Dialysis amyloid

Hirakura, Y., and Kagan, B. L. (2001). Pore formation by beta-2-microglobulin A mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid 8, 94-100. 

A cross-jS spine model was proposed for the fibril structure of human /]2-microglobulin (h/]2m) (Ivanova et al., 2004). h/I2m is a 99-amino acid serum protein with a 7-stranded /(-sandwich fold (Fig. 10A Saper et al, 1991). In patients on long-term kidney dialysis, the protein is deposited as amyloid fibrils in the joints (Floege and Ehlerding, 1996 Koch, 1992). In vitro-formed fibrils of h/)2m give a cross-/] X-ray diffraction pattern (Ivanova et al., 2004 Smith et al., 200S). Several studies have shown that segments of h/]2m form amyloid-like fibrils on their own (Ivanova et al., 2003 Jones et al., 2003 Kozhukh et al, 2002). 

Chaussidon M, Netter P, Kessler M, et al. 1993. Dialysis-associated arthropathy Secondary ion mass spectrometry evidence of aluminum silicate in beta2-microglobulin amyloid synovial tissue and articular cartilage. Nephron 65 559-563. 

Further differentiation distinguishes between AF amyloid (ATTR) (amyloid types in familial amyloidosis), endocrine EA amyloid and AS amyloid (occasionally detected in old age in its isolated form in the heart as well as in the brain) and AB amyloid (Af2m) (often observed in the osseous system during long-term dialysis). 

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