Abstract
β2-microglobulin (β2m) is capable of forming amyloid in osteoarticular structures in kidney failure patients that undergo chronic hemodialysis treatment. Although sophisticated analytical methods have yielded comprehensive data about the conformation of the native protein both as a monomer and as the light chain of the type I major histocompatibility complex, the cause and mechanisms leading to the transformation of β2m into amyloid deposits in patients with dialysis-related amyloidosis are unsettled. The impact on conformational stability of various truncations, cleavages, amino acid substitutions, and divalent cations, especially Cu2+, however, are highly relevant for understanding β2m unfolding pathways leading to amyloid formation. This review describes the current knowledge about such conformationally destabilizing and amyloidogenic factors and links these to the structure and function of β2m in normal physiology and pathology. Tables listing modifications of β2m found in amyloid from patients and a systematic overview of laboratory conditions conducive to β2m-fibrillogenesis are also included.
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