Abstract
Amyloidosis is a generic term for a group of diseases caused by misfolding and extracellular accumulation of certain proteins as fibrillar deposits that stain with Congo red and produce pathognomonic green birefringence when viewed by microscopy under crossed polarised light. The process of amyloid formation and deposition causes progressive organ dysfunction. Amyloidosis is remarkably diverse and can be hereditary or acquired, localised or systemic and lethal or merely an incidental finding. So far, 27 different human proteins with in vivo amyloidogenic potential have been identified of which 15 cause systemic amyloidosis. The classification of amyloid is based on the fibril protein, and different amyloidogenic proteins give rise to distinct but frequently overlap** clinical syndromes. The kidneys are frequently involved in systemic amyloidosis (Table 29.1) which, without treatment, is usually fatal. Current management of amyloidosis is dependent upon determining the fibril protein and reducing its abundance. This can result in regression of amyloid deposits, prevention or recovery of organ failure and improved survival.
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References
Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006;75:333–66.
Greenwald J, Riek R. Biology of amyloid: structure, function, and regulation. Structure. 2010;18(10):1244–60. 3801–8.
Pepys MB. Amyloidosis. Annu Rev Med. 2006;57:223–41.
Palladini G, Lavatelli F, Russo P, Perlini S, Perfetti V, Bosoni T, et al. Circulating amyloidogenic free light chains and serum N-terminal natriuretic peptide type B decrease simultaneously in association with improvement of survival in AL. Blood. 2006;107(10):3854–8.
Tufveson G, Geerlings W, Brunner FP, Brynger H, Dykes SR, Ehrich JHH, et al. The combined report on regular dialysis and transplantation in Europe. XIX 1988. Nephrol Dial Transplant. 1989;4 Suppl 4:1–30.
Kyle RA, Therneau TM, Rajkumar SV, Offord JR, Larson DR, Plevak MF, et al. A long-term study of prognosis in monoclonal gammopathy of undetermined significance. N Engl J Med. 2002;346:564–9.
Kyle RA, Gertz MA. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin Hematol. 1995;32:45–59.
Wechalekar AD, Lachmann HJ, Goodman HJ, Bradwell A, Hawkins PN, Gillmore JD. AL amyloidosis associated with IgM paraproteinemia: clinical profile and treatment outcome. Blood. 2008;112:4009–16.
Perfetti V, Colli Vinarelli M, Anesi E, Garini P, Quaglini S, Ascari E, et al. The degrees of plasma cell clonality and marrow infiltration adversely influence the prognosis of AL amyloidosis patients. Haematologica. 1999;84(3):218–21.
Ballardie FW, Kerr DNS, Tennent G, Pepys MB. Haemodialysis versus CAPD: equal predisposition to amyloidosis? Lancet. 1986;i:795–6.
Jadoul M. Dialysis-related amyloidosis: importance of biocompatibility and age. Nephrol Dial Transplant. 1998;13((Suppl)):61–4.
Schwalbe S, Holzhauer M, Schaeffer J, Galanski M, Koch KM, Floege J. Beta 2-microglobulin associated amyloidosis: a vanishing complication of long-term hemodialysis? Kidney Int. 1997;52:1077–83.
Murphy CL, Wang S, Kestler D, Larsen C, Benson D, Weiss DT, et al. Leukocyte chemotactic factor 2 (LECT2)-associated renal amyloidosis: a case series. Am J Kidney Dis. 2010;56:1100–7.
Gertz MA, Leung N, Lacy MQ, Dispenzieri A, Zeldenrust SR, Hayman SR, et al. Clinical outcome of immunoglobulin light chain amyloidosis affecting the kidney. Nephrol Dial Transplant. 2009;24:3132–7.
Pinney JH, Lachmann HJ, Bansi L, Wechalekar AD, Gilbertson JA, Rowczenio D, et al. Outcome in renal AL amyloidosis following chemotherapy. J Clin Oncol. 2011;29(6):674–81.
Palladini G, Campana C, Klersy C, Balduini A, Vadacca G, Perfetti V, et al. Serum N-terminal pro-brain natriuretic peptide is a sensitive marker of myocardial dysfunction in AL amyloidosis. Circulation. 2003;107(19):2440–5.
