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Oxidative modification of human ceruloplasmin induced by a catechol neurotoxin, salsolinol

강정훈|김승섭|Jae Yoon Kang
생화학분자생물학회 (Korean Society Of Biochemistry And Molecular Biology)|2016.01|BMB Reports|제49권 제1호|pp. 45-50

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참고문헌

키워드

Reactive oxygen speciesCopperSalsolinolCeruloplasmin
주제분류화학

초록

Salsolinol (SAL), a compound derived from dopamine metabolism, is the most probable neurotoxin involved in the pathogenesis of Parkinson’s disease (PD). In this study, we investigated the modification and inactivation of human ceruloplasmin (hCP) induced by SAL. Incubation of hCP with SAL increased the protein aggregation and enzyme inactivation in a dose-dependent manner. Reactive oxygen species scavengers and copper chelators inhibited the SAL-mediated hCP modification and inactivation. The formation of dityrosine was detected in SAL-mediated hCP aggregates. Amino acid analysis post the exposure of hCP to SAL revealed that aspartate, histidine, lysine, threonine and tyrosine residues were particularly sensitive. Since hCP is a major copper transport protein, oxidative damage of hCP by SAL may induce perturbation of the copper transport system, which subsequently leads to deleterious conditions in cells. This study of the mechanism by which ceruloplasmin is modified by salsolinol may provide an explanation for the deterioration of organs under neurodegenerative disorders such as PD.

Abstract

Salsolinol (SAL), a compound derived from dopamine metabolism, is the most probable neurotoxin involved in the pathogenesis of Parkinson’s disease (PD). In this study, we investigated the modification and inactivation of human ceruloplasmin (hCP) induced by SAL. Incubation of hCP with SAL increased the protein aggregation and enzyme inactivation in a dose-dependent manner. Reactive oxygen species scavengers and copper chelators inhibited the SAL-mediated hCP modification and inactivation. The formation of dityrosine was detected in SAL-mediated hCP aggregates. Amino acid analysis post the exposure of hCP to SAL revealed that aspartate, histidine, lysine, threonine and tyrosine residues were particularly sensitive. Since hCP is a major copper transport protein, oxidative damage of hCP by SAL may induce perturbation of the copper transport system, which subsequently leads to deleterious conditions in cells. This study of the mechanism by which ceruloplasmin is modified by salsolinol may provide an explanation for the deterioration of organs under neurodegenerative disorders such as PD.

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관련 논문AI추천

Salsolinol, a catechol neurotoxin, induces oxidative modification of cytochrome c강정훈생화학분자생물학회 · BMB Reports2013 · 제46권 제2호Salsolinol, a tetrahydroisoquinoline-derived neurotoxin, induces oxidative modification of neurofilament-L: protection by histidyl dipeptides강정훈생화학분자생물학회 · BMB Reports2012 · 제45권 제2호Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein강정훈생화학분자생물학회 · BMB Reports2013 · 제46권 제11호Oxidative modification of ferritin induced by hydrogen peroxide강정훈, 이명선, Inn Goo Kyeong, Jung Hwan Yoon, Sang-Chul Kwon, Sung Ho An생화학분자생물학회 · BMB Reports2011 · 제44권 제3호Protective effects of carnosine and homocarnosine on ferritin and hydrogen peroxide-mediated DNA damage강정훈생화학분자생물학회 · BMB Reports2010 · 제43권 제10호Oxidative modification of ferritin induced by methylglyoxal강정훈, 이명선, Sung Ho An생화학분자생물학회 · BMB Reports2012 · 제45권 제3호

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