Iron catalysis of lipid peroxidation in ferroptosis: Regulated enzymatic or random free radical reaction?
Stoyanovsky D. A., Tyurina Y. Y., Shrivastava I., Bahar I., Tyurin V. A., Protchenko O., Jadhav S., Bolevich S., Kozlov A. V., Vladimirov Yu. A., Shvedova A. A., Philpott C. C., Bayir H., Kagan V. E.
Free Radical Biology & Medicine
Vol.133, P. 153-161
Опубликовано: 2019
Тип ресурса: Обзор
DOI:10.1016/j.freeradbiomed.2018.09.008
Аннотация:
Duality of iron as an essential cofactor of many enzymatic metabolic processes and as a catalyst of poorly controlled redox-cycling reactions defines its possible biological beneficial and hazardous role in the body. In this review, we discuss these two “faces” of iron in a newly conceptualized program of regulated cell death, ferroptosis. Ferroptosis is a genetically programmed iron-dependent form of regulated cell death driven by enhanced lipid peroxidation and insufficient capacity of thiol-dependent mechanisms (glutathione peroxidase 4, GPX4) to eliminate hydroperoxy-lipids. We present arguments favoring the enzymatic mechanisms of ferroptotically engaged non-heme iron of 15-lipoxygenases (15-LOX) in complexes with phosphatidylethanolamine binding protein 1 (PEBP1) as a catalyst of highly selective and specific oxidation reactions of arachidonoyl- (AA) and adrenoyl-phosphatidylethanolamines (PE). We discuss possible role of iron chaperons as control mechanisms for guided iron deliv
Ключевые слова:
15-lipoxygenase; Ferroptosis; Glutathione; GPX4; Hydroperoxy-arachidonoyl-phosphatidylethanolamine; Iron; Iron chaperons; Lipid peroxidation
arachidonate 15 lipoxygenase; electrophile; free radical; iron; phosphatidylethanolamine; phosphatidylethanolamine binding protein; phosphatidylethanolamine binding protein 1; phospholipid hydroperoxide glutathione peroxidase; thiol; unclassified drug; arachidonate 15 lipoxygenase; iron; PEBP1 protein, human; phosphatidylethanolamine binding protein; phospholipid hydroperoxide glutathione peroxidase; catalysis; cell death; cell metabolism; enzyme mechanism; enzyme regulation; ferroptosis; human; lipid peroxidation; nonhuman; nucleophilicity; oxidation; oxidation reduction reaction; priority journal; protein analysis; protein cleavage; protein protein interaction; radical reaction; Review; animal; ferroptosis; genetics; lipid peroxidation; metabolism; Animals; Arachidonate 15-Lipoxygenase; Ferroptosis; Free Radicals; Humans; Iron; Lipid Peroxidation; Oxidation-Reduction; Phosphatidylethanolamine Binding Protein; Phospholipid Hydroperoxide Glutathione Peroxidase
Язык текста: Английский
ISSN: 1873-4596
Stoyanovsky D. A.
Tyurina Y. Y.
Shrivastava I.
Bahar I.
Tyurin V. A.
Protchenko O.
Jadhav S.
Bolevich S. Sergej 1964-
Kozlov A. V. Andrej Viktorovich 0001-
Vladimirov Yu. A. Yurij Andreevich 1932-
Shvedova A. A.
Philpott C. C.
Bayir H.
Kagan V. E. Valerian E 1946-
Стояновскy Д. А.
Тюрина Y. Y.
Шривастава И.
Бахар И.
Тюрин В. А.
Протченко О.
Йадхав С.
Болевич С. Сергей 1964-
Козлов А. В. Андрей Викторович 0001-
Владимиров Ю. А. Юрий Андреевич 1932-
Шведова А. А.
Пхилпотт C. C.
Байир Х.
Каган В. Е. Валериан Е 1946-
Iron catalysis of lipid peroxidation in ferroptosis: Regulated enzymatic or random free radical reaction?
Текст визуальный непосредственный
Free Radical Biology & Medicine
Elsevier Science Publisher B.V.
Vol.133 P. 153-161
2019
Обзор
15-lipoxygenase Ferroptosis Glutathione GPX4 Hydroperoxy-arachidonoyl-phosphatidylethanolamine Iron Iron chaperons Lipid peroxidation
arachidonate 15 lipoxygenase electrophile free radical iron phosphatidylethanolamine phosphatidylethanolamine binding protein phosphatidylethanolamine binding protein 1 phospholipid hydroperoxide glutathione peroxidase thiol unclassified drug arachidonate 15 lipoxygenase iron PEBP1 protein, human phosphatidylethanolamine binding protein phospholipid hydroperoxide glutathione peroxidase catalysis cell death cell metabolism enzyme mechanism enzyme regulation ferroptosis human lipid peroxidation nonhuman nucleophilicity oxidation oxidation reduction reaction priority journal protein analysis protein cleavage protein protein interaction radical reaction Review animal ferroptosis genetics lipid peroxidation metabolism Animals Arachidonate 15-Lipoxygenase Ferroptosis Free Radicals Humans Iron Lipid Peroxidation Oxidation-Reduction Phosphatidylethanolamine Binding Protein Phospholipid Hydroperoxide Glutathione Peroxidase
Duality of iron as an essential cofactor of many enzymatic metabolic processes and as a catalyst of poorly controlled redox-cycling reactions defines its possible biological beneficial and hazardous role in the body. In this review, we discuss these two “faces” of iron in a newly conceptualized program of regulated cell death, ferroptosis. Ferroptosis is a genetically programmed iron-dependent form of regulated cell death driven by enhanced lipid peroxidation and insufficient capacity of thiol-dependent mechanisms (glutathione peroxidase 4, GPX4) to eliminate hydroperoxy-lipids. We present arguments favoring the enzymatic mechanisms of ferroptotically engaged non-heme iron of 15-lipoxygenases (15-LOX) in complexes with phosphatidylethanolamine binding protein 1 (PEBP1) as a catalyst of highly selective and specific oxidation reactions of arachidonoyl- (AA) and adrenoyl-phosphatidylethanolamines (PE). We discuss possible role of iron chaperons as control mechanisms for guided iron deliv