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dc.contributor.authorSamouillan, Valeriees_ES
dc.contributor.authorRevuelta-López, Elenaes_ES
dc.contributor.authorSoler-Botija, Carolinaes_ES
dc.contributor.authorDandurand, Janyes_ES
dc.contributor.authorBenitez-Amaro, Aleydaes_ES
dc.contributor.authorNasarre, Lauraes_ES
dc.contributor.authorGonzalo-Calvo, David dees_ES
dc.contributor.authorBayés Genís, Antonies_ES
dc.contributor.authorLacabanne, Colettees_ES
dc.contributor.authorLlorente-Cortés, Vicentaes_ES
dc.identifier.citationBiochimica et Biophysica Acta - Molecular Basis of Disease 1863(6): 1500-1509 (2017)es_ES
dc.description.abstractAdverse cardiac remodeling after myocardial infarction (MI) causes impaired ventricular function and heart failure. Histopathological characterization is commonly used to detect the location, size and shape of MI sites. However, the information about chemical composition, physical structure and molecular mobility of peri- and infarct zones post-MI is rather limited. The main objective of this work was to explore the spatiotemporal biochemical and biophysical alterations of key cardiac components post-MI. The FTIR spectra of healthy and remote myocardial tissue shows amides A, I, II and III associated with proteins in freeze-died tissue as major absorptions bands. In infarcted myocardium, the spectrum of these main absorptions was deeply altered. FITR evidenced an increase of the amide A band and the distinct feature of the collagen specific absorption band at 1338 cm−1 in the infarct area at 21 days post-MI. At 21 days post-MI, it also appears an important shift of amide I from 1646 cm−1 to 1637 cm−1 that suggests the predominance of the triple helical conformation in the proteins. The new spectra bands also indicate an increase in proteoglycans, residues of carbohydrates in proteins and polysaccharides in ischemic areas. Thermal analysis indicates a deep increase of unfreezable water/freezable water in peri- and infarcted tissues. In infarcted tissue is evidenced the impairment of myofibrillar proteins thermal profile and the emergence of a new structure. In conclusion, our results indicate a profound evolution of protein secondary structures in association with collagen deposition and reorganization of water involved in the scar maturation of periand infarct zones post-MI.es_ES
dc.description.sponsorshipThe research leading to these results received funding from the Instituto de Salud Carlos III (FIS PI14/01729 and FIS PI14/01682) that was cofinanced by the European Fund for Regional Development, and CIBER Cardiovascular (CB16/11/00403), as well as from the Ministerio de Ciencia e Innovación (SAF2011-30067-C02-01), the Fundació La Marató de TV3 (201521_10, 201502_30 and 080330), the Red de Terapia Celular-TerCel (RD12/0019/0029), the Sociedad Española de Cardiología and the Fundació Privada Daniel Bravo Andreu. DdG is a recipient of CD14/0109 from Sara Borell of the Instituto de Salud Carlos III.es_ES
dc.subjectMyocardial infarctiones_ES
dc.subjectPhysical characterizationes_ES
dc.titleConformational and thermal characterization of left ventricle remodeling post-myocardial infarctiones_ES
dc.description.peerreviewedPeer reviewedes_ES
dc.contributor.funderInstituto de Salud Carlos IIIes_ES
dc.contributor.funderEuropean Commissiones_ES
dc.contributor.funderMinisterio de Ciencia e Innovación (España)es_ES
dc.contributor.funderFundació La Marató de TV3es_ES
dc.contributor.funderRed de Terapia Celular (España)es_ES
dc.contributor.funderSociedad Española de Cardiologíaes_ES
dc.contributor.funderFundació Privada Daniel Bravo Andreues_ES
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