The amyloid fibrils of the constant domain of immunoglobulin light chain

Kaori Yamamoto, Hisashi Yagi, Young Ho Lee, József Kardos, Yoshihisa Hagihara, Hironobu Naiki, Yuji Goto

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14 Citations (Scopus)

Abstract

Light chain-associated (AL) amyloidosis is characterized by dominant fibril deposition of the variable domain (VL) of an immunoglobulin light chain, and thus its constant domain (CL) has been considered not to be amyloidogenic. We examined the in vitro fibril formation of the isolated CL in comparison with β2-microglobulin (β2-m), an immunoglobulin domain-like amyloidogenic protein responsible for dialysis-related amyloidosis. Two methods useful for β2-m at neutral pH also induced amyloid fibrils of CL, which were monitored by thioflavin-T binding and electron microscopy (EM). These results suggest that CL plays an important role, more than previously assumed, in the development of AL-amyloidosis.

Original languageEnglish
Pages (from-to)3348-3353
Number of pages6
JournalFEBS letters
Volume584
Issue number15
DOIs
Publication statusPublished - Aug 1 2010

Keywords

  • AL-amyloidosis
  • Amyloid fibril
  • Dialysis-related amyloidosis
  • Immunoglobulin domain
  • β-Microglobulin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Yamamoto, K., Yagi, H., Lee, Y. H., Kardos, J., Hagihara, Y., Naiki, H., & Goto, Y. (2010). The amyloid fibrils of the constant domain of immunoglobulin light chain. FEBS letters, 584(15), 3348-3353. https://doi.org/10.1016/j.febslet.2010.06.019