What Is Responsible for the Initiating Chemistry of Iron-Mediated Lipid Peroxidation:  An Update

Cheng, Zhiyong; Li, Yuanzong

doi:10.1021/cr040077w

Cited by 188 publications

(115 citation statements)

References 303 publications

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“…In addition to endothelial damage and thrombosis, patients with aHUS also experience intravascular hemolysis (27), leading to liberation of hemoglobin and iron into plasma. "Free" redox-active iron cannot only initiate but particularly efficiently catalyze lipid peroxidation (48,49), a source of MDA (1). Taken together, it is evident that MDA is formed in aHUS.…”

Section: Discussionmentioning

confidence: 99%

Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome

Hyvärinen

Uchida

Varjosalo

et al. 2014

Journal of Biological Chemistry

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Background: Malondialdehyde (MDA) released during oxidative stress modifies proteins covalently. Results: The C terminus of complement regulator factor H binds negative patches on MDA-modified proteins, and aHUSrelated mutations affect the interaction. Conclusion: Defects in factor H binding to MDA-modified surfaces might allow deleterious complement activation on them. Significance: MDA-modifications are potentially a new factor in aHUS pathogenesis.

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Section: Discussionmentioning

confidence: 99%

Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome

Hyvärinen

Uchida

Varjosalo

et al. 2014

Journal of Biological Chemistry

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“…The peroxidation of PUFAs in membranes generates toxic lipid hydroperoxides, resulting in the formation of lethal lipid radicals in the presence of ferrous iron, while inhibiting GPX4 (7,15,52). Lipid radicals react with adjacent PUFAs in lipid membranes and induce lipid peroxidation in ferroptosis.…”

Section: Ferroptosis Is Induced By Lipid Peroxidation Cell Lines Selmentioning

confidence: 99%

“…DFO chelates lysosomal iron, which should be present at a different location in the cell, promoting L-ROS production. In addition, lipophilic iron chelators are able to cross membranes and chelate the labile iron pool, which is critical for the fragmentation and peroxidation of PUFAs (22,23,52). Excess active iron donates electrons to generate ROS based on the Fenton reaction, promoting lipid peroxidation and the initiation of ferroptosis (54).…”

Section: Ferroptosis Is Induced By Lipid Peroxidation Cell Lines Selmentioning

confidence: 99%

Metabolic networks in ferroptosis (Review)

et al. 2018

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Abstract.Ferroptosis is an iron-dependent and peroxidation-driven form of cell death associated with multiple metabolic disorders and disrupted homeostasis. A number of metabolic processes and homeostasis are affected by ferroptosis. The molecules that regulate ferroptosis are involved in metabolic pathways that regulate cysteine exploitation, glutathione state, nicotinamide adenine dinucleotide phosphate function, lipid peroxidation and iron homeostasis. The present review summarizes the metabolic networks involved in ferroptosis based on previous studies, and discusses the function of ferroptosis in pathological processes, including cancer. Finally, the clinical significance of ferroptosis is highlighted, to provide evidence for further studies.

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“…Iron is a troublesome substrate in a reconstituted transport assay in proteoliposomes due to 1) its oxidation from 2+ to 3+ and subsequent precipitation and 2) its ability to catalyze lipid peroxidation, leading to leaky liposomes (28). Many of the common buffers used for biochemistry also coordinate iron, thus significantly affecting the molecular identity of the species available for transport (29).…”

mentioning

confidence: 99%

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

Christenson

Gallegos

Banerjee

2018

Journal of Biological Chemistry

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Mitoferrin-1 is a promiscuous transition metal transporterThe reactivity of iron is exploited across all kingdoms of life. The physiological roles that iron takes on are many-iron readily participates in redox reactions where it can donate or accept electrons, depending on its oxidation state. Iron plays essential roles in gas transport and sensing and can also act as a non-redox active metal ion cofactor in enzymes. Additionally, iron-containing cofactors can impart stability to folded proteins (1). Iron naturally occurs in the 2+ and the 3+ oxidation states but owing to the insolubility of Fe(III), the bioavailable form of iron is almost exclusively the 2+ form. The main route of cellular iron uptake is via the transferrin receptor pathway whereby transferrin-bound iron is targeted to endosomes and subsequently released from transferrin during endosomal acidification. Fe(II) is transported out of endosomes by divalent metal ion transporter (DMT1) and becomes available for incorporation into iron-containing proteins and cofactors (2).In eukaryotes, mitochondria are the hotspots for iron utilization-these organelles house heme assembly and the majority of Fe-S cluster biosynthesis apparatus (3,4). Mitochondria contain respiratory complexes which comprise many ironcontaining cofactors. Not surprisingly, http://www.jbc.org/cgi

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What Is Responsible for the Initiating Chemistry of Iron-Mediated Lipid Peroxidation: An Update

Cited by 188 publications

References 303 publications

Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome

Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome

Metabolic networks in ferroptosis (Review)

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

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