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Dialysis-related amyloidosis

Jonathan Kay, MD
William L Henrich, MD, MACP
Wajeh Y Qunibi, MD
Section Editors
Jeffrey S Berns, MD
Steve J Schwab, MD
Deputy Editor
Alice M Sheridan, MD


Dialysis-related amyloidosis (DRA) is a disabling disease characterized by accumulation and tissue deposition of amyloid fibrils consisting of beta2-microglobulin (beta2-m) in the bone, periarticular structures, and viscera of patients with chronic kidney disease (CKD) [1-8]. Beta2-m is a component of the major histocompatibility complex that is present on cell surfaces and is normally cleared by glomerular filtration, with subsequent reabsorption and catabolism in proximal tubules. Clearance declines in patients with reduced kidney function, which leads to plasma accumulation and slow tissue deposition.

The prevalence of DRA has decreased with the use of high-flux biocompatible membranes, which provide better clearance of beta2-m and are less likely to induce reactive inflammation. (See 'Epidemiology and risk factors' below.)

However, even these more modern hemodialysis therapies can be associated with retention of beta2-m. An overview of DRA is presented in this topic review. Other bone diseases and other complications associated with renal disease are discussed elsewhere. (See "Overview of chronic kidney disease-mineral bone disease (CKD-MBD)" and "Management of secondary hyperparathyroidism and mineral metabolism abnormalities in adult predialysis patients with chronic kidney disease" and "Management of secondary hyperparathyroidism and mineral metabolism abnormalities in dialysis patients" and "Complications of hemodialysis in the older patient".)

Other forms of amyloidosis are also discussed elsewhere. (See "Overview of amyloidosis".)


DRA is characterized by the tissue deposition of beta2-microglobulin (beta2-m) amyloid, particularly in bone, articular cartilage, synovium, muscle, tendons, and ligaments [9-11]. Beta2-m amyloid also deposits in other tissues, especially blood vessels [10,12] and the gastrointestinal tract [12]. In contrast to fragments of immunoglobulin light chains in primary amyloidosis and serum amyloid A in secondary amyloidosis, the amyloid protein in DRA is composed primarily of beta2-m [2,13,14].


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