Cited by 813Advanced Glycation End Products researchProtein Kinase Regulation and GTPase SignalingNitric Oxide and Endothelin Effects

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Activation of the Receptor for Advanced Glycation End Products Triggers a p21 -dependent Mitogen-activated Protein Kinase Pathway Regulated by Oxidant Stress

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Lander, Harry M., Tauras, James M., Ogiste, Jason S., Hori, Osamu, Moss, Rebecca A., Schmidt, Ann Marie·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.28.17810

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Abstract

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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Arbeitsstoffe, D. F. S. S. Z. P. G., & Greim, H. (2015) · The MAK-Collection for Occupational Health and Safety · doi:10.1002/3527600418.mb10722e3814
Glycation
D’Agati, V. D., & Schmidt, A. M. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-153-6_8
Self-citation
Glyoxal [MAK Value Documentation in German language, 2004]
Makromolekülen, G. K. I. A. Z. D. O. –. V. I. N. R. –. A. V. B., Proteinen, C. V., & werden., K. S. M. D. S. G. (2012) · The MAK-Collection for Occupational Health and Safety · doi:10.1002/3527600418.mb10722d0038
Rôle de la glycation des protéines dans les complications et la thérapie du diabète: revue bibliographique
Anago, E., Djogbede, G., Fiogbe, E. M. S., Sègbo, G. J., & Akpovi, C. D. (2023) · International Journal of Biological and Chemical Sciences · doi:10.4314/ijbcs.v16i6.37 · Cited by 1
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Receptor for Advanced Glycation End Products in Various Types of Cancers
Rani, R., Malik, P., & Mukherjee, T. K. (2025) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815322521125010011
Additional file 1 of Association between endothelial function and skin advanced glycation end-products (AGEs) accumulation in a sample of predominantly young and healthy adults
Fewkes, J. J., Dordevic, A. L., Murray, M., Williamson, G., & Kellow, N. J. (2024) · Figshare · doi:10.6084/m9.figshare.26974420

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.
ORCID: Tauras, James M.
Hori, Osamu
Moss, Rebecca A.
Schmidt, Ann Marie
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-07
Volume: 272
Issue: 28
Pages: 17810-17814
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.28.17810
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8502 d)
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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Activation of the Receptor for Advanced Glycation End Products Triggers a p21 -dependent Mitogen-activated Protein Kinase Pathway Regulated by Oxidant Stress

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