Artigo Revisado por pares

New Insights into the Pathogenesis of Hemodialysis‐Associated Amyloidosis

1990; Wiley; Volume: 3; Issue: 3 Linguagem: Inglês

10.1111/j.1525-139x.1990.tb00032.x

ISSN

1525-139X

Autores

Àngel Argilés, Georges Mourad, Robert C. Atkins, C Mion,

Tópico(s)

Trace Elements in Health

Resumo

Seminars in DialysisVolume 3, Issue 3 p. 149-151 New Insights into the Pathogenesis of Hemodialysis-Associated Amyloidosis Angel Argilés, Angel Argilés Departments of Nephrology, Prince Henry's Hospital, Monash University, Melbourne, AustraliaSearch for more papers by this authorGeorges Mourad, Georges Mourad Hopital Lapeyronie, Universite de Montpellier, Montpellier, FranceSearch for more papers by this authorRobert C. Atkins, Corresponding Author Robert C. Atkins Departments of Nephrology, Prince Henry's Hospital, Monash University, Melbourne, AustraliaProfessor Robert C. Atkins, Department of Nephrology, Prince Henry's Hospital, St. Kilda Road, Melbourne 3004, Australia.Search for more papers by this authorCharles M. Mion, Charles M. Mion Hopital Lapeyronie, Universite de Montpellier, Montpellier, FranceSearch for more papers by this author Angel Argilés, Angel Argilés Departments of Nephrology, Prince Henry's Hospital, Monash University, Melbourne, AustraliaSearch for more papers by this authorGeorges Mourad, Georges Mourad Hopital Lapeyronie, Universite de Montpellier, Montpellier, FranceSearch for more papers by this authorRobert C. Atkins, Corresponding Author Robert C. Atkins Departments of Nephrology, Prince Henry's Hospital, Monash University, Melbourne, AustraliaProfessor Robert C. Atkins, Department of Nephrology, Prince Henry's Hospital, St. Kilda Road, Melbourne 3004, Australia.Search for more papers by this authorCharles M. Mion, Charles M. Mion Hopital Lapeyronie, Universite de Montpellier, Montpellier, FranceSearch for more papers by this author First published: July 1990 https://doi.org/10.1111/j.1525-139X.1990.tb00032.xCitations: 12AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Virchow, R: Zur cellulose-frage. Virchows Arch 6: 416, 1854. 10.1007/BF02116546 Google Scholar 2 Cohen AS, Connors LH: The pathogenesis and biochemistry of amyloidosis. J Pathol 151: 1–10, 1987. 10.1002/path.1711510102 CASPubMedWeb of Science®Google Scholar 3 Pepys MB: Amyloidosis: Some recent developments. Q J Med 67: 283–298, 1988. CASPubMedWeb of Science®Google Scholar 4 Assenat H, Calemard E, Charra B, Laurent G, Terrat JC, et al. Hemodialyse, syndrome du canal carpien et substance amyloide. Nouv Press Med 24: 1715, 1980. Google Scholar 5 Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, Kunimoto T, Kataoka H, Suzuki M, Hirasawa Y, Shirahama T, Cohen AS, Schmid K: A new form of amyloid protein associated with chronic haemodialysis was identified as beta 2 microglobulin. Biochem Biophys Res Commun 129: 701–706, 1985. 10.1016/0006-291X(85)91948-5 CASPubMedWeb of Science®Google Scholar 6 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. 10.1172/JCI112257 CASPubMedWeb of Science®Google Scholar 7 Gejyo F, Odani S, Yamada T, Honma N, Saito H, Suzuki Y, Nakagawa Y, Kobayashi H, Maruyama Y, Hirasawa Y, Suzuki M, Arakawa M. Beta 2 microglobulin, a new form of amyloid protein associated with chronic hemodialysis. Kidney Int 30: 385–390, 1986. 10.1038/ki.1986.196 CASPubMedWeb of Science®Google Scholar 8 Connors LH, Shirahama T, Skinner M, Fenves A, Cohen AS: In vitro formation of amyloid fibrils from intact beta 2 microglobulin. Biochem Biophys Res Commun 131: 1063–1068, 1985. 