Destruction of Amyloid Fibrils of Keratoepithelin Peptides by Laser Irradiation Coupled with Amyloid-specific Thioflavin T

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Abstract

This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Yuichi Kaji, Hisashi Yagi, Kazumasa Sakurai, Toru Kawakami, Hironobu Naiki, and Yuji Goto. Destruction of Amyloid Fibrils of Keratoepithelin Peptides byLaser Irradiation Coupled with Amyloid-specific Thioflavin T. J. Biol. Chem. 2011; 286, 10856-10863. © the American Society for Biochemistry and Molecular Biology

Mutations in keratoepithelin are associated with blinding ocular diseases, including lattice corneal dystrophy type 1 and granular corneal dystrophy type 2. These diseases are characterized by deposits of amyloid fibrils and/or granular non-amyloid aggregates in the cornea. Removing the deposits in the cornea is important for treatment. Previously, we reported the destruction of amyloid fibrils of β2-microglobulin K3 fragments and amyloid β by laser irradiation coupled with the binding of an amyloid-specific thioflavin T. Here, we studied the effects of this combination on the amyloid fibrils of two 22-residue fragments of keratoepithelin. The direct observation of individual amyloid fibrils was performed in real time using total internal reflection fluorescence microscopy. Both types of amyloid fibrils were broken up by the laser irradiation, dependent on the laser power. The results suggest the laser-induced destruction of amyloid fibrils to be a useful strategy for the treatment of these corneal dystrophies.

Journal

  • Journal of Biological Chemistry

    Journal of Biological Chemistry 286(12), 10856-10863, 2011-03

    American Society for Biochemistry and Molecular Biology

Codes

  • NII Article ID (NAID)
    120006557644
  • NII NACSIS-CAT ID (NCID)
    AA1202453X
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    1083-351X
  • Data Source
    IR 
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