Extracellular matrix components modulate different stages in β₂-microglobulin amyloid formation.

ABSTRACT: Amyloid deposition of WT human β₂-microglobulin (WT-hβ₂m) in the joints of long-term hemodialysis patients is the hallmark of dialysis-related amyloidosis. In vitro, WT-hβ₂m does not form amyloid fibrils at physiological pH and temperature unless co-solvents or other reagents are added. Therefore, understanding how fibril formation is initiated and maintained in the joint space is important for elucidating WT-hβ₂m aggregation and dialysis-related amyloidosis onset. Here, we investigated the roles of collagen I and the commonly administered anticoagulant, low-molecular-weight (LMW) heparin, in the initiation and subsequent aggregation phases of WT-hβ₂m in physiologically relevant conditions. Using thioflavin T fluorescence to stu

SUBMITTER: Benseny-Cases N 

PROVIDER: S-EPMC6579475 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature