Reactions of proteins with oxidizing lipids

Nielsen, Henrik Kofoed; Löliger, J.; Hurrell, Richard F.

doi:10.1079/bjn19850011

Cited by 61 publications

(8 citation statements)

References 36 publications

(33 reference statements)

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“…Met(O) can also be further oxidized to methionine sulfone, although this reaction occurs to a much lesser extent293031. Despite these well-known confounding factors regulating Met oxidation and the claimed technical difficulties associated with quantifying peptides containing Met and Met(O), the present study has indicated that [Met(O)]/[Met] of specific residues may be promising clinical biomarkers for oxidative stress.…”

Section: Discussionmentioning

confidence: 65%

Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress

Suzuki

Kodera

Saito

et al. 2016

Sci Rep

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Oxidative stress contributes to the pathophysiology of a variety of diseases, and circulating biomarkers of its severity remains a topic of great interest for researchers. Our peptidomic strategy enables accurate and reproducible analysis of circulating proteins/peptides with or without post-translational modifications. Conventional wisdom holds that hydrophobic methionines exposed to an aqueous environment or experimental handling procedures are vulnerable to oxidation. However, we show that the mass spectra intensity ratio of oxidized to non-oxidized methionine residues in serum tryptic proteins can be accurately quantified using a single drop of human serum and give stable and reproducible results. Our data demonstrate that two methionine residues in serum albumin (Met-111 and Met-147) are highly oxidized to methionine sulfoxide in patients with diabetes and renal failure and in healthy smokers versus non-smoker controls. This label-free mass spectrometry approach to quantify redox changes in methionine residues should facilitate the identification of additional circulating biomarkers suitable for predicting the development or progression of human diseases.

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Section: Discussionmentioning

confidence: 65%

Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress

Suzuki

Kodera

Saito

et al. 2016

Sci Rep

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“…Further oxidation products of methionine sulphoxide (e.g. the sulphone [93]) cannot be reversed by the reductase. Methionine oxidation and repair may be a biological control mechanism [94], analogous to reversible thiolation.…”

Section: Methioninementioning

confidence: 99%

Biochemistry and pathology of radical-mediated protein oxidation

Dean

Stocker

et al. 1997

Biochemical Journal

1,548

982

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Radical-mediated damage to proteins may be initiated by electron leakage, metal-ion-dependent reactions and autoxidation of lipids and sugars. The consequent protein oxidation is O2-dependent, and involves several propagating radicals, notably alkoxyl radicals. Its products include several categories of reactive species, and a range of stable products whose chemistry is currently being elucidated. Among the reactive products, protein hydroperoxides can generate further radical fluxes on reaction with transition-metal ions; protein-bound reductants (notably dopa) can reduce transition-metal ions and thereby facilitate their reaction with hydroperoxides; and aldehydes may participate in Schiff-base formation and other reactions. Cells can detoxify some of the reactive species, e.g. by reducing protein hydroperoxides to unreactive hydroxides. Oxidized proteins are often functionally inactive and their unfolding is associated with enhanced susceptibility to proteinases. Thus cells can generally remove oxidized proteins by proteolysis. However, certain oxidized proteins are poorly handled by cells, and together with possible alterations in the rate of production of oxidized proteins, this may contribute to the observed accumulation and damaging actions of oxidized proteins during aging and in pathologies such as diabetes, atherosclerosis and neurodegenerative diseases. Protein oxidation may also sometimes play controlling roles in cellular remodelling and cell growth. Proteins are also key targets in defensive cytolysis and in inflammatory self-damage. The possibility of selective protection against protein oxidation (antioxidation) is raised.

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“…Frying of fish resulted in maximum loss of lysine and sulphur amino acids. The most labile amino acids during damage to proteins by peroxidized lipids are methionine, histidine, cysteine and lysine [10,11]. Rafalski et al [12] reported that peroxidized linoleic acid reacts selectively with the sulphur amino acids.…”

Section: Resultsmentioning

confidence: 99%

Repeated use of oil for frying fish. Effects of feeding the fried fish to rats

Ammu¹,

Raghunath

Sankar

et al. 2000

Nahrung

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Four groups of weanling male albino rats (Wistar strain) were fed isonitrogenous diet (10% protein) identical in all respects except in the nature of the protein source, for 4 weeks. Control group (group 1) had steamed mackerel meat as the protein source, whereas groups 2, 3 and 4 had mackerel fried on the 1st, 3rd and 4th days in the same coconut oil repeatedly used for frying each day. Four groups of adult male rats weighing around 130 g were fed on the same diet for 12 weeks. Weanlings fed on fish fried on the 4th day showed significantly lower feed consumption and weight gain compared to the other three groups. All the three groups of adult rats fed on fried fish compared well with control rats in weight gain and hepatosomatic index. There was a decrease in the total lipid and cholesterol content of the liver of rats fed with fried fish in comparison with the control rats. The total lipid and cholesterol in heart and serum cholesterol levels increased significantly from control rats through group 4. The C22:6/C20:5 ratio in the heart lipid showed a very high value compared to the dietary lipids. Histopathological examination showed initial stages of cell damage in the liver and kidney of rats fed with fish fried on the 4th day. In-vitro digestibility of proteins of fried fish were lower than that of steamed fish, but the difference in this respect between proteins of fish fried on different days was not significant.

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Reactions of proteins with oxidizing lipids

Cited by 61 publications

References 36 publications

Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress

Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress

Biochemistry and pathology of radical-mediated protein oxidation

Repeated use of oil for frying fish. Effects of feeding the fried fish to rats

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