Study on the Anti-aggregation Function of Group 3 LEA Peptides using an in vivo Assay System for Intracellular Amyloidogenesis

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  • 細胞内タンパク質凝集アッセイ系を用いたG3LEAペプチドのタンパク質凝集抑制機能に関する研究
  • サイボウ ナイ タンパクシツ ギョウシュウ アッセイケイ オ モチイタ G3LEA ペプチド ノ タンパクシツ ギョウシュウ ヨクセイ キノウ ニ カンスル ケンキュウ

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Abstract

Here we examined whether a short model peptide which has two tandem repeats of the 11-mer motif of a group 3 late embryogenesis abundant (LEA) protein has anti-aggregation activity against aggregation-prone proteins in cells. For this purpose, we transiently expressed GFP-fused polyQ in mammalian cells in which the model peptide had been constitutively expressed in advance. By fluorescence microscopic measurements, we counted the number of cells involving aggregated GFP-fused polyQ and evaluated the degree of anti-aggregation as a function of time. Simultaneously, we measured anti-aggregation activity of LEA proteins from the anhydrobiotic midge, Polypedilum vanderplanki. Positive control experiments were performed for cells expressing a LEA protein derived from the anhydrobiotic nematode Aphelenchus avenae. As a result, it was shown that the model peptide has the anti-aggregation activity comparable to the native LEA protein in cells.

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