The Danish National Foundation Research Center for Heart Arrhythmia

Copenhagen, Denmark

The Danish National Foundation Research Center for Heart Arrhythmia

Copenhagen, Denmark
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Brazhe N.A.,Copenhagen University | Treiman M.,Copenhagen University | Treiman M.,The Danish National Foundation Research Center for Heart Arrhythmia | Brazhe A.R.,Moscow State University | And 4 more authors.
PLoS ONE | Year: 2012

This paper presents a nonivasive approach to study redox state of reduced cytochromes c, c1 and b of complexes II and III in mitochondria of live cardiomyocytes by means of Raman microspectroscopy. For the first time with the proposed approach we perform studies of rod- and round-shaped cardiomyocytes, representing different morphological and functional states. Raman mapping and cluster analysis reveal that these cardiomyocytes differ in the amounts of reduced cytochromes c, c1 and b. The rod-shaped cardiomyocytes possess uneven distribution of reduced cytochromes c, c1 and b in cell center and periphery. Moreover, by means of Raman spectroscopy we demonstrated the decrease in the relative amounts of reduced cytochromes c, c1 and b in the rod-shaped cardiomyocytes caused by H2O2-induced oxidative stress before any visible changes. Results of Raman mapping and time-dependent study of reduced cytochromes of complexes II and III and cytochrome c in cardiomyocytes are in a good agreement with our fluorescence indicator studies and other published data. © 2012 Brazhe et al.


Brazhe N.A.,Copenhagen University | Treiman M.,Copenhagen University | Treiman M.,The Danish National Foundation Research Center for Heart Arrhythmia | Faricelli B.,Copenhagen University | And 4 more authors.
PLoS ONE | Year: 2013

We developed a Raman spectroscopy-based approach for simultaneous study of redox changes in c-and b-type cytochromes and for a semiquantitative estimation of the amount of oxygenated myoglobin in a perfused rat heart. Excitation at 532 nm was used to obtain Raman scattering of the myocardial surface of the isolated heart at normal and hypoxic conditions. Raman spectra of the heart under normal pO2 demonstrate unique peaks attributable to reduced c-and b-type cytochromes and oxymyoglobin (oMb). The cytochrome peaks decreased in intensity upon FCCP treatment, as predicted from uncoupling mitochondrial respiration. Conversely, transient hypoxia causes the reversible increase in the intensity of peaks assigned to cytochromes c and c1, reflecting electron stacking proximal to cytochrome oxidase due to the lack of terminal electron acceptor O2. Intensities of peaks assigned to oxy- and deoxyhemoglobin were used for the semiquantitative estimation of oMb deoxygenation that was found to be of approximately 50% under hypoxia conditions. © 2013 Brazhe et al.

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