The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Modifications of proteins by polyunsaturated fatty acid peroxidation products
Open accessAbstract
The ability of unsaturated fatty acid methyl esters to modify amino acid residues in bovine serum albumin (BSA), glutamine synthetase, and insulin in the presence of a metal-catalyzed oxidation system [ascorbate/Fe(III)/O 2 ] depends on the degree of unsaturation of the fatty acid. The fatty acid-dependent generation of carbonyl groups and loss of lysine residues increased in the order methyl linoleate < methyl linolenate < methyl arachidonate. The amounts of alkyl hydroperoxides, malondialdehyde, and a number of other aldehydes that accumulated when polyunsaturated fatty acids were oxidized in the presence of BSA were significantly lower than that observed in the absence of BSA. Direct treatment of proteins with various lipid hydroperoxides led to a slight increase in the formation of protein carbonyl derivatives, whereas treatment with the hydroperoxides together with Fe(II) led to a substantial increase in the formation of protein carbonyls. These results are consistent with the proposition that metal-catalyzed oxidation of polyunsaturated fatty acids can contribute to the generation of protein carbonyls by direct interaction of lipid oxidation products (α,β-unsaturated aldehydes) with lysine residues (Michael addition reactions) and also by interactions with alkoxyl radicals obtained by Fe(II) cleavage of lipid hydroperoxides that are formed. In addition, saturated aldehydes derived from the polyunsaturated fatty acids likely react with lysine residues to form Schiff base adducts.
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Cites
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
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Self-citationLipid hydroperoxide generation, turnover, and effector action in biological systems
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Activation of Stress Signaling Pathways by the End Product of Lipid Peroxidation
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Cited by
Protein carbonylation, cellular dysfunction, and disease progression
Dalle-Donne, I., Aldini, G., Carini, M., Colombo, R., Rossi, R., & Milzani, A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00407.x · Cited by 831
Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress
Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 745
Biomedicine Meets Fenton Chemistry
Tang, Z., Zhao, P., Wang, H., Liu, Y., & Bu, W. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00977 · Cited by 745
Protein Oxidation in Aging and Age‐Related Diseases
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Self-citationPlatelet activation in type 2 diabetes mellitus
Ferroni, P., Basili, S., Falco, A., & Davì, G. (2004) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2004.00836.x · Cited by 493
Metadata
- Authors
- Refsgaard, H. H. F., Tsai, L., & Stadtman, E. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-18
- Volume
- 97
- Issue
- 2
- Pages
- 611-616
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2049126986
- Cited by
- 329
- References
- 38
- FWCI
- 8.76
- Type
- journal article
- Language
- en
- Open access
- green
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