10.1016/0006-291X(85)90198-6 CASPubMedWeb of Science®Google Scholar 9 Gejyo F, Homma N, Suzuki Y, Arakawa M: Serum levels of beta 2 microglobulin, as a new form of amyloid protein in patients undergoing long-term hemodialysis. N Engl J Med 314: 585–586, 1986. 10.1056/NEJM198602273140920 CASPubMedWeb of Science®Google Scholar 10 Argiles A, Mourad G, Berta PH, Polito C, Canaud B, Robinet-Levy M, Mion C: Dialysis associated amyloidosis in a patient on long-term post-dilutional hemofiltration. Nephron 46: 96–97, 1987. 10.1159/000184316 CASPubMedWeb of Science®Google Scholar 11 Glenner GG, Ein D, Eanes ED, Bladen HA, Terry WD, Page DL: Creation of amyloid fibrils from Bence Jones proteins in vitro. Science 174: 712–714, 1971. 10.1126/science.174.4010.712 CASPubMedWeb of Science®Google Scholar 12 Linke RP, Zucker-Franklin D, Franklin EC: Morphologic, chemical and immunologic studies of amyloid-like fibrils formed from Bence Jones proteins by proteolysis. J Immunol 111: 10–23, 1973. CASPubMedWeb of Science®Google Scholar 13 Shirahama T, Benson MD, Cohen AS, Tanaka A: Fibrillar assemblage of variable segments of immunoglobulin light chains: An electron microscopy study. J Immunol 110: 21–30, 1973. CASPubMedWeb of Science®Google Scholar 14 Epstein WV, Tan M, Wood IS: Formation of amyloid in vitro by action of human kidney lysosomal enzymes on Bence Jones proteins. J Lab Clin Med 84: 107–110, 1974. CASPubMedWeb of Science®Google Scholar 15 Glenner GG: Amyloid deposits and amyloidosis. N Engl J Med 302: 1283–1292, 1333–1343, 1980. 10.1056/NEJM198006053022305 CASPubMedWeb of Science®Google Scholar 16 Glenner GG, Harbaugh J, Ohms JI, Harada M, Cuatrecasas P: An amyloid protein: The amino-termino variable fragment of an immunoglobulin light chain. Biochem Biophys Res Commun 41: 1287–1289, 1970. 10.1016/0006-291X(70)90227-5 CASPubMedWeb of Science®Google Scholar 17 Page DL, Isersky C, Harada M, Glenner GG: Immunoglobulin origin of localized nodular pulmonary amyloidosis. Res Exp Med (Berl) 159: 75–86, 1972. 10.1007/BF01856034 PubMedGoogle Scholar 18 Sletten K, Husby G, Natvig JB: N-terminal aminoacid sequence of amyloid fibril protein AR, prototype of a new lambda-variable subgroup, VlambdaV. Scand J Immunol 3: 833–836, 1974. 10.1111/j.1365-3083.1974.tb01319.x CASPubMedWeb of Science®Google Scholar 19 Skinner M, Benson MD, Cohen AS: Amyloid fibril protein related to immunoglobulin lambda-chains. J Immunol 114: 1433–1435, 1975. CASPubMedWeb of Science®Google Scholar 20 Lavie G, Zucker-Franklin D, Franklin EC: Degradation of serum A protein by surface associated enzymes of human blood monocytes. J Exp Med 148: 1020–1031, 1978. 10.1084/jem.148.4.1020 CASPubMedWeb of Science®Google Scholar 21 Husebekk A, Skogen B, Husby G, Marhaug G: Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scand J Immunol 21: 283–287, 1985. 10.1111/j.1365-3083.1985.tb01431.x CASPubMedWeb of Science®Google Scholar 22 Saraiva MJM, Birken S, Costa PP, Goodman DS: Family studies of the genetic abnormality in transthyretin (prealbumin) in Portuguese patients with familial amyloidotic neuropathy. Ann NY Acad Sci 435: 86–100, 1984. 10.1111/j.1749-6632.1984.tb13742.x CASPubMedWeb of Science®Google Scholar 23 Nakazato M, Kangawa K, Minamino N, Tawara S, Matsuo H, Araki S: Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin. Biochim Biophys Res Commun 123: 921–928, 1984. 10.1016/S0006-291X(84)80222-3 CASPubMedWeb of Science®Google Scholar 24 Wallace MR, Dwulet FE, Conneally PM, Benson MD: Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest 78: 6–12, 1986. 