The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
The myeloperoxidase system of human phagocytes generates Nε-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation
Open accessAbstract
Reactive aldehydes derived from reducing sugars and peroxidation of lipids covalently modify proteins and may contribute to oxidative tissue damage. We recently described another mechanism for generating reactive aldehydes from free alpha-amino acids. The pathway begins with myeloperoxidase, a heme enzyme secreted by activated neutrophils. Conversion of alpha-amino acids to aldehydes requires hypochlorous acid (HOCl), formed from H2O2 and chloride by myeloperoxidase. When L-serine is the substrate, HOCl generates high yields of glycolaldehyde. We now demonstrate that a model protein, ribonuclease A (RNase A), exposed to free L-serine and HOCl exhibits the biochemical hallmarks of advanced glycation end (AGE) products -- browning, increased fluorescence, and cross-linking. Furthermore, Nepsilon-(carboxymethyl)lysine (CML), a chemically well-characterized AGE product, was generated on RNase A when it was exposed to reagent HOCl-serine, the myeloperoxidase-H2O2-chloride system plus L-serine, or activated human neutrophils plus L-serine. CML production by neutrophils was inhibited by the H2O2 scavenger catalase and the heme poison azide, implicating myeloperoxidase in the cell-mediated reaction. CML was also generated on RNase A by a myeloperoxidase-dependent pathway when neutrophils were activated in a mixture of amino acids. Under these conditions, we observed both L-serine-dependent and L-serine-independent pathways of CML formation. The in vivo production of glycolaldehyde and other reactive aldehydes by myeloperoxidase may thus play an important pathogenic role by generating AGE products and damaging tissues at sites of inflammation.
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.
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
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
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
Role of Oxidative Stress in Development of Complications in Diabetes
Baynes, J. W. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,793
Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic Complications
Flier, J. S., Underhill, L. H., Brownlee, M., Cerami, A., & Vlassara, H. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805193182007 · Cited by 2,511
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417 · cited 2×
“To investigate the ability of different antioxidants to inhibit CML formation by the HOClserine system (40), we incubated L-serine together with equimolar concentrations of antioxidant and HOCl, added RNase A to the reaction mixture, and then quantified the levels of CML in the protein after a 24-hour incubation.”
BackgroundMethodThe role of oxidized lipoproteins in atherogenesis
Berliner, J. A., & Heinecke, J. W. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02173-6 · Cited by 1,366
Self-citationYan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y. S., Pinsky, D., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,306
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
Self-citationStructure Elucidation of a Senescence Cross-Link from Human Extracellular Matrix
Sell, D. R., & Monnier, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88225-8 · Cited by 1,081
Cited by
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Understanding RAGE, the receptor for advanced glycation end products
Bierhaus, A., Humpert, P. M., Morcos, M., Wendt, T., Chavakis, T., Arnold, B., Stern, D. M., & Nawroth, P. P. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0688-7 · Cited by 1,297
Kislinger, T., Fu, C., Huber, B., Qu, W., Taguchi, A., Du Yan, S., Hofmann, M., Yan, S. F., Pischetsrieder, M., Stern, D., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31740 · Cited by 869
Ramasamy, R., Vannucci, S. J., Yan, S. S. D., Herold, K., Yan, S. F., & Schmidt, A. M. (2005) · Glycobiology · doi:10.1093/glycob/cwi053 · Cited by 834
van Heerebeek, L., Hamdani, N., Handoko, M. L., Falcao-Pires, I., Musters, R. J., Kupreishvili, K., Ijsselmuiden, A. J. J., Schalkwijk, C. G., Bronzwaer, J. G. F., Diamant, M., et al. (2008) · Circulation · doi:10.1161/circulationaha.107.728550 · Cited by 723
Metadata
- Authors
- Anderson, M. M., Requena, J. R., Crowley, J. R., Thorpe, S. R., & Heinecke, J. W.
- Venue
- Journal of Clinical Investigation
- Published
- 1999-07-01
- Volume
- 104
- Issue
- 1
- Pages
- 103-113
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W2008219736
- Cited by
- 349
- References
- 61
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- bronze
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The myeloperoxidase system of human phagocytes generates Nε-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. https://app.cochat.ai/papers/10.1172/jci3042
- The paper
- Anderson, M. M., Requena, J. R., Crowley, J. R., Thorpe, S. R., & Heinecke, J. W. (1999). The myeloperoxidase system of human phagocytes generates Nε-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. Journal of Clinical Investigation. https://doi.org/10.1172/jci3042
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
