Accumulation of albumin-linked and free-form pentosidine in the circulation of uremic patients with end-stage renal failure: Renal implications in the pathophysiology of pentosidine

Journal of the American Society of Nephrology

Volumn 7, Issue 8, 1996, Pages 1198-1206

  Miyata, Toshio ^a   Ueda, Yasuhiko ^b   Shinzato, Toru ^a   Iida, Yoshiyasu ^a   Tanaka, Shuichi ^b   Kurokawa, Kiyoshi ^c   Van Ypersele De Strihou, Charles ^d   Maeda, Kenji ^a  

^a NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b Fuso Pharmaceutical Industries   (Japan)

^c TOKAI UNIVERSITY   (Japan)

^d UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

Advanced glycation end products; Diabetes; Glycoxidation; Hemodialysis; Pentosidine

Indexed keywords

ALBUMIN; GLYCOSYLATED PROTEIN; MATRIX PROTEIN; PENTOSIDINE; UNCLASSIFIED DRUG;

ADULT; ALBUMIN BLOOD LEVEL; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; DIET; FEMALE; GLOMERULUS FILTRATION RATE; HEMODIALYSIS; HUMAN; KIDNEY FAILURE; KIDNEY FUNCTION; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; RAT; UREMIA;

EID: 0030391546     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (41)

