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Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes.
Open accessAbstract
Vascular cell adhesion molecule-1 (VCAM-1), an inducible cell-cell recognition protein on the endothelial cell surface (EC), has been associated with early stages of atherosclerosis. In view of the accelerated vascular disease observed in patients with diabetes, and the enhanced expression of VCAM-1 in diabetic rabbits, we examined whether irreversible advanced glycation endproducts (AGEs), could mediate VCAM-1 expression by interacting with their endothelial cell receptor (receptor for AGE, RAGE). Exposure of cultured human ECs to AGEs induced expression of VCAM-1, increased adhesivity of the monolayer for Molt-4 cells, and was associated with increased levels of VCAM-1 transcripts. The inhibitory effect of anti-RAGE IgG, a truncated form of the receptor (soluble RAGE) or N-acetylcysteine on VCAM-1 expression indicated that AGE-RAGE-induced oxidant stress was central to VCAM-1 induction. Electrophoretic mobility shift assays on nuclear extracts from AGE-treated ECs showed induction of specific DNA binding activity for NF-kB in the VCAM-1 promoter, which was blocked by anti-RAGE IgG or N-acetylcysteine. Soluble VCAM-1 antigen was elevated in human diabetic plasma. These data are consistent with the hypothesis that AGE-RAGE interaction induces expression of VCAM-1 which can prime diabetic vasculature for enhanced interaction with circulating monocytes.
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“Excessive AGE formation is particularly associated with cross-linking of matrix proteins such as collagen, vitronectin, and laminin.[2,10,11]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [11]
In the citing paper
“Binding of AGEs to the receptor for AGE (RAGE) enhances the expression of adhesion molecules on endothelial cells to promote the migration and differentiation of monocytes into macrophages.”
From The Vasculature in Prediabetes (2018) · cites this paper as [60]
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BackgroundMünch, G. W., Keis, R., Weßels, A., Riederer, P. F., Bahner, U., Heidland, A., Niwa, T., Lemke, H., & Schinzel, R. (1997) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1997.35.9.669 · Cited by 313
Schmidt, A. M., Weidman, E., Lalla, E., Yan, S. D., Hori, O., Cao, R. Y., Brett, J. G., & Lamster, I. B. (1996) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1996.tb01417.x · Cited by 304
Self-citationRAGE (receptor for advanced glycation end products): a central player in the inflammatory response
Chavakis, T., Bierhaus, A., & Nawroth, P. P. (2004) · Microbes and Infection · doi:10.1016/j.micinf.2004.08.004 · Cited by 307
(2002) · PubMed · Cited by 292
Role of NF-κB in the pathogenesis of diabetes and its associated complications
Patel, S., & Santani, D. D. (2009) · Pharmacological Reports · doi:10.1016/s1734-1140(09)70111-2 · Cited by 300
Negative consequences of glycation
Brownlee, M. (2000) · Metabolism · doi:10.1016/s0026-0495(00)80078-5 · Cited by 284
Miyata, T., Hori, O., Zhang, J., Yan, S. S., Ferran, L., Iida, Y., & Schmidt, A. M. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118889 · Cited by 278
Self-citationKislinger, T., Tanji, N., Wendt, T., Qu, W., Lu, Y., Ferran, L. J., Taguchi, A., Olson, K. E., Bucciarelli, L. G., Goova, M. T., et al. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.6.905 · Cited by 284
Self-citationQuehenberger, P., Bierhaus, A., Fasching, P., Muellner, C., Klevesath, M. S., Hong, M., Stier, G., Sattler, M., Schleicher, E., Speiser, W., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.9.1561 · Cited by 290
Schram, M. T., Chaturvedi, N., Schalkwijk, C., Fuller, J., Stehouwer, C. D. A., & EURODIAB Prospective Complications Study Group (2005) · Diabetologia · doi:10.1007/s00125-004-1628-8 · Cited by 285
“mediating, in part, the effects of conventional risk factors such as blood pressure, HbA1c and advanced glycation endproducts (AGEs) [5].”
BackgroundStern, D. M., Yan, S. D., Yan, S. F., & Schmidt, A. M. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00160-6 · Cited by 281
Self-citationUremic Toxicity: Present State of the Art
Vanholder, R. C., Argilés, À., Baurmeister, U., Brunet, P., Clark, W. R., Cohen, G., Dedeyn, P. P., Deppisch, R. M., Descamps‐Latscha, B., Henle, T., et al. (2001) · The International Journal of Artificial Organs · doi:10.1177/039139880102401004 · Cited by 285
“Advanced glycation end products (AGEs) that accumulate in CRF induce endothelial cell activation (297).”
