Differential analysis of D-beta-Asp-containing proteins found in normal and infrared irradiated rabbit lens

Biochemical and Biophysical Research Communications
Takumi TakataNoriko Fujii

Abstract

Although proteins are generally composed of l-alpha-amino acids, d-beta-aspartic acid (Asp)-containing proteins have been reported in various elderly tissues. Our previous study detected several d-beta-Asp-containing proteins in a rabbit lens derived from epithelial cell line by Western blot analysis of a 2D-gel using a polyclonal antibody that is highly specific for d-beta-Asp-containing proteins. The identity of each spot was subsequently determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and the Ms-Fit online database searching algorithm. In this study, we discovered novel d-beta-Asp-containing proteins from rabbit lens. The results indicate that beta-crystallin A3, beta-crystallin A4, beta-crystallin B1, beta-crystallin B2, beta-crystallin B3, gamma-crystallin C, gamma-crystallin D, and lambda-crystallin in rabbit lens contain d-beta-Asp residues. Furthermore, the occurrence of d-beta-Asp residues increases with infrared ray (IR) irradiation. Additionally, some d-beta-Asp-containing proteins only appear after IR irradiation. One such protein is the alpha-enolase, which shows homology to tau-crystallin.

References

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Jul 26, 2005·Biochemical and Biophysical Research Communications·Takumi TakataNoriko Fujii

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Citations

Jun 27, 2019·The Journal of Biological Chemistry·Rebeccah A WarmackSteven G Clarke
Sep 8, 2006·Biochemical and Biophysical Research Communications·David Sheehan

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