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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
Open accessAbstract
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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“RAGE, a member of the immunoglobulin superfamily of pattern recognition receptors, is not known to be related to oxytocin or oxytocin signalling22–33.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [29]
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Mechanisms of Diabetic Complications
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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
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Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150
Mechanisms of diabetes mellitus-induced bone fragility
On behalf of the IOF Bone and Diabetes Working Group, Napoli, N., Chandran, M., Pierroz, D. D., Abrahamsen, B., Schwartz, A. V., & Ferrari, S. L. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.153 · Cited by 1,107
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Metadata
- 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
- 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
- hybrid
- doi.org
- 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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