Analyzing structural alterations of mitochondrial intermembrane space superoxide scavengers cytochrome-c and SOD1 after methylglyoxal treatment
Mitochondria are quantitatively the most important sources of reactive oxygen species (ROS) which are formed as by-products during cellular respiration. ROS generation occurs when single electrons are transferred to molecular oxygen. This leads to a number of different ROS types, among them superoxi...
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| description | Mitochondria are quantitatively the most important sources of reactive oxygen species (ROS) which are formed as by-products during cellular respiration. ROS generation occurs when single electrons are transferred to molecular oxygen. This leads to a number of different ROS types, among them superoxide. Although most studies focus on ROS generation in the mitochondrial matrix, the intermembrane space (IMS) is also important in this regard. The main scavengers for the detoxification of superoxide in the IMS are Cu, Zn superoxide dismutase (SOD1) and cytochrome-c. Similar to ROS, certain reactive carbonyl species are known for their high reactivity. The consequences are deleterious modifications to essential components compromising cellular functions and contributing to the etiology of severe pathological conditions like cancer, diabetes and neurodegeneration. In this study, we investigated the susceptibility of SOD1 and cytochrome-c to in vitro glycation by the dicarbonyl methylglyoxal (MGO) and the resulting effects on their structure. We utilized experimental techniques like immunodetection of the MGO-mediated modification 5-hydro-5-methylimidazolone, differential scanning calorimetry, fluorescence emission and circular dichroism measurements. We found that glycation of cytochrome-c leads to monomer aggregation, an altered secondary structure (increase in alpha helical content) and slightly more compact folding. In addition to structural changes, glycated cytochrome-c displays an altered thermal unfolding behavior. Subjecting SOD1 to MGO does not influence its secondary structure. However, similar to cytochrome-c, subunit aggregation is observed under denaturating conditions. Furthermore, the appearance of a second peak in the calorimetry diagram indirectly suggests de-metallation of SOD1 when high MGO levels are used. In conclusion, our data demonstrate that MGO has the potential to alter several structural parameters in important proteins of energy metabolism (cytochrome-c) and antioxidant defense (cytochrome-c, SOD1). |
| doi_str_mv | 10.1371/journal.pone.0232408 |
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ROS generation occurs when single electrons are transferred to molecular oxygen. This leads to a number of different ROS types, among them superoxide. Although most studies focus on ROS generation in the mitochondrial matrix, the intermembrane space (IMS) is also important in this regard. The main scavengers for the detoxification of superoxide in the IMS are Cu, Zn superoxide dismutase (SOD1) and cytochrome-c. Similar to ROS, certain reactive carbonyl species are known for their high reactivity. The consequences are deleterious modifications to essential components compromising cellular functions and contributing to the etiology of severe pathological conditions like cancer, diabetes and neurodegeneration. In this study, we investigated the susceptibility of SOD1 and cytochrome-c to in vitro glycation by the dicarbonyl methylglyoxal (MGO) and the resulting effects on their structure. We utilized experimental techniques like immunodetection of the MGO-mediated modification 5-hydro-5-methylimidazolone, differential scanning calorimetry, fluorescence emission and circular dichroism measurements. We found that glycation of cytochrome-c leads to monomer aggregation, an altered secondary structure (increase in alpha helical content) and slightly more compact folding. In addition to structural changes, glycated cytochrome-c displays an altered thermal unfolding behavior. Subjecting SOD1 to MGO does not influence its secondary structure. However, similar to cytochrome-c, subunit aggregation is observed under denaturating conditions. Furthermore, the appearance of a second peak in the calorimetry diagram indirectly suggests de-metallation of SOD1 when high MGO levels are used. In conclusion, our data demonstrate that MGO has the potential to alter several structural parameters in important proteins of energy metabolism (cytochrome-c) and antioxidant defense (cytochrome-c, SOD1).