Characterization of new D-beta-aspartate-containing proteins in a lens-derived cell line |
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Authors: | Takata Takumi Shimo-Oka Tadashi Miki Kunio Fujii Noriko |
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Affiliation: | Research Reactor Institute, Kyoto University, Kumatori-cho, Sennan, Osaka 590-0494, Japan. |
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Abstract: | Although proteins are generally composed of l-alpha-amino acids, biologically uncommon D-beta-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-beta-Asp-containing proteins of approximately 50 kDa by Western blot analysis of a 2D-gel using a polyclonal antibody that is highly specific for D-beta-Asp-containing proteins. In this study, we identified the D-beta-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 tau-crystallin. Other D-beta-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, alpha-B-crystallin, and peptidyl-prolyl cis-trans isomerase A (PPlase). |
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Keywords: | α-Crystallin Enzyme smallcaps" >d-β-Aspartate Lens Cell line Western blot analysis Two-dimensional electrophoresis smallcaps" >d-Amino acid Posttranslational modification Proteomics |
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