, layered connective tissue with compartmentalized extracellular matrix (ECM) produced by specialized cell types, which directs blood flow in one direction through the heart. There is evidence suggesting remodeling of such ECM during aortic stenosis development. Thus, a better characterization of the role of ECM proteins in this disease would increase our understanding of the underlying molecular mechanisms. Aortic valve samples were collected from 18 patients which underwent aortic valve replacement (50\% males, mean age of 74 years) and 18 normal control valves were obtained from necropsies (40\% males, mean age of 69 years). The proteome of the samples was analyzed by 2D-LC MS/MS iTRAQ methodology. The results showed an altered expression of 13 ECM proteins of which 3 (biglycan, periostin, prolargin) were validated by Western blotting and/or SRM analyses. These findings are substantiated by our previous results demonstrating differential ECM protein expression. The present study has demonstrated a differential ECM protein pattern in individuals with AS, therefore supporting previous evidence of a dynamic ECM remodeling in human aortic valves during AS development. Sci Rep. 2015; 5:17290 10.1038/srep17290 2045-2322 Scientific Reports 26620461 http://hdl.handle.net/20.500.12105/5256 LEUCINE-RICH REPEAT OSTEOBLAST-SPECIFIC FACTOR TOLL-LIKE RECEPTOR-4 ATHEROSCLEROTIC PLAQUES INTERSTITIAL-CELLS OXIDIZED LDL PERIOSTIN STENOSIS BIGLYCAN PROTEIN iTRAQ proteomic analysis of extracellular matrix remodeling in aortic valve disease