</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0232408</identifier><identifier>PMID: 32353034</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Age ; Agglomeration ; Antioxidants ; Binding sites ; Biology and Life Sciences ; Calorimetry ; Carbonyl compounds ; Carbonyls ; Circular dichroism ; Copper ; Cytochrome ; Cytochrome c ; Cytochromes ; Detoxification ; Diabetes mellitus ; Dichroism ; Differential scanning calorimetry ; Emission measurements ; Energy metabolism ; Enzymes ; Etiology ; Experiments ; Fluorescence ; Glycosylation ; Heat measurement ; Metabolism ; Mitochondria ; Mutation ; Neurodegeneration ; Oxygen ; Physical Sciences ; Protein structure ; Proteins ; Pyruvaldehyde ; Reactive oxygen species ; Research and Analysis Methods ; Scavengers ; Secondary structure ; Single electrons ; Superoxide dismutase</subject><ispartof>PloS one, 2020-04, Vol.15 (4), p.e0232408-e0232408</ispartof><rights>2020 Mercado-Uribe et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://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>2020 Mercado-Uribe et al 2020 Mercado-Uribe et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-706608817389b0fa6a1f172cbfc441e7c66ee34807e52ea9eaace334a99398f13</citedby><cites>FETCH-LOGICAL-c526t-706608817389b0fa6a1f172cbfc441e7c66ee34807e52ea9eaace334a99398f13</cites><orcidid>0000-0002-2924-7547 ; 0000-0002-2602-660X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7192434/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7192434/$$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/32353034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Salimi, Ahmad</contributor><creatorcontrib>Mercado-Uribe, Hilda</creatorcontrib><creatorcontrib>Andrade-Medina, Mariana</creatorcontrib><creatorcontrib>Espinoza-Rodríguez, Juan Horacio</creatorcontrib><creatorcontrib>Carrillo-Tripp, Mauricio</creatorcontrib><creatorcontrib>Scheckhuber, Christian Quintus</creatorcontrib><title>Analyzing structural alterations of mitochondrial intermembrane space superoxide scavengers cytochrome-c and SOD1 after methylglyoxal treatment</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Mitochondria are quantitatively the most important sources of reactive oxygen species (ROS) which are formed as by-products during cellular respiration. ROS generation occurs when single electrons are transferred to molecular oxygen. This leads to a number of different ROS types, among them superoxide. Although most studies focus on ROS generation in the mitochondrial matrix, the intermembrane space (IMS) is also important in this regard. The main scavengers for the detoxification of superoxide in the IMS are Cu, Zn superoxide dismutase (SOD1) and cytochrome-c. Similar to ROS, certain reactive carbonyl species are known for their high reactivity. The consequences are deleterious modifications to essential components compromising cellular functions and contributing to the etiology of severe pathological conditions like cancer, diabetes and neurodegeneration. In this study, we investigated the susceptibility of SOD1 and cytochrome-c to in vitro glycation by the dicarbonyl methylglyoxal (MGO) and the resulting effects on their structure. We utilized experimental techniques like immunodetection of the MGO-mediated modification 5-hydro-5-methylimidazolone, differential scanning calorimetry, fluorescence emission and circular dichroism measurements. We found that glycation of cytochrome-c leads to monomer aggregation, an altered secondary structure (increase in alpha helical content) and slightly more compact folding. In addition to structural changes, glycated cytochrome-c displays an altered thermal unfolding behavior. Subjecting SOD1 to MGO does not influence its secondary structure. However, similar to cytochrome-c, subunit aggregation is observed under denaturating conditions. Furthermore, the appearance of a second peak in the calorimetry diagram indirectly suggests de-metallation of SOD1 when high MGO levels are used. In conclusion, our data demonstrate that MGO has the potential to alter several structural parameters in important proteins of energy metabolism (cytochrome-c) and antioxidant defense (cytochrome-c, SOD1).</description><subject>Age</subject><subject>Agglomeration</subject><subject>Antioxidants</subject><subject>Binding sites</subject><subject>Biology and Life Sciences</subject><subject>Calorimetry</subject><subject>Carbonyl compounds</subject><subject>Carbonyls</subject><subject>Circular dichroism</subject><subject>Copper</subject><subject>Cytochrome</subject><subject>Cytochrome c</subject><subject>Cytochromes</subject><subject>Detoxification</subject><subject>Diabetes mellitus</subject><subject>Dichroism</subject><subject>Differential scanning calorimetry</subject><subject>Emission measurements</subject><subject>Energy metabolism</subject><subject>Enzymes</subject><subject>Etiology</subject><subject>Experiments</subject><subject>Fluorescence</subject><subject>Glycosylation</subject><subject>Heat