Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation

FEBS Lett. 2006 Jan 23;580(2):491-6. doi: 10.1016/j.febslet.2005.12.047. Epub 2005 Dec 22.


Transthyretin (TTR) amyloid fibril formation, which is triggered by the dissociation of tetrameric TTR, appears to be the causative factor in familial amyloidotic polyneuropathy and senile systemic amyloidosis. Binding of thyroxine (T(4)), a native ligand of TTR, stabilizes the tetramer, but the bioavailability of T(4) for TTR binding is limited due to the preferential binding of T(4) to globulin, the major T(4) carrier in plasma. Here, we show that Cr(3+) increased the T(4)-binding capacity of wild-type (WT) and amyloidogenic V30M-TTR. Moreover, we demonstrate that Cr(3+) and T(4) cooperatively suppressed in vitro fibril formation due to the stabilization of WT-TTR and V30M-TTR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Chromium / chemistry*
  • Chromium / metabolism
  • Humans
  • Point Mutation
  • Prealbumin / chemistry*
  • Prealbumin / genetics
  • Prealbumin / metabolism*
  • Protein Binding
  • Protein Structure, Quaternary*
  • Thyroxine / metabolism*


  • Amyloid
  • Prealbumin
  • Chromium
  • Thyroxine