Antioxidant and prooxidant modulation of lipid peroxidation by integral membrane proteins

Hajieva, Parvana; Abrosimov, Roman; Kunath, Sascha; Moosmann, Bernd

doi:10.1080/10715762.2023.2201391

Cited by 10 publications

(11 citation statements)

References 85 publications

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“…Radical propagation can also be effectively terminated by redox processes involving nonlipid molecules, including antioxidants such as α-tocopherol, − squalenes, hydropersulfides, and tryptophan and tyrosine residues in transmembrane proteins …”

Section: Oxidationmentioning

confidence: 99%

“…Cysteine, methionine and glutathione are potential sources of sulfur-centered radicals in vivo . , Cysteine has a low abundance in the transmembrane regions of proteins, and it has been suggested that its presence may act to accelerate propagation, noting that lipophilic thiols generally accelerate peroxidation and isomerization reactions . Aside from thiyl radical formation by hydrogen transfer to allylic radicals, pulse radiolysis experiments with Cys suggest that the intermediate thiyl radical ( 130 , Scheme ) undergoes 1,2- and 1,3-hydrogen shifts. , In the latter case, subsequent β-scission generates dehydroalanine ( 132 ) and a sulfhydryl radical ( 133 ).…”

Section: Isomerizationmentioning

confidence: 99%

“…375 Radical propagation can also be effectively terminated by redox processes involving nonlipid molecules, including antioxidants such as α-tocopherol, 376−382 squalenes, 383 hydropersulfides, 380 and tryptophan and tyrosine residues in transmembrane proteins. 384 Secondary Processes. Hydroperoxides (21) constitute the major primary products of fatty acid oxidation.…”

mentioning

confidence: 99%

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The Chemical Reactivity of Membrane Lipids

Duché,

Sanderson

2024

Chem. Rev.

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It is well-known that aqueous dispersions of phospholipids spontaneously assemble into bilayer structures. These structures have numerous applications across chemistry and materials science and form the fundamental structural unit of the biological membrane. The particular environment of the lipid bilayer, with a water-poor low dielectric core surrounded by a more polar and better hydrated interfacial region, gives the membrane particular biophysical and physicochemical properties and presents a unique environment for chemical reactions to occur. Many different types of molecule spanning a range of sizes, from dissolved gases through small organics to proteins, are able to interact with membranes and promote chemical changes to lipids that subsequently affect the physicochemical properties of the bilayer. This Review describes the chemical reactivity exhibited by lipids in their membrane form, with an emphasis on conditions where the lipids are well hydrated in the form of bilayers. Key topics include the following: lytic reactions of glyceryl esters, including hydrolysis, aminolysis, and transesterification; oxidation reactions of alkenes in unsaturated fatty acids and sterols, including autoxidation and oxidation by singlet oxygen; reactivity of headgroups, particularly with reactive carbonyl species; and E/Z isomerization of alkenes. The consequences of reactivity for biological activity and biophysical properties are also discussed. CONTENTS

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Section: Oxidationmentioning

confidence: 99%

Section: Isomerizationmentioning

confidence: 99%

mentioning

confidence: 99%

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The Chemical Reactivity of Membrane Lipids

Duché,

Sanderson

2024

Chem. Rev.

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“…. DHLA (dihydrolipoate, a lipid soluble thiol) protects against microsomal lipid peroxidation in the presence of vitamin E." The spectrum of molecules protective against lipid peroxidation has recently been extended to include redoxactive proteins (with tryptophan and tyrosine moieties) embedded in lipid membranes (19). Protection of liposomal lipids against radiation-induced oxidative damage was demonstrated in 1979 using a-tocopherol even without the "recyclers" or embedded proteins noted above (20).…”

Section: Models Of Lipid Peroxidationmentioning

confidence: 99%

Radiation-Chemical Perspective of the Radiobiology of Pulsed (High Dose-Rate) Radiation (FLASH): A Postscript

Wardman

2023

Radiation Research

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An earlier commentary (Wardman P, Radiat Res. 2020; 194:607-617) discussed possible chemical reaction pathways that might be involved in the differential responses of tissues to high- vs. low-dose-rate irradiation, focusing on reactions between radicals, and radiolytic depletion of a chemical influencing radiosensitivity. This brief postscript updates discussion to consider recent modeling and experimental studies, and presents more detail to support the earlier suggestion that rapid depletion of nitric oxide will certainly occur after a radiation pulse of a few grays, underlining the need to include the consequences of such a change when considering FLASH effects.

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“…The former may arise when a major or minor route of oxidation leads to irreparable damage of the protein or its surroundings, such as during protein cysteine thiyl radical formation [ 5 , 6 ], which appears to account for the avoidance of mitochondrial membrane cysteines in long-lived animal species [ 7 , 8 , 9 ]. Cysteine thiyl radicals can relay damage into the interior of proteins [ 10 ] and act as chain-transfer catalysts in vivo [ 5 ]; they are incompletely scavenged by aqueous antioxidants like ascorbate and glutathione [ 5 , 6 , 11 ], and no efficient system seems to exist for their scavenging in hydrophobic environments [ 6 , 12 ]. Thus, cysteine one-electron oxidation or a related type of oxidation may account at least in part for the very low degree of conservation of solitary surface cysteine residues, as opposed to paired cysteine residues, in the general proteome [ 13 , 14 ], since disulfides are much more resistant to one-electron oxidation and less damaging in the one-electron oxidized state than free thiol groups [ 6 , 11 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

Cysteine Is the Only Universally Affected and Disfavored Proteomic Amino Acid under Oxidative Conditions in Animals

Schindeldecker,

Moosmann

2024

Antioxidants

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Oxidative modifications of amino acid side chains in proteins are a hallmark of oxidative stress, and they are usually regarded as structural damage. However, amino acid oxidation may also have a protective effect and may serve regulatory or structural purposes. Here, we have attempted to characterize the global redox role of the 20 proteinogenic amino acids in animals by analyzing their usage frequency in 5 plausible evolutionary paradigms of increased oxidative burden: (i) peroxisomal proteins versus all proteins, (ii) mitochondrial proteins versus all proteins, (iii) mitochondrially encoded respiratory chain proteins versus all mitochondrial proteins, (iv) proteins from long-lived animals versus those from short-lived animals, and (v) proteins from aerobic, free-living animals versus those from facultatively anaerobic animals. We have found that avoidance of cysteine in the oxidative condition was the most pronounced and significant variation in the majority of comparisons. Beyond this preeminent pattern, only local signals were observed, primarily increases in methionine and glutamine as well as decreases in serine and proline. Hence, certain types of cysteine oxidation appear to enforce its proteome-wide evolutionary avoidance despite its essential role in disulfide bond formation and metal ligation. The susceptibility to oxidation of all other amino acids appears to be generally unproblematic, and sometimes advantageous.

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Antioxidant and prooxidant modulation of lipid peroxidation by integral membrane proteins

Cited by 10 publications

References 85 publications

The Chemical Reactivity of Membrane Lipids

The Chemical Reactivity of Membrane Lipids

Radiation-Chemical Perspective of the Radiobiology of Pulsed (High Dose-Rate) Radiation (FLASH): A Postscript

Cysteine Is the Only Universally Affected and Disfavored Proteomic Amino Acid under Oxidative Conditions in Animals

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