PMID- 20686241
OWN - NLM
STAT- MEDLINE
DCOM- 20101214
LR  - 20190720
IS  - 1347-5215 (Electronic)
IS  - 0918-6158 (Linking)
VI  - 33
IP  - 8
DP  - 2010
TI  - Immunoproteomic and two-dimensional difference gel electrophoresis analysis of 
      Arabidopsis dehydration response element-binding protein 1A (DREB1A)-transgenic 
      potato.
PG  - 1418-25
AB  - 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.
FAU - Nakamura, Rika
AU  - Nakamura R
AD  - Division of Novel Foods and Immunochemistry, National Institute of Health 
      Sciences, Tokyo, Japan.
FAU - Satoh, Rie
AU  - Satoh R
FAU - Nakamura, Ryosuke
AU  - Nakamura R
FAU - Shimazaki, Takayoshi
AU  - Shimazaki T
FAU - Kasuga, Mie
AU  - Kasuga M
FAU - Yamaguchi-Shinozaki, Kazuko
AU  - Yamaguchi-Shinozaki K
FAU - Kikuchi, Akira
AU  - Kikuchi A
FAU - Watanabe, Kazuo N
AU  - Watanabe KN
FAU - Teshima, Reiko
AU  - Teshima R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Japan
TA  - Biol Pharm Bull
JT  - Biological & pharmaceutical bulletin
JID - 9311984
RN  - 0 (Allergens)
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (DREB1A protein, Arabidopsis)
RN  - 0 (Plant Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (patatin protein, Solanum tuberosum)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 3.1.1.- (Carboxylic Ester Hydrolases)
SB  - IM
MH  - Allergens/genetics/immunology
MH  - Arabidopsis Proteins/*genetics
MH  - Carboxylic Ester Hydrolases/genetics/immunology
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Food Hypersensitivity/blood/*immunology
MH  - Humans
MH  - Immunoblotting
MH  - Immunoglobulin E/*blood
MH  - Plant Proteins/genetics/immunology
MH  - *Plants, Genetically Modified/adverse effects/genetics/immunology
MH  - Protein Binding
MH  - *Solanum tuberosum/adverse effects/genetics/immunology
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Transcription Factors/*genetics
MH  - Transfection
MH  - Transgenes
EDAT- 2010/08/06 06:00
MHDA- 2010/12/16 06:00
CRDT- 2010/08/06 06:00
PHST- 2010/08/06 06:00 [entrez]
PHST- 2010/08/06 06:00 [pubmed]
PHST- 2010/12/16 06:00 [medline]
AID - JST.JSTAGE/bpb/33.1418 [pii]
AID - 10.1248/bpb.33.1418 [doi]
PST - ppublish
SO  - Biol Pharm Bull. 2010;33(8):1418-25. doi: 10.1248/bpb.33.1418.