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The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins
Cereal endosperm is a highly differentiated tissue containing specialized organelles for the accumulation of storage proteins, which are ultimately deposited either within protein bodies derived from the endoplasmic reticulum, or in protein storage vacuoles (PSVs). During seed maturation endosperm c...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153030/ https://www.ncbi.nlm.nih.gov/pubmed/25232360 http://dx.doi.org/10.3389/fpls.2014.00439 |
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author | Arcalis, Elsa Ibl, Verena Peters, Jenny Melnik, Stanislav Stoger, Eva |
author_facet | Arcalis, Elsa Ibl, Verena Peters, Jenny Melnik, Stanislav Stoger, Eva |
author_sort | Arcalis, Elsa |
collection | PubMed |
description | Cereal endosperm is a highly differentiated tissue containing specialized organelles for the accumulation of storage proteins, which are ultimately deposited either within protein bodies derived from the endoplasmic reticulum, or in protein storage vacuoles (PSVs). During seed maturation endosperm cells undergo a rapid sequence of developmental changes, including extensive reorganization and rearrangement of the endomembrane system and protein transport via several developmentally regulated trafficking routes. Storage organelles have been characterized in great detail by the histochemical analysis of fixed immature tissue samples. More recently, in vivo imaging and the use of tonoplast markers and fluorescent organelle tracers have provided further insight into the dynamic morphology of PSVs in different cell layers of the developing endosperm. This is relevant for biotechnological applications in the area of molecular farming because seed storage organelles in different cereal crops offer alternative subcellular destinations for the deposition of recombinant proteins that can reduce proteolytic degradation, allow control over glycan structures and increase the efficacy of oral delivery. We discuss how the specialized architecture and developmental changes of the endomembrane system in endosperm cells may influence the subcellular fate and post-translational modification of recombinant glycoproteins in different cereal species. |
format | Online Article Text |
id | pubmed-4153030 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-41530302014-09-17 The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins Arcalis, Elsa Ibl, Verena Peters, Jenny Melnik, Stanislav Stoger, Eva Front Plant Sci Plant Science Cereal endosperm is a highly differentiated tissue containing specialized organelles for the accumulation of storage proteins, which are ultimately deposited either within protein bodies derived from the endoplasmic reticulum, or in protein storage vacuoles (PSVs). During seed maturation endosperm cells undergo a rapid sequence of developmental changes, including extensive reorganization and rearrangement of the endomembrane system and protein transport via several developmentally regulated trafficking routes. Storage organelles have been characterized in great detail by the histochemical analysis of fixed immature tissue samples. More recently, in vivo imaging and the use of tonoplast markers and fluorescent organelle tracers have provided further insight into the dynamic morphology of PSVs in different cell layers of the developing endosperm. This is relevant for biotechnological applications in the area of molecular farming because seed storage organelles in different cereal crops offer alternative subcellular destinations for the deposition of recombinant proteins that can reduce proteolytic degradation, allow control over glycan structures and increase the efficacy of oral delivery. We discuss how the specialized architecture and developmental changes of the endomembrane system in endosperm cells may influence the subcellular fate and post-translational modification of recombinant glycoproteins in different cereal species. Frontiers Media S.A. 2014-09-03 /pmc/articles/PMC4153030/ /pubmed/25232360 http://dx.doi.org/10.3389/fpls.2014.00439 Text en Copyright © 2014 Arcalis, Ibl, Peters, Melnik and Stoger. http://creativecommons.org/licenses/by/3.0/ 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 Arcalis, Elsa Ibl, Verena Peters, Jenny Melnik, Stanislav Stoger, Eva The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title | The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title_full | The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title_fullStr | The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title_full_unstemmed | The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title_short | The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
title_sort | dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153030/ https://www.ncbi.nlm.nih.gov/pubmed/25232360 http://dx.doi.org/10.3389/fpls.2014.00439 |
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