The DOI matches its Crossref record; 33 of the 35 references it cites were found in a registry or an index.
Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein
Open accessAbstract
Malondialdehyde (MDA) and 4-hydroxynonenal (HNE) are major end-products of oxidation of polyunsaturated fatty acids, and are frequently measured as indicators of lipid peroxidation and oxidative stress in vivo. MDA forms Schiff-base adducts with lysine residues and cross-links proteins in vitro; HNE also reacts with lysines, primarily via a Michael addition reaction. We have developed methods using NaBH4 reduction to stabilize these adducts to conditions used for acid hydrolysis of protein, and have prepared reduced forms of lysine-MDA [3-(Nε-lysino)propan-1-ol (LM)], the lysine-MDA-lysine iminopropene cross-link [1,3-di(Nε-lysino)propane (LML)] and lysine-HNE [3-(Nε-lysino)-4-hydroxynonan-1-ol (LHNE)]. Gas chromatography/MS assays have been developed for quantification of the reduced compounds in protein. RNase incubated with MDA or HNE was used as a model for quantification of the adducts by gas chromatography/MS. There was excellent agreement between measurement of MDA bound to RNase as LM and LML, and as thiobarbituric acid-MDA adducts measured by HPLC; these adducts accounted for 70Ő80% of total lysine loss during the reaction with MDA. LM and LML (0.002Ő0.12mmol/mol of lysine) were also found in freshly isolated low-density lipoprotein (LDL) from healthy subjects. LHNE was measured in RNase treated with HNE, but was not detectable in native LDL. LM, LML and LHNE increased in concert with the formation of conjugated dienes during the copper-catalysed oxidation of LDL, but accounted for modification of < 1% of lysine residues in oxidized LDL. These results are the first report of direct chemical measurement of MDA and HNE adducts to lysine residues in LDL. LM, LML and LHNE should be useful as biomarkers of lipid peroxidative modification of protein and of oxidative stress in vitro and in vivo.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“To our knowledge, MDA modified proteins have not been used as biomarkers in recent clinical investigations although antibodies are commercially available and highly selective MS methods have been established, previously [57].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [57]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“This positive partial charge is attacked by nucleophiles such as cysteine and histidine and stable Michael adducts are formed (Fig. 4B) [50]. Nucleophilic attack of lysine forms unstable Michael adducts, which require reduction, e.g., by sodium borohydride prior to analysis [57].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [57]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672
Janero, D. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90131-2 · Cited by 2,735
Role of oxidized low density lipoprotein in atherogenesis.
Witztum, J. L., & Steinberg, D. H. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115499 · Cited by 2,675
The role of lipid peroxidation and antioxidants in oxidative modification of LDL
Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307
Ylä‐Herttuala, S., Palinski, W., Rosenfeld, M. E., Parthasarathy, S., Carew, T. E., Butler, S. S., Witztum, J. L., & Steinberg, D. H. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114271 · Cited by 1,877
Autoantibody against oxidised LDL and progression of carotid atherosclerosis
Salonen, J. T., Korpela, H., Salonen, R., Nyyssönen, K., Ylä‐Herttuala, S., Yamamoto, R., Butler, S., Palinski, W., & Witztum, J. L. (1992) · The Lancet · doi:10.1016/0140-6736(92)90926-t · Cited by 1,311
Fu, M.-X., Requena, J. R., Jenkins, A. J., Lyons, T. J., Baynes, J. W., & Thorpe, S. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.9982 · Cited by 822
Self-citationSteinbrecher, U. P. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61395-x · Cited by 618
Palinski, W., Ylä‐Herttuala, S., Rosenfeld, M. E., Butler, S. W., Socher, S. S., Parthasarathy, S., Curtiss, L. K., & Witztum, J. L. (1990) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.10.3.325 · Cited by 616
Research works printed but not linked: 2
- Fruebis, J., Parthasarathy, S. and Steinberg, D. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 10588-10592
- Sell, D. R. and Monnier, V. M. (1989) in Physiology of Aging (Masero, E. J., ed.), pp. 235-305, Oxford University Press, New York
Cited by
Sorted by citations
Antioxidant enzymes and human diseases
MatÉs, J. M., Pérez-Gómez, C., & De Castro, I. N. (1999) · Clinical Biochemistry · doi:10.1016/s0009-9120(99)00075-2 · Cited by 2,099
Maness, P., Smolinski, S. L., Blake, D. M., Huang, Z. Q., Wolfrum, E. J., & Jacoby, W. A. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.9.4094-4098.1999 · Cited by 1,411
Measurement of Lipid Peroxidation
Moore, K. P., & Roberts, L. J. (1998) · Free Radical Research · doi:10.3109/10715769809065821 · Cited by 773
QUANTIFICATION AND SIGNIFICANCE OF PROTEIN OXIDATION IN BIOLOGICAL SAMPLES*
Shacter, E. B. (2000) · Drug Metabolism Reviews · doi:10.1081/dmr-100102336 · Cited by 748
Protein Oxidation: Basic Principles and Implications for Meat Quality
Zhang, W., Xiao, S., & Ahn, D. U. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.577540 · Cited by 736
Metadata
- Authors
- REQUENA, J. R., FU, M. X., AHMED, M. U., JENKINS, A. J., LYONS, T. J., BAYNES, J. W., & THORPE, S. R.
- Affiliations
- University of South Carolina (US)
- Medical University of South Carolina (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-02-15
- Volume
- 322
- Issue
- 1
- Pages
- 317-325
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1218194
- OpenAlex
- W1843398852
- Cited by
- 293
- References
- 35
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 3 · 2023: 13 · 2022: 7 · 2021: 6 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 9 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 11 · 2012: 14
- FWCI
- 10.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Scholar Commons (University of South Carolina) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Funders
- National Institutes of Health (5r01ag011472-04)
- National Institute on Aging (AG-11472)
- National Eye Institute (5R29 EY10697, R29EY010697)
- Topics
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Paraoxonase enzyme and polymorphisms
- Keywords
- malondialdehyde, 4-hydroxynonenal, lipid peroxidation, lysine adducts, low-density lipoprotein, protein oxidation, Schiff base adducts, Michael addition, sodium borohydride reduction, oxidative stress biomarkers, conjugated dienes, protein cross-linking
- MeSH terms
- Aldehydes, Amino Acids, Collagen, Copper, Crystallins, Drug Stability, Humans, Lipoproteins, LDL, Lysine, Malondialdehyde, Gas Chromatography-Mass Spectrometry, Oxidation-Reduction, Ribonucleases, Schiff Bases, Skin, Lipid Peroxidation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