10.1172/JCI112573 CASPubMedWeb of Science®Google Scholar 25 Dwulet FE, Benson MD: Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss) J Clin Invest 78: 880–886, 1986. 10.1172/JCI112675 CASPubMedWeb of Science®Google Scholar 26 Ericson LH, Eriksen N, Walsh KA, Benditt EP: Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor. FEBS Lett 218: 11–16, 1987. 10.1016/0014-5793(87)81008-6 CASPubMedWeb of Science®Google Scholar 27 Buxbaum J: Aberrant immunoglobulin synthesis in light chain amyloidosis. J Clin Invest 78: 798–806, 1986. 10.1172/JCI112643 CASPubMedWeb of Science®Google Scholar 28 Werdelin O, Ranlov P: Amyloidosis in mice produced by transplantation of spleen cells from casein-treated mice. Acta Pathol Microbiol Immunol Scand 68: 1–8, 1966. 10.1111/apm.1966.68.1.1 CASPubMedWeb of Science®Google Scholar 29 Kisilevsky R, Boudreau L: Kinetics of amyloid deposition. I. The effects of amyloid enhancing factor and splenectomy. Lab Invest 48: 53–59, 1983. CASPubMedWeb of Science®Google Scholar 30 Snow AD, Willmer J, Kisilevsky R: Sulfated glycosaminoglycans: A common constituent of all amyloids Lab Invest 56: 120–123, 1987. CASPubMedWeb of Science®Google Scholar 31 Snow AD, Kisilevsky R: Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: A histochemical study. Lab Invest 53: 37–44, 1985. CASPubMedWeb of Science®Google Scholar 32 Kisilevsky R: From arthritis to Alzheimer's disease: current concepts on the pathogenesis of amyloidosis. Can J Physiol Pharmacol 65: 1805–1815, 1987. 10.1139/y87-282 CASPubMedWeb of Science®Google Scholar 33 Pepys MB, Baltz M, De Beer FC, et al. Biology of serum amyloid P component. Ann NY Acad Sci 389: 286–297, 1982. 10.1111/j.1749-6632.1982.tb22144.x CASPubMedWeb of Science®Google Scholar 34 Pepys MB: Amyloidosis: Aspects of structure, pathogenesis and management. in Nephrology. edited by AM Davidson. London , Balliere Tindall, 1988, pp 761–778. Google Scholar 35 Li JJ, McAdam PW: Human amyloid P component: An elastase inhibitor. Scand J Immunol 20: 219–224, 1984. 10.1111/j.1365-3083.1984.tb00995.x CASPubMedWeb of Science®Google Scholar 36 Pepys MB: Amyloid P-component: Structure and properties. in Amyloidosis edited by J Marrink, M VanRijswijk, Dordrecht , The Netherlands , Martinus Nijhoff, 43–50, 1986. 10.1007/978-94-009-4309-4_5 Google Scholar 37 Pepys FC, Dyck RF, De Beer FC, Skinner M, Cohen AS: Binding of serum amyloid P-component (SAP) by amyloid fibrils. Clin Exp Immunol 38: 284–296, 1979. CASPubMedWeb of Science®Google Scholar 38 Hamazaki H: Ca2+-mediated association of human amyloid P component with heparan sulfate and dermatan sulfate. J Biol Chem 262: 1456–1460, 1987. CASPubMedWeb of Science®Google Scholar 39 Cary NRB, Sethy D, Brown EA, Erhardt CC, Wooddrow DF, Gower PE: Dialysis arthropathy, amyloid or iron Br Med J 293: 1392–1394, 1986. 10.1136/bmj.293.6559.1392 CASPubMedWeb of Science®Google Scholar 40 Argiles A, Mourad G, Axelrud-Cavadore C, Derancourt J, Jauregui-Adell J, Mion C, Cavadore JC: Haemodialysis associated amyloidosis: Beta 2 microglobulin alone or associated with globin chains Clin Sci 73: 515–518, 1987. 10.1042/cs0730515 CASPubMedWeb of Science®Google Scholar 41 Gorevic PD, Munoz PC, Casey TT, DiRaimondo CR, Stone WJ, Prelli FC, Rodriguez MM, Poulik MD, Frangione B: Polymerization of intact beta 2 microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. Proc Natl Acad Sci USA 83: 7908–7912, 1986. 10.1073/pnas.83.20.7908 CASPubMedWeb of Science®Google Scholar 42 Linke RP, Bommer J, Ritz E, Waldherr R, Eulitz M: Amyloid kidney stones of uremic patients consist of beta 2 microglobulin fragments. Biochem Biophys Res Commun 136: 665–671, 1986. 