Publication Cover
Amyloid
The Journal of Protein Folding Disorders
Volume 5, 1998 - Issue 1
14
Views
8
CrossRef citations to date
0
Altmetric
Original Article

Synovial inflammatory cells captured 131I-β2-microglobulin in patients with dialysis related amyloidosis

, &
Pages 24-29 | Received 11 Jun 1997, Accepted 23 Oct 1997, Published online: 06 Jul 2009

References

  • Gejyo F, Honma N, Arakawa M. Long-term complications of dialysis: pathogenetic factors with special reference to amyloidosis. Kidney Int 1993; 43(Suppl41)S78–S82
  • Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, Kunitomo T, Kataoka H, Suzuki M, Hirasawa Y, Shirahama T, Cohen A S, Schmid K. A new form of amyloid protein associated with chronic hemodialysis was identified asβ2-microglobulin. Biochem Biophys Res Commun 1985; 129: 701–706
  • Sethi D, Gower P E. Synovial fluid beta 2-microglobulin levels in dialysis arthropathy (letter). N Eng J Med 1986; 315: 1419–1420
  • Kleinman K S, Coburn J W. Amyloid syndromes associated with hemodialysis. Kidney Int 1989; 35: 567–573
  • Koch K M. Dialysis-related amyloidosis. Kidney Int 1992; 41: 1416–1429
  • Nelson S R, Hawkins P N, Richardson S, Lavender J P, Sethi D, Gower P E, Pugh C W, Winearls C G, Oliver D O, Pepys M B. Imaging of haemodialysis-associated amyloidosis with 1231-serum amyloid P component. Lancet 1991; 338: 335–339
  • Floege J, Burchert W, Brandis A, Gielow P, Nonnast-Daniel B, Hundeshagen H, Shaldon S, Koch K M. Imaging of dialysis-related amyloid (AB-amyloid) deposits with 131I-P2-microglobulin. Kidney Int 1990; 38: 1169–1176
  • Gejyo F, Kazama J J, Hasegawa S., Hanma N, Nisht S, Arakawa M, Odano I. 131I-(32-microglobulin scintigraphy in patients with dialysis amyloidosis. Clin Nephrol 1995; 44: S14–S18
  • Hunter W M, Greenwood F C. Preparation of iodine-131 labeled human growth hormone of high specific activity. Nature 1962; 194: 495–496
  • Kazama J J, Takeda T, Katagiri T, Kuwano R, Kumanishi T, Ozawa H, Arakawa M. A histocytochemical study of spot 35-calbindin-D28K in rat kidney. Nephrology 1995; 1: 73–82
  • Kazama J J, Gejyo F, Ejiri S, Okada M, Ei I, Arakawa M, Ozawa H. Application of confocal laser scanning microscopy to the observation of bone biopsy specimens. Bone 1993; 14: 885–889
  • Argiles A, Mourad G, Kerr P G, Garcia M, Collins B, Demaille J G. The cells surrounding haemodialysis associated amyloid deposits are mainly macrophages. Nephrol Dial Transp 1994; 9: 662–667
  • Ohashi K, Hara M, Kawai R, Ogura Y, Honda K, Nihei H, Mimura N. Cervical discs are most susceptible to beta2-microglobulin amyloid deposition in the vertebral column. Kidney Int 1992; 41: 1646–1652
  • Niwa T, Miyazaki S, Katsuzaki T, Tatemichi N, Takei Y, Miyazaki T, Morita T, Hirasawa Y. Immunohis-tochemical detection of advanced glycation end products in dialysis-related amyloidosis. Kidney Int 1995; 48: 771–778
  • Gejyo F, Maruyama H, Teramura T, Kazama J J, Ei I, Arakawa M. Role of macrophages in β2-microglobulin-related dialysis amyloidosis. Contrib Nephrol 1995; 112: 97–104
  • Floege J, Ehlerding G. Beta-2-microglobulin-asso-ciated amyloidosis. Nephron 1996; 72: 9–26
  • Rainsbouly R. Location of metastatic breast carcinoma by a monoclonal antibody chelate labeled with indium-111. Lancet 1983; ii: 934–938
  • Schaeffer J, Floege J, Koch K M. Whole-body scintigraphy. Dialysis Amyloid, C van Ypersele, T B Drueke. FOxford University, New York and London 1996; 145–155
  • Jadoul M, Noel H, Malghem J, Galant C, van Ypersele C. Histological beta-2-microglobulin amyloidosis 10 years after a successful renal transplantation. Ame J Kid Dis 1996; 27: 888–890
  • Vincent C, Chanard J, Caudwell V, Lavaud S, Toupance O, Wong T, Revillard J-P. Kinetics of 125I-β2-microglobulin turnover in dialyzed patients. Kidney Int 1992; 42: 1434–1443
  • Chanard J, Vincent C, Caudwell V, Lavaud S, Wong T, Revillard J-P. Beta 2-microglobulin metabolism in uremic patients who are undergoing dialysis. Kidney Int 1993; 43(Suppl 41)S83–S87
  • Nguyen-Simonnet H, Vincent C, Gauthier C, Revillard J P, Pellet M V. Turnover studies of human β-m in the rat. J Clin Sci 1982; 62: 403–410
  • Brownlee M. Glycation and diabetic complications. Diabetes 1994; 43: 836–841
  • Niwa T, Katsuzaki T, Momoi T, Miyazaki T, Ogawa H, Saito A, Miyazaki S, Maeda K, Tatemichi N, Takei Y. Modification of β2M with advanced glycation end products as observed in dialysis-related amyloidosis by 3-DG accumulating in uremic serum. Kidney Int 1996; 49: 861–867
  • Miyata T, Inagi R, Iida Y, Sato M, Yamada N, Oda O, Maeda K, Seo H. 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-alfa and interleukin-1. J Clin Invest 1994; 93: 521–528
  • Linke R P, Hampl H, Lobeck H, Ritz E, Bommer J, Waldherr R, Eulitz M. Lysine-specific cleavage of beta-2-microglobulin in amyloid deposits associated with hemodialysis. Kidney Int 1989; 36: 675–681
  • Niwa T, Sato M, Katsuzaki T, Tomoo T, Miyazaki T, Tatemichi N, Takei Y, Kondo T. Amyloid P2-microglobulin is modified with N-(carboxymethyl)lysine in dialysis-related amyloidosis. Kidney Int 1996; 50: 1303–1309
  • Campistol J M, Bernard D, Papastoitsis G, Sole M, Kasirsky J, Skinner M. Polymerization of normal and intact β2-microglobulin as the amyloidogenic protein in dialysis-amyloidosis. Kidney Int 1996; 50: 1262–1267
  • Miyata T, Oda O, Inagi R, Iida Y, Araki N, Yamada N, Horiuchi S, Taniguchi N, Maeda K, Kinoshita T. (32-microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. J Clin Invest 1993; 92: 1243–1252
  • Giardino I, Edelstein D, Brownlee M. Nonenzy-matic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity. J Clin Invest 1994; 94: 110–117

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.