Immunoproteomic and Two-Dimensional Difference Gel Electrophoresis Analysis of Arabidopsis Dehydration Response Element-Binding Protein 1A (DREB1A)-Transgenic Potato
-
- Nakamura Rika
- Division of Novel Foods and Immunochemistry, National Institute of Health Sciences
-
- Satoh Rie
- Division of Novel Foods and Immunochemistry, National Institute of Health Sciences
-
- Nakamura Ryosuke
- Division of Novel Foods and Immunochemistry, National Institute of Health Sciences
-
- Shimazaki Takayoshi
- Gene Research Center, Graduate School of Life and Environmental Sciences, University of Tsukuba
-
- Kasuga Mie
- Biological Resources Division, Japan International Research Center for Agricultural Sciences (JIRCAS)
-
- Yamaguchi-Shinozaki Kazuko
- Biological Resources Division, Japan International Research Center for Agricultural Sciences (JIRCAS)
-
- Kikuchi Akira
- Gene Research Center, Graduate School of Life and Environmental Sciences, University of Tsukuba
-
- Watanabe Kazuo N.
- Gene Research Center, Graduate School of Life and Environmental Sciences, University of Tsukuba
-
- Teshima Reiko
- Division of Novel Foods and Immunochemistry, National Institute of Health Sciences
Search this article
Abstract
To produce crops that are more tolerant to stresses such as heat, cold, and salt, transgenic plants have been produced those express stress-associated proteins. In this study, we used immunoproteomic and two-dimensional difference gel electrophoresis (2D-DIGE) methods to investigate the allergenicity of transgenic potatoes expressing Arabidopsis DREB1A (dehydration responsive element-binding protein 1A), driven by the rd29A promoter or the 35S promoter. Immunoproteomic analysis using sera from potato-allergic patients revealed several immunoglobulin E (IgE)-binding protein spots. The patterns of protein binding were almost the same between transgenic and non-transgenic potatoes. The IgE-binding proteins in potato were identified as patatin precursors, a segment of serine protease inhibitor 2, and proteinase inhibitor II by matrix assisted laser desorption/ionization-time of flight (MALDI-TOF) MS/MS. 2D-DIGE analysis revealed several differences in protein expression between non-transgenic potato and transgenic potato; those showing increased expression in transgenic potatoes were identified as precursors of patatin, a major potato allergen, and those showing decreased expression in transgenic potatoes were identified as lipoxygenase and glycogen (starch) synthase. These results suggested that transgenic potatoes may express slightly higher levels of allergens, but their IgE-binding patterns were almost the same as those of control potatoes. Further research on changes in protein expressions in response to environmental factors is required to confirm whether the differences observed in this study are due to gene transfection, rather than environmental factors.
Journal
-
- Biological and Pharmaceutical Bulletin
-
Biological and Pharmaceutical Bulletin 33 (8), 1418-1425, 2010
The Pharmaceutical Society of Japan
- Tweet
Keywords
Details
-
- CRID
- 1390282679603383808
-
- NII Article ID
- 130000300370
-
- NII Book ID
- AA10885497
-
- ISSN
- 13475215
- 09186158
-
- NDL BIB ID
- 10764714
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
-
- Abstract License Flag
- Disallowed