1. Brownlee M, Cerami A, Vlassara H: Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. N Engl J Med 1988;318:1315-1321.
2. Baynes JW, Monnier VM: The Maillard reaction in aging, diabetes and nutrition. Prog Clin Biol Res 1989;304:1-410.
3. Kirstein M, Brett J, Radoff S, Ogawa S, Stern D, Vlassara H: Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: Role in vascular disease of diabetes and aging. Proc Natl Acad Sci USA 1990;87: 9010-9014.
4. Vlassara H, Brownlee M, Manogue KR, Dinarello CA, Pasagian A: Cachectin/TNF and IL-1 induced by glucose-modified proteins: Role in normal tissue remodeling. Science (Wash DC) 1988;240:1546-1548.
5. Schmidt AM, Yon SD, Brett J, Mora R, Nowygrod R, Stern D: Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. J Clin Invest 1993;92:2155-2168.
6. Wautier JL, Wautier MP, Schmidt AM, et al.: Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: A link between surface-associated AGEs and diabetic complications. Proc Natl Acad Sci USA 1994;91:7742-7746.
7. Skolnik EY, Yang Z, Makita Z, Radoff S, Kirstein M, Vlassara H: Human and rat mesangial cell receptors for glucose-modified proteins: Potential role in kidney tissue remodelling and diabetic nephropathy. J Exp Med 1991; 174:931-939.
8. Doi T, Vlassara H, Kirstein M, Yamada Y, Striker GE, Striker LJ: Receptor-specific increase in extracellular matrix production in mouse mesangial cells by advanced glycosylation end products is mediated via platelet-derived growth factor. Proc Natl Acad Sci USA 1992;89: 2873-2877.
9. Beisswenger PJ, Moore LL, Brink-Johnsen T: Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy. J Clin Invest 1993;92:212-217.
10. Miyata T, Oda O, Inagi R, et al.: β2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. J Clin Invest 1993;92:1243-1252.
11. Miyata T, Inagi R, Iida Y, et al.: Involvement of β2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis: Induction of human monocyte chemotaxis and macrophage secretion of tumor necrosis factor-α and interleukin 1. J Clin Invest 1994;93:521-528.
12. Iida Y, Miyata T, Inagi R, Sugiyama S, Maeda K: β2-Microglobulin modified with advanced glycation end products induces interleukin-6 from human macrophages: Role in the pathogenesis of hemodialysis-associated amyloidosis. Biochem Biophys Res Commun 1994;201:1235-1241.
13. Miyata T, Iida Y, Ueda Y, et al.: Monocyte/macrophage response to β2-microglobulin modified with the advanced glycation end products. Kidney Int 1996;49:538-550.
14. Miyata T, Taneda S, Kawai R, et al.: Identification of pentosidine as a native structure for advanced glycation end products in β2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis. Proc Natl Acad Sci USA 1996;93:2353-2358.
15. Miyata T, Inagi R, Wada Y, et al.: Glycation of human β2-microglobulin in patients with hemodialysis-associated amyloidosis: Identification of the glycated sites. Biochemistry 1994;33:12215-12221.
16. Smith MA, Taneda S, Richey PL, et al.: Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc Natl Acad Sci USA 1994;91: 5710-5714.
17. Vitek MP, Bhattacharya K, Glendening JM, et al.: Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci USA 1994;91: 4766-4770.
18. Yan SD, Yan FF, Chen X, 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 1995;1:693-699.
19. Neeper M, Schmidt AM, Brett J, et al.: Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J Biol Chem 1992; 267:14998-15004.
20. Yan SD, Schmidt AM, Anderson GM, et al.: Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J Biol Chem 1994;269:9889-9897.
21. Baynes JW: Perspectives in diabetes: Role of oxidative stress in development of complications in diabetes. Diabetes 1991;40:405-412.
22. Sell DR, Monnier VM: Structure elucidation of a senescence cross-link from human extracellular matrix. J Biol Chem 1989;264:21597-21602.
23. Sell DR, Monnier VM: End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen. J Clin Invest 1990;85:380-384.
24. Dyer DG, Dunn JA, Thorpe SR, et al.: Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 1993;91:2463-2469.
25. Monnier VM, Sell DR, Nagaraj RH, et al.: Maillard reaction-mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia. Diabetes 1992;41:36-41.
26. Odetti P, Forgarty J, Sell DR, Monnier VM: Chromatographic quantitation of plasma and erythrocyte pentosidine in diabetic and uremic subjects. Diabetes 1992;41: 153-159.
27. Taneda S, Monnier VM: Enzyme-linked immunosorbent assay (ELISA) for pentosidine, an advanced glycation end product in biological specimens. Clin Chem 1994; 40:1766-1773.
28. Sell DR, Lapolla A, Odetti P, Forgarty J, Monnier VM: Pentosidine formation in skin correlates with severity of complication in individuals with long standing IDDM. Diabetes 1992;41:1286-1292.
29. McCance DR, Dyer DG, Dunn JA, et al.: Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 1993; 91:2470-2478.
30. Hricik DE, Schulak JA, Sell DR, Fogarty JF, Monnier VM: Effect of kidney or kidney-pancreas transplantation on plasma pentosidine. Kidney Int 1993;43:398-403.
31. Grandhee SK, Monnier VM: Mechanism of formation of the Maillard protein cross-link pentosidine. J Biol Chem 1991;266:11649-11653.
32. Platt R, Roscoe MH, Smith FW: Experimental renal failure. Clin Sci 1952;11:217.
33. Dyer DG, Blackledge JA, Thorpe SR, Baynes JW: Formation of pentosidine during nonenzymatic browning of protein by glucose: Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. J Biol Chem 1991;266:11654-11660.
34. Makita Z, Bucala R, Rayfield EJ, et al.: Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure. Lancet 1994;343:1519-1522.
35. Makita Z, Radoff S, Rayfield EJ, et al.: Advanced glycosylation end products in patients with diabetic nephropathy. N Engl J Med 1990;325:836-842.
36. Makita Z, Vlassara H, Cerami A, Bucala R: Immunochemical detection of advanced glycosylation end products in vivo. J Biol Chem 1992;267:5133-5138.
37. ∈-(carboxymethyl)rysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry 1995;34:10872-10878.
38. Horiuchi S, Araki N, Morino Y: Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. J Biol Chem 1991;266:7329-7332.
39. Bucala R, Makita Z, Vega G, et al.: Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. Proc Natl Acad Sci USA 1994;91:9441-9445.
40. Gejyo F, Yamada T, Odani S, et al.: A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin. Biochem Biophys Res Commun 1985;129:701-706.
41. Gorevic PD, Munoz PC, Casey TT, et al.: Polymerization of intact β2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. Proc Natl Acad Sci USA 1986;83:7908-7912.