Amyloid β2-microglobulin is modified with imidazolone, a novel advanced glycation end product, in dialysis-related amyloidosis

Kidney International

Volumn 51, Issue 1, 1997, Pages 187-194

  Niwa, Toshimitsu ^a   Katsuzaki, Tomoyuki ^b   Miyazaki, Shigeru ^b   Momoi, Tomoko ^b   Akiba, Takashi ^b   Miyazaki, Takashi ^b   Nokura, Kazuya ^b   Hayase, Fumitaka ^b   Tatemichi, Noriyuki ^b   Takei, Yoshifumi ^b  

^a NAGOYA UNIVERSITY HOSPITAL   (Japan)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; IMIDAZOLONE; UNCLASSIFIED DRUG;

ADULT; AMYLOIDOSIS; ARTICLE; CLINICAL ARTICLE; FEMALE; GLYCATION; HEMODIALYSIS; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MALE; PRIORITY JOURNAL;

EID: 8044244836     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1038/ki.1997.23     Document Type: Article

References (36)

1. DRÜEKE TB: Beta-2-microglobulin and renal hone disease. Miner Electrol Metab 17:261-272, 1991
2. 2-microglobulin. Biochem Biophys Res Commun 129:701-706, 1985
3. GOREVIC PD, CASEY TT, STONE WJ, DIRAIMONDO CR, PRELLI FC, FRANGIONE B: Beta-2 microglobulin is an amyloidogenic protein in man. J Clin Invest 76:2425-2429, 1985
4. 2-Microglobulin: A new form of amyloid protein associated with chronic hemodialysis. Kidney Int 30:385-390, 1986
5. 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. Proc Natl Acad Sci USA 83:7908-7912, 1986
6. 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis. N Engl J Med 314:585-586, 1986
7. 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. J Clin Invest 92:1243-1252, 1993
8. 2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis. J Clin Invest 93:521-528, 1994
9. NIWA T, MIYAZAKI S, KATSUZAKI T, TATEMICHI N, TAKEI Y, MIYAZAKI T, MORITA T, HIRASAWA Y: Immunohistochemical detection of advanced glycation end products in dialysis-related amyloidosis. Kidney Int 48:771-778, 1995
10. ε-(carboxymethyl)lysine in dialysis-related amyloidosis. Kidney Int 50:1303-1309, 1996
11. NIWA T, TAKEDA N, MIYAZAKI T, YOSHIZUMI H, TATEMATSU A, MAEDA A, OHARA M, TOMIYAMA S, NIIMURA K: Elevated serum levels of 3-deoxyglucosone, a potent protein-cross-linking intermediate of the Maillard reaction, in uremic serum. Nephron 69:438-443, 1995
12. 2-m with advanced glycation end products as observed in dialysis-related amyloidosis by 3-DG accumulating in uremic serum. Kidney Int 49:861-867, 1996
13. KATO H, SHIN DB, HAYASE F: 3-Deoxyglucosone crosslinks proteins under physiological conditions. Agr Biol Chem 51:2009-2011, 1987
14. SHIN DB, HAYASE F, KATO H: Polymerization of proteins caused by reaction with sugars and the formation of 3-deoxyglucosone under physiological conditions. Agr Biol Chem 52:1451-1458, 1988
15. KATO H: Chemical studies on amino-carbonyl reaction. Part I. Isolation of 3-deoxypentosone and 3-deoxyhexosones formed by browning degradation of N-glycosides. Agr Biol Chem 26:187-192, 1962
16. KATO H, CHO RK, OITANI A, HAYASE F: Responsibility of 3-deoxyglucosone for the glucose-induced polymerization of proteins. Agr Biol Chem 51:683-689, 1987
17. ε-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry 34:10872-10878, 1995
18. NJOROGE FG, SAYRE LM, MONNIER VM: Detection of glucose-derived pyrrole compounds during Maillard reaction under physiological conditions. Carbohydr Res 167:211-220, 1487
