The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Activation of the Receptor for Advanced Glycation End Products Triggers a p21 -dependent Mitogen-activated Protein Kinase Pathway Regulated by Oxidant Stress
Open accessAbstract
Advanced glycation end products (AGEs) exert their cellular effects on cells by interacting with specific cellular receptors, the best characterized of which is the receptor for AGE (RAGE). The transductional processes by which RAGE ligation transmits signals to the nuclei of cells is unknown and was investigated. AGE-albumin, a prototypic ligand, activated p21(ras) in rat pulmonary artery smooth muscle cells that express RAGE, whereas nonglycated albumin was without effect. MAP kinase activity was enhanced at concentrations of AGE-albumin, which activated p21(ras) and NF-kappaB. Depletion of intracellular glutathione rendered cells more sensitive to AGE-mediated activation of this signaling pathway. In contrast, signaling was blocked by preventing p21(ras) from associating with the plasma membrane or mutating Cys118 on p21(ras) to Ser. Signaling was receptor-dependent, because it was prevented by blocking access to RAGE with either anti-RAGE IgG or by excess soluble RAGE. These data suggest that RAGE-mediated induction of cellular oxidant stress triggers a cascade of intracellular signals involving p21(ras) and MAP kinase, culminating in transcription factor activation. The molecular mechanism that triggers this pathway likely involves oxidant modification and activation of p21(ras).
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“Increases in the levels of circulating TNF-a, IL-6, IL-2R and CRP are also strong predictors of all-cause mortality risk in longitudinal studies of several elderly cohorts (190 -193) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [192]
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“AGEs activate the ERK, c-Jun N-terminal kinase (JNK), p38, and PI3K pathways and promote activation of NF-κB.”
From The Vasculature in Prediabetes (2018) · cites this paper as [59]
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Metadata
- Authors
- Lander, H. M., Tauras, J. M., Ogiste, J. S., Hori, O., Moss, R. A., & Schmidt, A. M.
- Affiliations
- Cornell University (US)
- Columbia University Irving Medical Center (US)
- Corresponding author
- Lander, Harry M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-07
- Volume
- 272
- Issue
- 28
- Pages
- 17810-17814
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2047964022
- Cited by
- 813
- References
- 34
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 11 · 2023: 14 · 2022: 13 · 2021: 12 · 2020: 14 · 2019: 9 · 2018: 19 · 2017: 26 · 2016: 24 · 2015: 28 · 2014: 31 · 2013: 32 · 2012: 36
- FWCI
- 14.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- National Institutes of Health (5r29ai037637-02, 5r01gm055509-03)
- National Institute on Aging (AG00602)
- National Institute of General Medical Sciences (GM55509)
- National Institute of Allergy and Infectious Diseases (AI37637)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- advanced glycation end products, receptor for advanced glycation end products, RAGE, p21ras, MAPK signaling, oxidative stress, glutathione depletion, NF-κB activation, pulmonary artery smooth muscle cells, receptor tyrosine kinase signaling
- MeSH terms
- Receptor for Advanced Glycation End Products, Animals, Enzyme Activation, Glutathione, Receptors, Immunologic, Transferases, Signal Transduction, PC12 Cells, Glycation End Products, Advanced, Calcium-Calmodulin-Dependent Protein Kinases, Oxidative Stress, Alkyl and Aryl Transferases, Rats
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