Dispenzieri A, Kyle RA, Gertz MA, Therneau TM, Miller WL, Chandrasekaran K, et al. Survival in patients with primary systemic amyloidosis and raised serum cardiac troponins. Lancet. 2003;361(9371):1787–9.
Dispenzieri A, Gertz MA, Kyle RA, Lacy MQ, Burritt MF, Therneau TM, et al. Serum cardiac troponins and N-terminal pro-brain natriuretic peptide: a staging system for primary systemic amyloidosis. J Clin Oncol. 2004;22(18):3751–7.
Fish R, Pinney J, Jain P, Addison C, Jones C, Jayawardene S, et al. The incidence of major hemorrhagic complications after renal biopsies in patients with monoclonal gammopathies. Clin J Am Soc Nephrol. 2010;5(11):1977–80.
Benson MD. Ostertag revisited: the inherited systemic amyloidoses without neuropathy. Amyloid. 2005;12:75–87.
Gertz M, Merlini G. Definition of organ involvement and response to treatment in AL amyloidosis: an updated consensus opinion. Amyloid. 2010 (Abstract CP-B);17(Suppl 1):48–9.
Wechalekar AD, Merlini G, Gillmore JD, Russo P, Lachmann HJ, Perlini S, et al. N-terminal fragment of brain natriuretic peptide (NT-ProBNP) – a new response criterion in AL amyloidosis. Amyloid. 2010 (Abstract OP-081);17(Suppl 1):84–5.
Merlini G. Reducing the amyloid burden through immunotherapy: a major therapeutic advance. Nephrol Dial Transplant. 2011;26(5):1471–3.
Dember LM, Sanchorawala V, Seldin DC, Wright DG, LaValley M, Berk JL, et al. Effect of dose-intensive intravenous melphalan and autologous blood stem-cell transplantation on AL amyloidosis-associated renal disease. Ann Intern Med. 2001;134:746–53.
Bergesio F, Ciciani AM, Manganaro M, Palladini G, Santostefano M, Brugnano R, et al. Renal involvement in systemic amyloidosis: an Italian collaborative study on survival And renal outcome. Nephrol Dial Transplant. 2008;23:941–51.
Miyata T, Jadoul M, Kurokawa K, van Ypersele de Strihou C. Beta-2 microglobulin in renal disease. J Am Soc Nephrol. 1998;9:1723–35.
Traut M, Haufe CC, Eismann U, Deppisch RM, Stein G, Wolf G. Increased binding of beta-2-microglobulin to blood cells in dialysis patients treated with high-flux dialyzers compared with low-flux membranes contributed to reduced beta-2-microglobulin concentrations. Results of a cross-over study. Blood Purif. 2007;25:432–40.
Dember LM. Amyloidosis-associated kidney disease. J Am Soc Nephrol. 2006;17:3458–71.
Immonen K, Finne P, Hakala M, Kautiainen H, Pettersson T, Gronhagen-Riska C. No improvement in survival of patients with amyloidosis associated with inflammatory rheumatic diseases – data from the Finnish national registry for kidney diseases. J Rheumatol. 2008;35:1334–8.
Lachmann HJ, Gillmore JD, Wechalekar AD, Sattianayagam PT, Gibbs SDJ, Pinney JH, et al. Survival on dialysis and outcome after renal transplantation in AA amyloidosis. Amyloid. 2010;17 Suppl 1:73.
Sattianayagam P, Gibbs SDJ, Wechalekar AD, Lachmann HJ, Whelan CJ, Pinney JH, et al. Solid organ transplantation in AL amyloidosis. Amyloid. 2009;17:149.
Leung N, Griffin MD, Dispenzieri A, Haugen EN, Gloor JM, Schwab TR, et al. Living donor kidney and autologous stem cell transplantation for primary systemic amyloidosis (AL) with predominant renal involvement. Am J Transplant. 2005;5:1660–70.
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Gillmore, J.D., Lachmann, H.J. (2014). Amyloidosis. In: Harber, M. (eds) Practical Nephrology. Springer, London. https://doi.org/10.1007/978-1-4471-5547-8_29
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DOI: https://doi.org/10.1007/978-1-4471-5547-8_29
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