Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10764214 | Biochemical and Biophysical Research Communications | 2010 | 5 Pages |
Abstract
⺠The de novo fibrillation of β2-microglobulin in dialysis related amyloidosis may involve the aggregation prone cleavage variant ÎK58-β2m. ⺠Glycosaminoglycans play a significant role for the consolidation of early ÎK58-β2m fibrils, thus enabling overt and irreversible fibrillation. ⺠The presence of heparan sulfate stabilizes the ÎK58-β2m fibrils and affect the morphology of these. ⺠The morphology of ÎK58-β2m fibrils clearly affects the ability of these to nucleate native β2m fibril formation.
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Authors
Dorthe B. Corlin, Christina K. Johnsen, Mogens H. Nissen, Niels H.H. Heegaard,