Cited by 1,151Advanced Glycation End Products researchConnective Tissue Growth Factor ResearchGalectins and Cancer Biology

The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin

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Hori, Osamu, Brett, Jerold, Slattery, Timothy, Cao, Rong, Zhang, Jinghua, Chen, Jing Xian, Nagashima, Mariko, Lundh, Erik R. +5 more·1995·Journal of Biological Chemistry

Abstract

The receptor for advanced glycation end products (RAGE), a newly-identified member of the immunoglobulin superfamily, mediates interactions of advanced glycation end product (AGE)-modified proteins with endothelium and other cell types. Survey of normal tissues demonstrated RAGE expression in situations in which accumulation of AGEs would be unexpected, leading to the hypothesis that under physiologic circumstances, RAGE might mediate interaction with ligands distinct from AGEs. Sequential chromatography of bovine lung extract identified polypeptides with M(r) values of approximately 12,000 (p12) and approximately 23,000 (p23) which bound RAGE. NH2-terminal and internal protein sequence data for p23 matched that reported previously for amphoterin. Amphoterin purified from rat brain or recombinant rat amphoterin bound to purified sRAGE in a saturable and dose-dependent manner, blocked by anti-RAGE IgG or a soluble form of RAGE (sRAGE). Cultured embryonic rat neurons, which express RAGE, displayed dose-dependent binding of 125I-amphoterin which was prevented by blockade of RAGE using antibody to the receptor or excess soluble receptor (sRAGE). A functional correlate of RAGE-amphoterin interaction was inhibition by anti-RAGE F(ab')2 and sRAGE of neurite formation by cortical neurons specifically on amphoterin-coated substrates. Consistent with a potential role for RAGE-amphoterin interaction in development, amphoterin and RAGE mRNA/antigen were co-localized in developing rat brain. These data indicate that RAGE has physiologically relevant ligands distinct from AGEs which are likely, via their interaction with the receptor, to participate in physiologic processes outside of the context of diabetes and accumulation of AGEs.

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Crossref · 10.1074/jbc.270.43.25752

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  • RAGE recognizes HMGB1.

    “In addition to AGes, RAGe also recognizes HMGb193 and the S100 family members19, which are released during cellular stress and necrotic cell death, and β-amyloid94, the accumulation of which is pathogenic in Alzheimer's disease.”

    From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [93]

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Authors
Hori, O., Brett, J., Slattery, T., Cao, R., Zhang, J., Chen, J. X., Nagashima, M., Lundh, E. R., Vijay, S., Nitecki, D., Morser, J., Stern, D., & Schmidt, A. M.
Affiliations
Columbia University (US)
Corresponding author
Schmidt, Ann Marie
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-10
Volume
270
Issue
43
Pages
25752-25761
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2005640704
Cited by
1,151
References
32
Citations by year
2026: 22 · 2025: 19 · 2024: 29 · 2023: 25 · 2022: 28 · 2021: 27 · 2020: 31 · 2019: 33 · 2018: 49 · 2017: 45 · 2016: 66 · 2015: 52 · 2014: 60 · 2013: 53 · 2012: 54
FWCI
6.00
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p50hl021006-17)
  • National Institute on Aging (AG00602)
  • National Heart, Lung, and Blood Institute (HL 21006)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connective Tissue Growth Factor Research
  • Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
Keywords
receptor for advanced glycation end products, RAGE, amphoterin, RAGE ligands, soluble RAGE, neurite outgrowth, cortical neurons, brain development, immunoglobulin superfamily receptors, ligand-receptor interactions, embryonic neurons
MeSH terms
Receptor for Advanced Glycation End Products, Animals, Base Sequence, Carrier Proteins, Cattle, Cells, Cultured, Cerebral Cortex, Chromatography, Affinity, High Mobility Group Proteins, Immunohistochemistry, Ligands, Lung, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Protein Binding, Receptors, Immunologic, RNA, Messenger, Neurites, Rats, Wistar, In Situ Hybridization, HMGB1 Protein, Rats

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