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

Núria Benseny-Cases1, Theodoros K Karamanos1, Cody L Hoop2

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Low-molecular-weight heparin promotes amyloid formation of wild-type human beta-2 microglobulin (WT-hβ2m), while collagen I has complex effects, influencing secondary nucleation and fibril growth in dialysis-related amyloidosis.

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Area of Science:

  • Biochemistry
  • Medical Research
  • Protein Aggregation

Background:

  • Dialysis-related amyloidosis is characterized by amyloid deposition of wild-type human beta-2 microglobulin (WT-hβ2m) in joints.
  • WT-hβ2m typically does not form amyloid fibrils in vitro under physiological conditions without additives.
  • Understanding the initiation and maintenance of WT-hβ2m fibril formation is crucial for addressing dialysis-related amyloidosis.

Purpose of the Study:

  • To investigate the roles of collagen I and low-molecular-weight (LMW) heparin in WT-hβ2m amyloid fibril formation.
  • To elucidate how these agents affect the initiation and aggregation phases of WT-hβ2m under physiologically relevant conditions.

Main Methods:

  • Utilized thioflavin T fluorescence to monitor amyloid formation kinetics.
  • Analyzed the impact of collagen I and LMW-heparin on specific stages of WT-hβ2m assembly.
  • Employed self-seeding and cross-seeding experiments with WT-hβ2m and a truncated variant.

Main Results:

  • LMW-heparin significantly promoted WT-hβ2m fibrillogenesis across all aggregation stages.
  • Collagen I decreased lag time with LMW-heparin but slowed aggregation rates at higher concentrations.
  • Collagen I interaction with WT-hβ2m fibrils attenuated surface-mediated growth, highlighting the role of secondary nucleation.

Conclusions:

  • Collagen I and LMW-heparin differentially modulate WT-hβ2m aggregation pathways.
  • These interactions significantly impact the kinetics of amyloid formation relevant to dialysis-related amyloidosis.
  • Secondary nucleation plays a key role in WT-hβ2m amyloid formation, influenced by collagen I.