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Related Experiment Videos

Structural prerequisites for serum amyloid A fibril formation

M C de Beer1, F C de Beer, W D McCubbin

  • 1Department of Medicine, University of Kentucky Medical Center, Lexington 40536.

The Journal of Biological Chemistry
|September 25, 1993
PubMed
Summary

The CE/J mouse strain exhibits remarkable resistance to amyloid A protein (AA) amyloidosis. This resistance stems from a unique apo-SAA isoform that prevents beta-sheet folding, crucial for amyloid fibril formation.

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Area of Science:

  • Biochemistry
  • Genetics
  • Immunology

Background:

  • Experimental amyloid A protein (AA) amyloidosis studies predominantly use BALB/c mice.
  • In BALB/c mice, SAA1 and SAA2 are major apo-SAA isoforms; only apo-SAA2 deposits as amyloid fibrils.
  • No mouse strain has demonstrated complete resistance to amyloid induction previously.

Purpose of the Study:

  • To investigate the resistance of the CE/J mouse strain to amyloidogenesis.
  • To identify the molecular basis for CE/J mouse resistance to amyloid formation.

Main Methods:

  • Comparative analysis of apo-SAA isoforms in different mouse strains.
  • Circular dichroism (CD) studies to analyze protein folding.
  • Investigation of apo-SAA isoform interaction with heparan sulfate proteoglycan.

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Main Results:

  • CE/J mice are highly resistant to amyloidogenesis.
  • CE/J mice possess a unique single apo-SAA isoform (pI 6.15), a hybrid of SAA1 and SAA2.
  • This CE/J apo-SAA isoform does not undergo typical beta-sheet folding when bound to heparan sulfate proteoglycan, unlike apo-SAA2.

Conclusions:

  • The unique apo-SAA isoform in CE/J mice is responsible for their resistance to amyloid formation.
  • Heparan sulfate proteoglycan-induced beta-sheet folding of apo-SAA2 is critical for amyloidogenesis.
  • This finding offers new insights into the mechanisms of AA amyloidosis.