10.1016/0006-291X(86)90492-4 CASPubMedWeb of Science®Google Scholar 43 Linke RP, Hampl H, Bartel-Schwartze S, Eulitz M: Beta 2 microglobulin, different fragments and polymers thereof in synovial amyloid in long-term hemodialysis. Biol Chem Hoppe Seyler 368: 137–144, 1987. 10.1515/bchm3.1987.368.1.137 CASPubMedWeb of Science®Google Scholar 44 Linke RP, Hampl H, Lobeck H, Ritz E, Bommer J, Waldherr R, Eulitz M: Lysine-specific cleavage of B2M in amyloid deposits associated with hemodialysis. Kidney Int 36: 675–681, 1989. 10.1038/ki.1989.245 CASPubMedWeb of Science®Google Scholar 45 Argilés A: Dialysis arthropathy: Amyloid or iron. Br Med J 294: 9751, 1987. 10.1136/bmj.294.6577.975-a Google Scholar 46 Skogen B, Natvig JB: Degradation of amyloid proteins by different serine proteases. Scand J Immunol 14: 389–396, 1981. 10.1111/j.1365-3083.1981.tb00579.x CASPubMedWeb of Science®Google Scholar 47 Argiles A, Mourad G, Axelrud-Cavadore C, Watrin A, Mion C, Cavadore JC: High molecular-mass proteins in haemodialysis-associated amyloidosis. Clin Science 76: 547–552, 1989. 10.1042/cs0760547 CASPubMedWeb of Science®Google Scholar 48 Harpel P: Alpha 2 macroglobulin. in The Chemistry and Pathology of the Human Plasma Proteins, edited by DH Bing, New York , Pergamon Press 1979, pp 385–399. Google Scholar 49 Sottrup-Jensen L. α-Macroglobulins: Structure, shape and mechanism of proteinase complex formation. J Biol Chem 264: 11539–11542, 1989. CASPubMedWeb of Science®Google Scholar 50 Imbert MJ, Pizzo SV, Johnson WJ, Adams DO: Selective diminution of the binding of mannose by murine macrophages in the late stages of activation. J Biol Chem 257: 5129–5135, 1982. PubMedWeb of Science®Google Scholar 51 Johnson WJ, Pizzo SV, Imber MJ, Adams DO: Receptors for maleylated proteins regulate secretion of neutral proteases by murine macrophages. Science 218: 574–576, 1982. 10.1126/science.6289443 CASPubMedWeb of Science®Google Scholar 52 Curatola G, Malara E, Sisca S, Postorino M, Cutrupi S, Maggiore Q: Biological markers of inflammation and carpal tunnel syndrome (CTS) in dialysis patients (Abstract). Nephrol Dial Transpl 4(5): 492, 1989. Google Scholar 53 Argiles A, Mourad G, Atkins RC, Mion C: Haemodialysis associated amyloidosis (HDAA) and antiproteases (Abstract). Nephrol Dial Transpl 4(5): 492, 1989. Google Scholar 54 Tanzi RE, McClatchey AI, Lamperti ED, Villa-Kamorov L, Gusella JF, Neve RL: Protease inhibition encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature 331: 528–530, 1988. 10.1038/331528a0 CASPubMedWeb of Science®Google Scholar 55 Ponte P, Gonzalez-Dewhitt P, Miller J, Hsu D, Greenberg B, Davis K, Wallace W, Lieberburg I, Fuller F, Cordell B: A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature 331: 525–528, 1988. 10.1038/331525a0 CASPubMedWeb of Science®Google Scholar 56 Kitaguchi N, Takahashi Y, Tokushima Y, Shiojiri S, Cole G: Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature 331: 530–532, 1988. 10.1038/331530a0 CASPubMedWeb of Science®Google Scholar 57 Oltersdof T, Fritz LC, Schenk DB, Liebergurg I, Johnson-Wood KL, Beattie EC, Ward P, Blacher RW, Dovey HF, Sinha S: The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II. Nature 341: 144–147, 1989. 10.1038/341144a0 CASPubMedWeb of Science®Google Scholar 58 Ghiso J, Jensson O, Frangione B: Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cistatin C). Proc Natl Acad Sci USA 83: 2974–2978, 1986. 10.1073/pnas.83.9.2974 CASPubMedWeb of Science®Google Scholar Citing Literature Volume3, Issue3July 1990Pages 149-151 ReferencesRelatedInformation

Referência(s)
Altmetric
PlumX