Abstract
Dialysis-related amyloidosis (DRA), which is an inevitable complication of long-term haemodialysis (HD), manifests major clinic-pathological characteristics, including carpal tunnel syndrome, which is the most common clinical sign; systemic involvement of many articular tissues; and the presence of β2-microglobulin (β2M) as a precursor protein in this amyloidosis.
Highlights
Amyloid is a fibrillar protein and is primarily a conformational variant of an originally globular precursor protein. β2M is an essential protein for normal conformation of major histocompatibility complex class I molecules on cell membranes and is degraded mainly in renal proximal tubules. β2M passes freely across vascular walls
HD can clear as much as 70% of circulating β2M, β2M in the interstitial space can accumulate and progressively lead to development of Dialysis-related amyloidosis (DRA) [1]
We have studied the amyloidogenicity of β2M and found a previously unknown amyloidogenic process, which we describe in this short review
Summary
Amyloid is a fibrillar protein and is primarily a conformational variant of an originally globular precursor protein. β2M is an essential protein for normal conformation of major histocompatibility complex class I molecules on cell membranes and is degraded mainly in renal proximal tubules. β2M passes freely across vascular walls. Amyloid is a fibrillar protein and is primarily a conformational variant of an originally globular precursor protein. Serum levels of β2M are extremely high in patients undergoing HD. HD can clear as much as 70% of circulating β2M, β2M in the interstitial space can accumulate and progressively lead to development of DRA [1].
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