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Nephrol Dial Transplant (2001) 16: 12-16
© 2001 European Renal Association-European Dialysis and Transplant Association


Scintigraphic methods to detect ß2-microglobulin associated amyloidosis (Aß2-microglobulin amyloidosis)

Jürgen Floege, Jürgen Schäffer1 and Karl Martin Koch1

Division of Nephrology, Department of Medicine, University of Aachen and 1 Division of Nephrology, Department of Medicine, University of Hannover, Germany

Abstract

ß2-Microglobulin-derived amyloidosis (Aß2m) represents a major cause or morbidity in patients with end-stage renal disease. Symptoms of Aß2m amyloid are mainly related to (peri-) articular amyloid deposition. Conventional non-invasive diagnostic techniques, i.e. clinical evaluation, joint ultrasonography or X-ray, computed tomography or magnetic resonance imaging findings, as well as conventional bone scans, suffer from relative non-specificity and/or low sensitivity. Two recent methods, namely scintigraphy with radiolabelled serum amyloid P component (SAP) or with the radiolabelled Aß2m-precursor protein, ß2-microglobulin (ß2m), yield more specific information. Using 123I-labelled SAP, Aß2m deposits have been visualized in several long-term haemodialysis (HD) patients. However, this scan did not show tracer accumulation in other frequently involved sites, such as hips or shoulders, but did frequently label the spleen, which is usually spared from Aß2m deposits. Scanning with 131I-labelled ß2m, in contrast, yielded tracer accumulations corresponding to the typical distribution pattern of Aß2m. Specificity of this method was shown by several methods, and the sensitivity was found to markedly exceed that of combined clinical and radiological investigations. Recently, both the radiation exposure and the optical resolution of this latter scan have been further refined by substituting 131I with 111In. In a final step we generated recombinant human ß2m (rhß2m). 111In-rhß2m again failed to show significant tracer accumulation over joint regions in patients on short-term HD without evidence of Aß2m amyloidosis. In contrast, local tracer accumulations similar to those observed with natural, 111In-labelled ß2m could be demonstrated in long-term HD patients with evidence of Aß2m amyloidosis. In conclusion, scintigraphy for Aß2m with 111In-labelled rhß2m provides a homogenous and safe recombinant protein source, and allows for the sensitive and specific non-invasive detection of Aß2m-amyloid deposits in dialysis patients.

Notes

Correspondence and offprint requests to: J. Floege, Medizinische Klinik II, University of Aachen, D-52057 Aachen, Germany.


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