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Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety
To investigate unintended effects in genetically modified crops (GMCs), a comparative proteomic analysis between the leaves of the phytase-transgenic maize and the non-transgenic plants was performed using two-dimensional gel electrophoresis and mass spectrometry. A total of 57 differentially expres...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4987384/ https://www.ncbi.nlm.nih.gov/pubmed/27582747 http://dx.doi.org/10.3389/fpls.2016.01211 |
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author | Tan, Yanhua Yi, Xiaoping Wang, Limin Peng, Cunzhi Sun, Yong Wang, Dan Zhang, Jiaming Guo, Anping Wang, Xuchu |
author_facet | Tan, Yanhua Yi, Xiaoping Wang, Limin Peng, Cunzhi Sun, Yong Wang, Dan Zhang, Jiaming Guo, Anping Wang, Xuchu |
author_sort | Tan, Yanhua |
collection | PubMed |
description | To investigate unintended effects in genetically modified crops (GMCs), a comparative proteomic analysis between the leaves of the phytase-transgenic maize and the non-transgenic plants was performed using two-dimensional gel electrophoresis and mass spectrometry. A total of 57 differentially expressed proteins (DEPs) were successfully identified, which represents 44 unique proteins. Functional classification of the identified proteins showed that these DEPs were predominantly involved in carbohydrate transport and metabolism category, followed by post-translational modification. KEGG pathway analysis revealed that most of the DEPs participated in carbon fixation in photosynthesis. Among them, 15 proteins were found to show protein-protein interactions with each other, and these proteins were mainly participated in glycolysis and carbon fixation. Comparison of the changes in the protein and tanscript levels of the identified proteins showed that most proteins had a similar pattern of changes between proteins and transcripts. Our results suggested that although some significant differences were observed, the proteomic patterns were not substantially different between the leaves of the phytase-transgenic maize and the non-transgenic isogenic type. Moreover, none of the DEPs was identified as a new toxic protein or an allergenic protein. The differences between the leaf proteome might be attributed to both genetic modification and hybrid influence. |
format | Online Article Text |
id | pubmed-4987384 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49873842016-08-31 Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety Tan, Yanhua Yi, Xiaoping Wang, Limin Peng, Cunzhi Sun, Yong Wang, Dan Zhang, Jiaming Guo, Anping Wang, Xuchu Front Plant Sci Plant Science To investigate unintended effects in genetically modified crops (GMCs), a comparative proteomic analysis between the leaves of the phytase-transgenic maize and the non-transgenic plants was performed using two-dimensional gel electrophoresis and mass spectrometry. A total of 57 differentially expressed proteins (DEPs) were successfully identified, which represents 44 unique proteins. Functional classification of the identified proteins showed that these DEPs were predominantly involved in carbohydrate transport and metabolism category, followed by post-translational modification. KEGG pathway analysis revealed that most of the DEPs participated in carbon fixation in photosynthesis. Among them, 15 proteins were found to show protein-protein interactions with each other, and these proteins were mainly participated in glycolysis and carbon fixation. Comparison of the changes in the protein and tanscript levels of the identified proteins showed that most proteins had a similar pattern of changes between proteins and transcripts. Our results suggested that although some significant differences were observed, the proteomic patterns were not substantially different between the leaves of the phytase-transgenic maize and the non-transgenic isogenic type. Moreover, none of the DEPs was identified as a new toxic protein or an allergenic protein. The differences between the leaf proteome might be attributed to both genetic modification and hybrid influence. Frontiers Media S.A. 2016-08-17 /pmc/articles/PMC4987384/ /pubmed/27582747 http://dx.doi.org/10.3389/fpls.2016.01211 Text en Copyright © 2016 Tan, Yi, Wang, Peng, Sun, Wang, Zhang, Guo and Wang. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Tan, Yanhua Yi, Xiaoping Wang, Limin Peng, Cunzhi Sun, Yong Wang, Dan Zhang, Jiaming Guo, Anping Wang, Xuchu Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title | Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title_full | Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title_fullStr | Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title_full_unstemmed | Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title_short | Comparative Proteomics of Leaves from Phytase-Transgenic Maize and Its Non-transgenic Isogenic Variety |
title_sort | comparative proteomics of leaves from phytase-transgenic maize and its non-transgenic isogenic variety |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4987384/ https://www.ncbi.nlm.nih.gov/pubmed/27582747 http://dx.doi.org/10.3389/fpls.2016.01211 |
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