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Cited by 716Advanced Glycation End Products researchRetinal Diseases and TreatmentsConnective Tissue Growth Factor Research

The DOI matches its Crossref record; 44 of the 46 references it cites were found in a registry or an index.

Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury

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YONEKURA, Hideto, YAMAMOTO, Yasuhiko, SAKURAI, Shigeru, PETROVA, Ralica G., ABEDIN, Md. Joynal, LI, Hui, YASUI, Kiyoshi, TAKEUCHI, Masayoshi, MAKITA, Zenji, TAKASAWA, Shin, OKAMOTO, Hiroshi, WATANABE, Takuo, YAMAMOTO, Hiroshi·2003·Biochemical Journal
DOI 10.1042/bj20021371PMC PMC1223244
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Abstract

The binding of advanced glycation end-products (AGE) to the receptor for AGE (RAGE) is known to deteriorate various cell functions and is implicated in the pathogenesis of diabetic vascular complications. In the present study, we show that the cellular constituents of small vessels, endothelial cells (EC) and pericytes express novel splice variants of RAGE mRNA coding for the isoforms that lack the N-terminal V-type immunoglobulin-like domain (N-truncated) or the C-terminal transmembrane domain (C-truncated), as well as the known full-length mRNA. The ratio of the expression of the three variants was different between EC and pericytes; the content of the C-truncated form was highest in EC, whereas the full-length form was the most abundant in pericytes. Transfection experiments with COS-7 cells demonstrated that those variant mRNAs were translated into proteins as deduced; C-truncated RAGE was efficiently secreted into the culture media, and N-truncated RAGE was located mainly on the plasma membrane. The three isoforms were also detected in primary cultured human EC and pericytes. Further, full-length and C-truncated forms of RAGE bound to an AGE-conjugated column, whereas N-truncated RAGE did not. The AGE induction of extracellular-signal-related kinase phosphorylation and vascular endothelial growth factor in EC and of the growth and cord-like structure formation of EC was abolished completely by C-truncated RAGE, indicating that this endogenous secretory receptor (endogenous secretory RAGE) is cytoprotective against AGE. The results may contribute to our understanding of the molecular basis for the diversity of cellular responses to AGE and for individual variations in the susceptibility to diabetic vascular complications.

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Authors
YONEKURA, H., YAMAMOTO, Y., SAKURAI, S., PETROVA, R. G., ABEDIN, M. J., LI, H., YASUI, K., TAKEUCHI, M., MAKITA, Z., TAKASAWA, S., OKAMOTO, H., WATANABE, T., & YAMAMOTO, H.
Affiliations
  • Kanazawa University (JP)
  • Hokuriku University (JP)
  • Kurume University (JP)
  • Tohoku University (JP)
Corresponding author
  • YONEKURA, Hideto
  • YAMAMOTO, Yasuhiko
  • SAKURAI, Shigeru
  • LI, Hui
  • YASUI, Kiyoshi
  • WATANABE, Takuo
  • YAMAMOTO, Hiroshi
ORCID
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2003-03-15
Volume
370
Issue
3
Pages
1097-1109
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj20021371
PMC
PMC1223244
OpenAlex
W2021346724
Cited by
716
References
46
Citations by year
2026: 12 · 2025: 8 · 2024: 15 · 2023: 34 · 2022: 32 · 2021: 34 · 2020: 26 · 2019: 27 · 2018: 24 · 2017: 26 · 2016: 42 · 2015: 34 · 2014: 20 · 2013: 38 · 2012: 41
FWCI
15.79
Type
journal article
Language
en
Open access
Licence
public-domain
Locations
  • Biochemical Journal (publishedVersion, public-domain)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Ministry of Education, Culture, Sports, Science and Technology (13670113)
  • Japan Society for the Promotion of Science (97L00805, 13470197, 13670113)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connective Tissue Growth Factor Research
Keywords
receptor for advanced glycation end products, advanced glycation end products, vascular endothelial cells, pericytes, diabetic vascular complications, vascular endothelial growth factor, cell proliferation
MeSH terms
Receptor for Advanced Glycation End Products, Amino Acid Sequence, Animals, Cell Movement, Cells, Cultured, Diabetes Mellitus, Endothelium, Vascular, Humans, Lymphokines, Molecular Sequence Data, Oligosaccharides, Protein Binding, Receptors, Immunologic, Endothelial Growth Factors, Sequence Alignment, Glycation End Products, Advanced, Alternative Splicing, Protein Isoforms, Pericytes, Mitogen-Activated Protein Kinases, Intercellular Signaling Peptides and Proteins, Vascular Endothelial Growth Factors, Vascular Endothelial Growth Factor A, Diabetes Complications

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