Non-enzymatic glycation, cellular receptors and oxidant stress together have implications for the pathogenesis of cellular dysfunction in diabetes and beyond (pages 1057–1061).
This is a preview of subscription content, access via your institution
Relevant articles
Open Access articles citing this article.
-
Antiglycation potential of Indigoferin a, Indigoferin B and Indigoferin C natural products from Indigofera heterantha Brandis
Clinical Phytoscience Open Access 06 January 2021
-
Increased glycated albumin and decreased esRAGE levels in serum are related to negative coronary artery remodeling in patients with type 2 diabetes: an Intravascular ultrasound study
Cardiovascular Diabetology Open Access 27 November 2018
Access options
Subscribe to this journal
Receive 12 print issues and online access
$209.00 per year
only $17.42 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Li, Y-M., Tan, A.X. & Vlassara, H. Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of AGE-modifled proteins to a conserved motif. Nature Med. 1, 1057–1061 (1995).
Ruderman, N., Wiliamson, J. & Brownlee, M. Glucose and diabetic vascular disease. FASEB J. 6, 2905–2914 (1992).
Harrington, C. & Colaco, C.A.L.S. Alzheimer's disease: A glycation connection. Nature 370, 247–248 (1994).
Miyata, T. et al. β2-Microglobulin modified with AGEs is a major component of hemodialysis-associated amyloidosis. J. clin. Invest. 92, 1243–1252 (1993).
Yan, S-D. et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide. Nature Med. 1, 693–699 (1995).
Vitek, M. et al. AGEs contribute to amyloidosis in Alzheimer's disease. Proc. natn. Acad. Sci. U.S.A. 91, 4766–4770 (1994).
Smith, M. et al. Advanced maillard reaction end-products are associated with Alzheimer disease pathology. Proc. natn. Acad. Sci. U.S.A. 91, 5710–5714 (1994).
Palinski, W. et al. Immunological presence of AGEs in atherosclerotic lesions of euglycemic rabbits. Arterioscl. Thromb. Vase. Biol. 15, 571–582 (1995).
Kirstein, M. et al. AGE induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: Role in vascular disease of diabetes and aging. Proc. natn. Acad. Sci. U.S.A. 87, 9010–9014 (1990).
Schmidt, A-M. et al. Regulation of human mononuclear phagocyte migration by cell surface binding proteins for AGEs. J. clin. Invest. 91, 2155–2168 (1993).
Vlassara, H., Bucala, R. & Striker, L. Pathogenic effects of AGEs: Biochemical, biologic, and clinical implications for diabetes and aging. Lab. Invest. 70, 138–151 (1994).
Schmidt, A-M. et al. Cellular receptors for AGEs: Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Arteroscler. Thromb. 14, 1521–1528 (1994)
Khoury, J. et al. Macrophages adhere to glucose-modified basement membrane via their scavenger receptors. J. biol. Chem. 269, 10197–10200 (1994).
Schmidt, A-M., Hori, O., Chen, J., Brett, J. & Stern, D. AGE interaction with their endothelial receptor induces expression of VCAM-1: A potential mechanism for the accelerated vasculopa-thy of diabetes. J. Clin Invest. 96, 1375–1403 (1995).
Li, H., Cybulsky, M., Gimbrone, M. & Libby, P. An atherogenic diet rapidly induces VCAM-1, a cytokine regulatable mononuclear leukocyte adhesion molecule, in rabbit aortic endothelium. Arteroscler. Thromb. 13, 197–204 (1993).
Hori, O. et al. RAGE is a cellular binding site for amphoterin: Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system. J. biol. Chem. (in the press).
Schmidt, A-M. et al. The endothelial binding site for AGEs consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide. J. biol. Chem. 269, 9882–9888 (1994).
Marhoffer, W., Stein, M., Maeser, E. & Federlin, K. Impairment of polymorphonuclear leukocyte function and metabolic control for diabetes. Diabetes Care 15, 256–260 (1992).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schmidt, A., Yan, S. & Stern, D. The dark side of glucose. Nat Med 1, 1002–1004 (1995). https://doi.org/10.1038/nm1095-1002
Issue Date:
DOI: https://doi.org/10.1038/nm1095-1002
This article is cited by
-
Antiglycation potential of Indigoferin a, Indigoferin B and Indigoferin C natural products from Indigofera heterantha Brandis
Clinical Phytoscience (2021)
-
A C. elegans Model for the Study of RAGE-Related Neurodegeneration
Neurotoxicity Research (2019)
-
Oxindole-based chalcones: synthesis and their activity against glycation of proteins
Medicinal Chemistry Research (2019)
-
Increased glycated albumin and decreased esRAGE levels in serum are related to negative coronary artery remodeling in patients with type 2 diabetes: an Intravascular ultrasound study
Cardiovascular Diabetology (2018)
-
Advanced glycation end products promote human aortic smooth muscle cell calcification in vitro via activating NF-κB and down-regulating IGF1R expression
Acta Pharmacologica Sinica (2013)