measurement</subject><subject>Metabolism</subject><subject>Mitochondria</subject><subject>Mutation</subject><subject>Neurodegeneration</subject><subject>Oxygen</subject><subject>Physical Sciences</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Pyruvaldehyde</subject><subject>Reactive oxygen species</subject><subject>Research and Analysis Methods</subject><subject>Scavengers</subject><subject>Secondary structure</subject><subject>Single electrons</subject><subject>Superoxide 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structural alterations of mitochondrial intermembrane space superoxide scavengers cytochrome-c and SOD1 after methylglyoxal treatment</title><author>Mercado-Uribe, Hilda ; Andrade-Medina, Mariana ; Espinoza-Rodríguez, Juan Horacio ; Carrillo-Tripp, Mauricio ; Scheckhuber, Christian Quintus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-706608817389b0fa6a1f172cbfc441e7c66ee34807e52ea9eaace334a99398f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Age</topic><topic>Agglomeration</topic><topic>Antioxidants</topic><topic>Binding sites</topic><topic>Biology and Life Sciences</topic><topic>Calorimetry</topic><topic>Carbonyl compounds</topic><topic>Carbonyls</topic><topic>Circular dichroism</topic><topic>Copper</topic><topic>Cytochrome</topic><topic>Cytochrome c</topic><topic>Cytochromes</topic><topic>Detoxification</topic><topic>Diabetes 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treatment</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2020-04-30</date><risdate>2020</risdate><volume>15</volume><issue>4</issue><spage>e0232408</spage><epage>e0232408</epage><pages>e0232408-e0232408</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Mitochondria are quantitatively the most important sources of reactive oxygen species (ROS) which are formed as by-products during cellular respiration. ROS generation occurs when single electrons are transferred to molecular oxygen. This leads to a number of different ROS types, among them superoxide. Although most studies focus on ROS generation in the mitochondrial matrix, the intermembrane space (IMS) is also important in this regard. The main scavengers for the detoxification of superoxide in the IMS are Cu, Zn superoxide dismutase (SOD1) and cytochrome-c. Similar to ROS, certain reactive carbonyl species are known for their high reactivity. The consequences are deleterious modifications to essential components compromising cellular functions and contributing to the etiology of severe pathological conditions like cancer, diabetes and neurodegeneration. In this study, we investigated the susceptibility of SOD1 and cytochrome-c to in vitro glycation by the dicarbonyl methylglyoxal (MGO) and the resulting effects on their structure. We utilized experimental techniques like immunodetection of the MGO-mediated modification 5-hydro-5-methylimidazolone, differential scanning calorimetry, fluorescence emission and circular dichroism measurements. We found that glycation of cytochrome-c leads to monomer aggregation, an altered secondary structure (increase in alpha helical content) and slightly more compact folding. In addition to structural changes, glycated cytochrome-c displays an altered thermal unfolding behavior. Subjecting SOD1 to MGO does not influence its secondary structure. However, similar to cytochrome-c, subunit aggregation is observed under denaturating conditions. Furthermore, the appearance of a second peak in the calorimetry diagram indirectly suggests de-metallation of SOD1 when high MGO levels are used. In conclusion, our data demonstrate that MGO has the potential to alter several structural parameters in important proteins of energy metabolism (cytochrome-c) and antioxidant defense (cytochrome-c, SOD1).</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>32353034</pmid><doi>10.1371/journal.pone.0232408</doi><orcidid>https://orcid.org/0000-0002-2924-7547</orcidid><orcidid>https://orcid.org/0000-0002-2602-660X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Age Agglomeration Antioxidants Binding sites Biology and Life Sciences Calorimetry Carbonyl compounds Carbonyls Circular dichroism Copper Cytochrome Cytochrome c Cytochromes Detoxification Diabetes mellitus Dichroism Differential scanning calorimetry Emission measurements Energy metabolism Enzymes Etiology Experiments Fluorescence Glycosylation Heat measurement Metabolism Mitochondria Mutation Neurodegeneration Oxygen Physical Sciences Protein structure Proteins Pyruvaldehyde Reactive oxygen species Research and Analysis Methods Scavengers Secondary structure Single electrons Superoxide dismutase |
| title | Analyzing structural alterations of mitochondrial intermembrane space superoxide scavengers cytochrome-c and SOD1 after methylglyoxal treatment |
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