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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Kinetic analysis of the polymerization and depolymerization of beta(2)-microglobulin-related amyloid fibrils in vitro

Suguru Yamamoto1, Kazuhiro Hasegawa, Itaru Yamaguchi

  • 1Division of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Science, Niigata 951-8510, Japan.

Biochimica Et Biophysica Acta
|August 9, 2005
PubMed

Insights

Beta(2)-microglobulin amyloidosis in dialysis patients involves protein unfolding. Molecules like GAGs and PGs can stabilize amyloid fibrils, influencing deposition in vivo.

Area of Science:

  • Biochemistry
  • Medical Science
  • Protein Chemistry

Background:

  • Beta(2)-microglobulin amyloidosis (Abeta(2)M) is a complication for dialysis patients.
  • Partial unfolding of beta(2)-microglobulin (beta(2)-m) is key to amyloid fibril formation.
  • Amyloid-associated molecules may influence Abeta(2)M development.

Purpose of the Study:

  • To investigate the role of specific molecules in Abeta(2)M amyloid fibril formation and stabilization.
  • To explore how factors like pH, TFE, and anionic phospholipids affect beta(2)-m structure and fibril assembly.
  • To understand the impact of apolipoprotein E, glycosaminoglycans, and proteoglycans on Abeta(2)M amyloidosis.

Main Methods:

  • In vitro formation and extension of Abeta(2)M amyloid fibrils.
  • Utilizing low pH conditions (2.0-3.0) and neutral pH with chemical agents (TFE, sodium dodecyl sulfate).
  • Assessing the stabilizing effects of apolipoprotein E, GAGs (heparin), and PGs (biglycan) on amyloid fibrils and beta(2)-m.

Main Results:

  • Abeta(2)M fibril formation was initially observed at low pH.
  • Neutral pH with TFE or sodium dodecyl sulfate induced fibril extension and beta(2)-m unfolding.
  • ApoE, GAGs, and PGs stabilized Abeta(2)M fibrils at neutral pH, forming complexes.
  • Heparin enhanced fibril extension with TFE; biglycan induced polymerization of acid-denatured beta(2)-m.

Conclusions:

  • Specific molecules significantly influence beta(2)-m conformation and amyloid fibril stability.
  • These molecular interactions are critical for the in vivo deposition of Abeta(2)M amyloid fibrils.
  • Findings support the hypothesis that molecular factors modulate Abeta(2)M amyloidosis progression.

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