19. SELL DR, MONNIER VM: Structure elucidation of a senescence cross-link from human extracellular matrix. J Biol Chem 264:21597-21602, 1989
20. NAKAMURA K, HASEGAWA T, FUKUNAGA Y, IENAGA K: Crosslines A and B as candidates for the fluorophores in age- and diabetes-related cross-linked proteins, and their diacetates produced by Maillard reaction of α-N-acetyl-L-lysine with D-glucose. J Chem Soc Chem Commun 14:992-994, 1992
21. KONISHI Y, HAYASE F, KATO H: Novel imidazolone compound formed by the advanced Maillard reaction of 3-deoxyglucosone and arginine residues in proteins. Biosci Biotech Biochem 58:1953-1955, 1994
22. HAYASE F, KONISHI Y, KATO H: Identification of the modified structure of arginine residues in proteins with 3-deoxyglucosone, a Maillard reaction intermediate. Biosci Biotech Biochem 59:1407-1411, 1995
23. BROWNLEE M, VLASSARA H, CERAMI A: Nonenzymatic glycation and the pathogenesis of diabetic complications. Ann Intern Med 101:527-537, 1984
24. KENNEDY L, BAYNES JW: Nonenzymatic glycosylation and chronic complications of diabetes: an overview. Diabetologia 27:92-98, 1984
25. MONNIER VM, KOHN RR, CERAMI A: Accelerated age-related browning of human collagen in diabetes mellitus. Proc Natl Acad Sci USA 81:583-587, 1984
26. MAKITA Z, VLASSARA H, RAYFIELD E, CARTWRIGHT K, FRIEDMAN E, RODBY R, CERAMI A, BUCALA R: Hemoglobin-AGE: A circulating marker of advanced glycosylation. Science 258:651-653, 1992
27. ARAKI N, UENO N, CHAKRABARTI B, MORINO Y, HORIUCHI S: Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging. J Biol Chem 267:931-939, 1992
28. VITEK MP, BHATTACHARYA K, GLENDENING JM, STOPA E, VLASSARA H, BUCALA R, MANOGUE K, CERAMI A: Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci USA 91:4766-4770, 1994
29. SMITH MA, TANEDA S, RICHEY PL, MIYATA S, YAN SD, STERN D, SAYER LM, MONNIER VM, PERRY G: Advanced Maillard reaction end products are associated with Alzheimer disease. Proc Natl Acad Sci USA 91:5710-5714, 1994
30. YAN SD, CHEN X, SCHMIDT AM, BRETT J, GODMAN G, ZOU YS, SCOTT CW, CAPUTO C, FRAPPIER T, SMITH MA, PERRY G, YEN SH, STERN D: Glycated tau protein in Alzheimer disease: A mechanism for induction of oxidant stress. Proc Natl Acad Sci USA 91:7787-7791, 1994
31. VLASSARA H, BROWNLEE M, CERAMI A: High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci USA 82:5588-5592, 1985
32. RADOFF S, CERAMI A, VLASSARA H: Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophage-derived cell line RAW 264.7. Diabetes 39:1510-1518, 1990
33. HAYASE F, NAGARAJ RH, MIYATA S, NJOROGE FG, MONNIER VM: Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. J Biol Chem 263: 3758-3764, 1989
34. DYER DG, BLACKLEDGE JA, THORPE SR, BAYNES JW: Formation of pentosidine during nonenzymatic browning of proteins by glucose. J Biol Chem 266:11654-11660, 1991
35. WITKO-SARSAT V, FRIEDLANDER M, CAPEILLERE-BLANDIN C, NGUYEN-KHOA T, NGUYEN AT, ZINGRAFF J, JUNGERS P, DESCAMPS-LATSCHA B: Advanced oxidation protein products as a novel marker of oxidative stress in uremia. Kidney Int 49:1304-1313, 1996
36. NIWA T, TAKEDA N, YOSHIZUMI H, TATEMATSU A, OHARA M, TOMIYAMA S, NIIMURA K: Presence of 3-deoxyglucosone, a potent protein crosslinking intermediate of Maillard reaction, in diabetic serum. Biochem Biophys Res Commun 196:837-843, 1993