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Title

Conformational and thermal characterization of left ventricle remodeling post-myocardial infarction

AuthorsSamouillan, Valerie; Revuelta-López, Elena; Soler-Botija, Carolina; Dandurand, Jany; Benitez-Amaro, Aleyda; Nasarre, Laura; Gonzalo-Calvo, David de; Bayés Genís, Antoni; Lacabanne, Colette; Llorente-Cortés, Vicenta
KeywordsMyocardial infarction
FITR
Physical characterization
DSC
Issue DateJun-2017
PublisherElsevier
CitationBiochimica et Biophysica Acta - Molecular Basis of Disease 1863(6): 1500-1509 (2017)
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.
Publisher version (URL)https://doi.org/10.1016/j.bbadis.2017.02.025
URIhttp://hdl.handle.net/10261/176099
DOI10.1016/j.bbadis.2017.02.025
ISSN0925-4439
Appears in Collections:(CIC) Artículos
(IIBB) Artículos
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