Expression of advanced glycation end products and their cellular receptor RAGE diabetic nephropathy and nondiabetic renal disease

Journal of the American Society of Nephrology

Volumn 11, Issue 9, 2000, Pages 1656-1666

  Tanji, N ^a   Markowitz, G S ^a   Fu, C ^a   Kislinger, T ^a   Taguchi, A ^a   Pischetsrieder, M ^a   Stern, D ^a   Schmidt, A M ^a   D'Agati, V D ^a  

^a College of Physicians and Surgeons ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; LYSINE DERIVATIVE; MESSENGER RNA; PENTOSIDINE;

ADULT; ARTICLE; CONTROLLED STUDY; DIABETIC NEPHROPATHY; DISEASE SEVERITY; FEMALE; GENE EXPRESSION; GENE EXPRESSION REGULATION; GENE LOCATION; GLOMERULOSCLEROSIS; GLOMERULUS BASEMENT MEMBRANE; GLYCATION; HUMAN; HUMAN TISSUE; KIDNEY DISEASE; KIDNEY TUBULE BASEMENT MEMBRANE; LUPUS ERYTHEMATOSUS NEPHRITIS; MALE; MESANGIUM; NEPHROSCLEROSIS; PRIORITY JOURNAL;

EID: 0033848466     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (31)

1. Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications
2. Identification of N-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
3. Structure elucidation of a senescence cross-link from human extracellular matrix
4. Maillard reaction-mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia
5. Glucose and diabetic vascular disease
6. The dark side of glucose
7. Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins
8. Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface
9. Human and rat mesangial cell receptors for glucose-modified proteins: Potential role in kidney tissue remodelling and diabetic nephropathy
10. Receptor-specific increase in extracellular matrix production in mouse mesangial cells by advanced glycosylation end products is mediated via platelet-derived growth factor
11. Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: Role in vascular disease of diabetes and aging
12. Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
13. Advanced glycation end products interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice
14. Enhanced cellular oxidant stress by the interaction of AGEs with their receptors/binding proteins
15. The receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to AGEs in the intravascular space
16. Suppression of accelerated diabetic atherosclerosis by soluble receptor for advanced glycation end products
17. Diabetes mellitus
18. Increased accumulation of the glycoxidation product N-carboxymethyl lysine in human tissues in diabetes and aging
19. Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions
20. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
21. Immunohistochemical evidence for increased oxidative stress and carbonyl modification of proteins in diabetic glomerular lesions
22. N(ε)-(Carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signalling pathways and modulate gene expression
23. Advanced glycation end products and their receptors co-localise in rat organs susceptible to diabetic microvascular injury
24. The receptor for advanced glycation end products (RAGE) mediates the interaction of AGE-beta 2-microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway: Implications for the pathogenesis of dialysis-related amyloidosis
25. Expression of receptors for advanced glycation end products in peripheral occlusive vascular disease
26. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin: Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system
27. Structure and function of podocytes: An update
28. Synaptopodin: An actin-associated protein in telencephalic dendrites and renal podocytes
29. Expression of a neutrophil respiratory burst cytochrome and reactive oxygen species in kidney glomeruli in association with proteinuria in passive Heymann nephritis
30. The myeloperoxidase system of human phagocytes generates N(ε)-(carboxymethyl)lysine on proteins: A mechanism for producing advanced glycation end products at sites of inflammation
31. RAGE mediates a novel proinflammatory axis: A central cell surface receptor for S100/calgranulin polypeptides