ABSTRACT
Assemat et al identified ß2-microglobulin amyloidosis (ß2m-A) in carpal tunnel from 9 dialysis patients. The prevalence of ß2m-A while progressing the dialysis treatment neighbored 100 percentages. The amyloid material was predominantly observed in tendons and joints, but it was also reported to involve heart, digestive tract, ears and other locations. In 1985, F. Gejyo et al purified and sequenced the main protein component of amyloid deposits obtained from the carpal tunnel of a dialysis patient. The first modifications that were proposed to explain the more acidic pI of the modified ß2m were deamidation of the Asn-17 and lysine specific N-terminal proteolysis. Since the clinical description of ß2m amyloidosis, much progress has been achieved. The main protein constituents have been identified, the cellular participation has been documented and some protein-protein and protein-cell interactions have been elucidated. The observations reported by S. Schwalbe et al are confirmed by our own clinical experience.
