Mapping of redox state of mitochondrial cytochromes in live cardiomyocytes using Raman microspectroscopy
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 cardiomyocyt...
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| Veröffentlicht in: | PloS one 2012-09, Vol.7 (9), p.e41990 |
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| creator | Brazhe, Nadezda A Treiman, Marek Brazhe, Alexey R Find, Ninett L Maksimov, Georgy V Sosnovtseva, Olga V |
| description | 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. |
| doi_str_mv | 10.1371/journal.pone.0041990 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0041990</identifier><identifier>PMID: 22957018</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Apoptosis ; Biology ; Cardiac arrhythmia ; Cardiomyocytes ; Cluster analysis ; Cytochrome ; Cytochromes ; Cytochromes - metabolism ; Fluorescence ; Fluorescent indicators ; Gene expression ; Heart cells ; Heart failure ; Hydrogen peroxide ; Hydrogen Peroxide - chemistry ; Hydroxyl Radical ; Ischemia ; Mapping ; Membrane Potentials ; Microscopy ; Microscopy, Fluorescence - methods ; Mitochondria ; Mitochondria - metabolism ; Models, Statistical ; Myocytes, Cardiac - cytology ; Oxidation-Reduction ; Oxidative Stress ; Raman spectroscopy ; Rats ; Redox properties ; Rodents ; Spectroscopy ; Spectrum analysis ; Spectrum Analysis, Raman - methods ; Studies ; Time Factors</subject><ispartof>PloS one, 2012-09, Vol.7 (9), p.e41990</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>Brazhe et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2012 Brazhe et al 2012 Brazhe et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-23d141847467e71ad8e6dca317c81516581feb4bc0ac00600153cb522edc367b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3434226/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3434226/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22957018$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Saks, Valdur</contributor><creatorcontrib>Brazhe, Nadezda A</creatorcontrib><creatorcontrib>Treiman, Marek</creatorcontrib><creatorcontrib>Brazhe, Alexey R</creatorcontrib><creatorcontrib>Find, Ninett L</creatorcontrib><creatorcontrib>Maksimov, Georgy V</creatorcontrib><creatorcontrib>Sosnovtseva, Olga V</creatorcontrib><title>Mapping of redox state of mitochondrial cytochromes in live cardiomyocytes using Raman microspectroscopy</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>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.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Biology</subject><subject>Cardiac arrhythmia</subject><subject>Cardiomyocytes</subject><subject>Cluster analysis</subject><subject>Cytochrome</subject><subject>Cytochromes</subject><subject>Cytochromes - metabolism</subject><subject>Fluorescence</subject><subject>Fluorescent indicators</subject><subject>Gene expression</subject><subject>Heart cells</subject><subject>Heart failure</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Hydroxyl Radical</subject><subject>Ischemia</subject><subject>Mapping</subject><subject>Membrane Potentials</subject><subject>Microscopy</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Mitochondria</subject><subject>Mitochondria - 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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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22957018</pmid><doi>10.1371/journal.pone.0041990</doi><tpages>e41990</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Apoptosis Biology Cardiac arrhythmia Cardiomyocytes Cluster analysis Cytochrome Cytochromes Cytochromes - metabolism Fluorescence Fluorescent indicators Gene expression Heart cells Heart failure Hydrogen peroxide Hydrogen Peroxide - chemistry Hydroxyl Radical Ischemia Mapping Membrane Potentials Microscopy Microscopy, Fluorescence - methods Mitochondria Mitochondria - metabolism Models, Statistical Myocytes, Cardiac - cytology Oxidation-Reduction Oxidative Stress Raman spectroscopy Rats Redox properties Rodents Spectroscopy Spectrum analysis Spectrum Analysis, Raman - methods Studies Time Factors |
| title | Mapping of redox state of mitochondrial cytochromes in live cardiomyocytes using Raman microspectroscopy |
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