BackgroundShipanova, I. N., Glomb, M. A., & Nagaraj, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0195 · Cited by 277
Diabetes-Induced Oxidative Stress and Low-Grade Inflammation in Porcine Coronary Arteries
Zhang, L., Zalewski, A. A., Liu, Y., Mazurek, T., Cowan, S., Martin, J. L., Hofmann, S. M., Vlassara, H., & Shi, Y. (2003) · Circulation · doi:10.1161/01.cir.0000080378.96063.23 · Cited by 277
Advanced glycation endproducts in ageing and Alzheimer's disease
Münch, G. W., Thome, J., Foley, P. B., Schinzel, R., & Riederer, P. F. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(96)00016-1 · Cited by 278
Soluble Vascular Cell Adhesion Molecule-1 as a Biohumoral Correlate of Atherosclerosis
Caterina, R. D., Basta, G., Lazzerini, G., Dell’Omo, G., Petrucci, R., Morale, M., Carmassi, F., & Pedrinelli, R. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.11.2646 · Cited by 268
Mechanisms of diabetic vasculopathy: an overview
Cooper, M. E. (2001) · American Journal of Hypertension · doi:10.1016/s0895-7061(00)01323-6 · Cited by 267
Advanced glycation End-products (AGEs): an emerging concern for processed food industries
Sharma, C., Kaur, A., Thind, S. S., Singh, B., & Raina, S. (2015) · Journal of Food Science and Technology · doi:10.1007/s13197-015-1851-y · Cited by 254
“AGEs can alter properties of the large matrix proteins collagen, vitronectin, and laminin, through AGE-AGE intermolecular covalent bonds, or crosslinking (Howard et al. 1996; Schmidt et al. 1995).”
BackgroundDemling, N., Ehrhardt, C., Kasper, M. E., Laue, M. M., Knels, L., & Rieber, E. P. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-0069-0 · Cited by 249
“Since the cDNA panel comprised only tissue preparations, we isolated RNA from primary HUVEC, which have been reported to express RAGE (Boulanger et al. 2002; Bierhaus et al. 1997; Schmidt et al. 1995 ) and, for a comparison, from lung tissue of two individuals (Fig. 1b).”
BackgroundMethodRAGE Control of Diabetic Nephropathy in a Mouse Model
Myint, K.-M., Yamamoto, Y., Doi, T., Kato, I., Harashima, A., Yonekura, H., Watanabe, T., Shinohara, H., Takeuchi, M., Tsuneyama, K., et al. (2006) · Diabetes · doi:10.2337/db06-0221 · Cited by 250
“sion molecule (VCAM)-1 assay was performed by ELISA as described (28).”
Method
Metadata
- Authors
- Schmidt, A. M., Hori, O., Chen, J. X., Li, J. F., Crandall, J., Zhang, J., Cao, R., Yan, S. D., Brett, J., & Stern, D.
- Affiliations
- Columbia University Irving Medical Center (US)
- Columbia University (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1995-09-01
- Volume
- 96
- Issue
- 3
- Pages
- 1395-1403
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC185762
- OpenAlex
- W2138928713
- Cited by
- 896
- References
- 43
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 15 · 2023: 16 · 2022: 13 · 2021: 21 · 2020: 16 · 2019: 23 · 2018: 16 · 2017: 26 · 2016: 17 · 2015: 34 · 2014: 32 · 2013: 35 · 2012: 36
- FWCI
- 17.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (University of Kansas) (submittedVersion, other-oa)
- Funders
- American Heart Association
- National Institutes of Health (5r01hl042833-10, 5p50hl021006-17)
- U.S. Public Health Service
- National Institute on Aging (AG00602)
- National Heart, Lung, and Blood Institute (HL-42833, HL 21006)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- advanced glycation end products, receptor for advanced glycation end products, VCAM-1, endothelial cells, diabetes mellitus, diabetic vascular disease, oxidative stress, NF-kB, soluble RAGE, N-acetylcysteine, monocyte adhesion, atherosclerosis, soluble VCAM-1
- MeSH terms
- Receptor for Advanced Glycation End Products, Animals, Base Sequence, Cell Adhesion, Cell Line, Cell Nucleus, Cells, Cultured, Diabetic Angiopathies, Endothelium, Vascular, Enzyme-Linked Immunosorbent Assay, Humans, Male, Models, Biological, Molecular Sequence Data, Receptors, Immunologic, Transcription, Genetic, Umbilical Veins, Cell Adhesion Molecules, Gene Expression, Polymerase Chain Reaction, Glycation End Products, Advanced, DNA Primers, Oxidative Stress, Vascular Cell Adhesion Molecule-1, Mice
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