Characterization of new d-β-aspartate-containing proteins in a lens-derived cell line
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- 作者：Takumi Takata ; Tadashi Shimo-Oka ; Kunio Miki and Noriko Fujii
- 关键词：α ; -Crystallin ; Enzyme ; d-β ; -Aspartate ; Lens ; Cell line ; Western blot analysis ; Two-dimensional electrophoresis ; d-Amino acid ; Posttranslational modification ; Proteomics
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2005
- 出版时间：2005
- 年：2005
- 卷：334
- 期：4
- 页码：1022-1031
- 全文大小：297 K
文摘
Although proteins are generally composed of l-α-amino acids, biologically uncommon d-β-aspartic acid (Asp)-containing proteins have been reported in various tissues from elderly individuals. Our previous study indicated that the N/N1003A cell line, derived from rabbit lens, includes d-β-Asp-containing proteins of 50 kDa by Western blot analysis of a 2D-gel using a polyclonal antibody that is highly specific for d-β-Asp-containing proteins. In this study, we identified the d-β-Asp-containing proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and the Mascot online database searching algorithm. The results indicate that one of these 50 kDa proteins is an enolase showing homology with τ-crystallin. Other d-β-Asp-containing proteins, which we have recently discovered include lamin A/C, cytoplasmic NADP+-dependent isocitrate dehydrogenase, fructose-bisphosphate aldolase A, aldose reductase, l-lactate dehydrogenase A or calponin H2, phosphoglycerate mutase 1, phosphatidylethanolamine-binding protein, α-B-crystallin, and peptidyl-prolyl cis–trans isomerase A (PPlase).