Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein
Acrolein is the most reactive aldehydic product of lipidperoxidation and is found to be elevated in the brain whenoxidative stress is high. The effects of acrolein on the structureand function of human Cu,Zn-superoxide dismutase (SOD) wereexamined. When Cu,Zn-SOD was incubated with acrolein, thecova...
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| Format: | Article |
| Language: | English |
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Korean Society for Biochemistry and Molecular Biology
2013-11-01
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| Series: | BMB Reports |
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| Online Access: | http://bmbreports.org/jbmb/pdf.php?data=MTMxMTI3MThAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0xMSU1RDEzMTEyNzE4MjhfJTI4NTU1LTU2MCUyOUJNQl8xMy0xMzgucGRm |
| _version_ | 1819208068853923840 |
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| author | Jung Hoon Kang |
| author_facet | Jung Hoon Kang |
| author_sort | Jung Hoon Kang |
| collection | DOAJ |
| description | Acrolein is the most reactive aldehydic product of lipidperoxidation and is found to be elevated in the brain whenoxidative stress is high. The effects of acrolein on the structureand function of human Cu,Zn-superoxide dismutase (SOD) wereexamined. When Cu,Zn-SOD was incubated with acrolein, thecovalent crosslinking of the protein was increased, and the loss ofenzymatic activity was increased in a dose-dependent manner.Reactive oxygen species (ROS) scavengers and copper chelatorsinhibited the acrolein-mediated Cu,Zn-SOD modification and theformation of carbonyl compound. The present study shows thatROS may play a critical role in acrolein-induced Cu,Zn-SODmodification and inactivation. When Cu,Zn-SOD that has beenexposed to acrolein was subsequently analyzed by amino acidanalysis, serine, histidine, arginine, threonine and lysine residueswere particularly sensitive. It is suggested that the modificationand inactivation of Cu,Zn-SOD by acrolein could be produced bymore oxidative cell environments. [BMB Reports 2013; 46(11):555-560] |
| first_indexed | 2024-12-23T05:33:31Z |
| format | Article |
| id | doaj.art-c12dd1ffc4bd4d6e87b5f19b943da939 |
| institution | Directory Open Access Journal |
| issn | 1976-6696 1976-670X |
| language | English |
| last_indexed | 2024-12-23T05:33:31Z |
| publishDate | 2013-11-01 |
| publisher | Korean Society for Biochemistry and Molecular Biology |
| record_format | Article |
| series | BMB Reports |
| spelling | doaj.art-c12dd1ffc4bd4d6e87b5f19b943da9392022-12-21T17:58:25ZengKorean Society for Biochemistry and Molecular BiologyBMB Reports1976-66961976-670X2013-11-014611555560http://dx.doi.org/10.5483/BMBRep.2013.46.11.138Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acroleinJung Hoon KangAcrolein is the most reactive aldehydic product of lipidperoxidation and is found to be elevated in the brain whenoxidative stress is high. The effects of acrolein on the structureand function of human Cu,Zn-superoxide dismutase (SOD) wereexamined. When Cu,Zn-SOD was incubated with acrolein, thecovalent crosslinking of the protein was increased, and the loss ofenzymatic activity was increased in a dose-dependent manner.Reactive oxygen species (ROS) scavengers and copper chelatorsinhibited the acrolein-mediated Cu,Zn-SOD modification and theformation of carbonyl compound. The present study shows thatROS may play a critical role in acrolein-induced Cu,Zn-SODmodification and inactivation. When Cu,Zn-SOD that has beenexposed to acrolein was subsequently analyzed by amino acidanalysis, serine, histidine, arginine, threonine and lysine residueswere particularly sensitive. It is suggested that the modificationand inactivation of Cu,Zn-SOD by acrolein could be produced bymore oxidative cell environments. [BMB Reports 2013; 46(11):555-560]http://bmbreports.org/jbmb/pdf.php?data=MTMxMTI3MThAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0xMSU1RDEzMTEyNzE4MjhfJTI4NTU1LTU2MCUyOUJNQl8xMy0xMzgucGRmAcroleinCuZn-superoxide dismutaseLipid peroxidationReactive oxygen species |
| spellingShingle | Jung Hoon Kang Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein BMB Reports Acrolein Cu Zn-superoxide dismutase Lipid peroxidation Reactive oxygen species |
| title | Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein |
| title_full | Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein |
| title_fullStr | Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein |
| title_full_unstemmed | Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein |
| title_short | Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein |
| title_sort | modification and inactivation of cu zn superoxide dismutase by the lipid peroxidation product acrolein |
| topic | Acrolein Cu Zn-superoxide dismutase Lipid peroxidation Reactive oxygen species |
| url | http://bmbreports.org/jbmb/pdf.php?data=MTMxMTI3MThAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0xMSU1RDEzMTEyNzE4MjhfJTI4NTU1LTU2MCUyOUJNQl8xMy0xMzgucGRm |
| work_keys_str_mv | AT junghoonkang modificationandinactivationofcuznsuperoxidedismutasebythelipidperoxidationproductacrolein |