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Serum amyloid P component accelerates the formation and enhances the stability of amyloid fibrils in a physiologically significant under-saturated solution of amyloid-β42.

Abstract
The mechanism whereby an under-saturated solution of amyloid-β (Aβ)42 precipitates as β sheets in vivo in Alzheimer's disease remains to be elucidated. Herein we present in vitro evidence that serum amyloid P component may mediate this process through its acceleration of amyloid formation from an under-saturated solution of Aβ42 and subsequently its stabilization of the amyloid fibrils formed over physiologically significant timeframes. Our observations support serum amyloid P component as a therapeutic target in Alzheimer's disease.
AuthorsMatthew Mold, Annette K Shrive, Christopher Exley
JournalJournal of Alzheimer's disease : JAD (J Alzheimers Dis) Vol. 29 Issue 4 Pg. 875-81 ( 2012) ISSN: 1875-8908 [Electronic] Netherlands
PMID22337829 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Amyloid
  • Amyloid beta-Peptides
  • Krebs-Henseleit solution
  • Peptide Fragments
  • Serum Amyloid P-Component
  • amyloid beta-protein (1-42)
  • Tromethamine
  • Copper
  • Aluminum
  • Magnesium
  • Glucose
  • Calcium
Topics
  • Aluminum (pharmacology)
  • Amyloid (drug effects, metabolism, ultrastructure)
  • Amyloid beta-Peptides (pharmacology)
  • Animals
  • Calcium (metabolism)
  • Copper (pharmacology)
  • Dose-Response Relationship, Drug
  • Glucose (pharmacology)
  • Humans
  • Magnesium (pharmacology)
  • Peptide Fragments (pharmacology)
  • Protein Structure, Secondary
  • Serum Amyloid P-Component (drug effects, metabolism, pharmacology, ultrastructure)
  • Time Factors
  • Tomography, X-Ray Computed
  • Tromethamine (pharmacology)

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