Cargando…
The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity
Although the protein translation inhibition activity of ribosome inactivating proteins (RIPs) is well documented, little is known about the contribution of the lectin chain to the biological activity of these proteins. In this study, we compared the in vitro and intracellular activity of several S....
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493096/ https://www.ncbi.nlm.nih.gov/pubmed/26148207 http://dx.doi.org/10.1371/journal.pone.0132389 |
_version_ | 1782379863601053696 |
---|---|
author | Shang, Chenjing Chen, Qiushi Dell, Anne Haslam, Stuart M. De Vos, Winnok H. Van Damme, Els J. M. |
author_facet | Shang, Chenjing Chen, Qiushi Dell, Anne Haslam, Stuart M. De Vos, Winnok H. Van Damme, Els J. M. |
author_sort | Shang, Chenjing |
collection | PubMed |
description | Although the protein translation inhibition activity of ribosome inactivating proteins (RIPs) is well documented, little is known about the contribution of the lectin chain to the biological activity of these proteins. In this study, we compared the in vitro and intracellular activity of several S. nigra (elderberry) RIPs and non-RIP lectins. Our data demonstrate that RIPs from elderberry are much more toxic to HeLa cells than to primary fibroblasts. Differences in the cytotoxicity between the elderberry proteins correlated with differences in glycan specificity of their lectin domain, cellular uptake efficiency and intracellular destination. Despite the fact that the bulk of the RIPs accumulated in the lysosomes and partly in the Golgi apparatus, we could demonstrate effective inhibition of protein synthesis in cellula. As we also observed cytotoxicity for non-RIP lectins, it is clear that the lectin chain triggers additional pathways heralding cell death. Our data suggest that one of these pathways involves the induction of autophagy. |
format | Online Article Text |
id | pubmed-4493096 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-44930962015-07-15 The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity Shang, Chenjing Chen, Qiushi Dell, Anne Haslam, Stuart M. De Vos, Winnok H. Van Damme, Els J. M. PLoS One Research Article Although the protein translation inhibition activity of ribosome inactivating proteins (RIPs) is well documented, little is known about the contribution of the lectin chain to the biological activity of these proteins. In this study, we compared the in vitro and intracellular activity of several S. nigra (elderberry) RIPs and non-RIP lectins. Our data demonstrate that RIPs from elderberry are much more toxic to HeLa cells than to primary fibroblasts. Differences in the cytotoxicity between the elderberry proteins correlated with differences in glycan specificity of their lectin domain, cellular uptake efficiency and intracellular destination. Despite the fact that the bulk of the RIPs accumulated in the lysosomes and partly in the Golgi apparatus, we could demonstrate effective inhibition of protein synthesis in cellula. As we also observed cytotoxicity for non-RIP lectins, it is clear that the lectin chain triggers additional pathways heralding cell death. Our data suggest that one of these pathways involves the induction of autophagy. Public Library of Science 2015-07-06 /pmc/articles/PMC4493096/ /pubmed/26148207 http://dx.doi.org/10.1371/journal.pone.0132389 Text en © 2015 Shang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Shang, Chenjing Chen, Qiushi Dell, Anne Haslam, Stuart M. De Vos, Winnok H. Van Damme, Els J. M. The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title | The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title_full | The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title_fullStr | The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title_full_unstemmed | The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title_short | The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity |
title_sort | cytotoxicity of elderberry ribosome-inactivating proteins is not solely determined by their protein translation inhibition activity |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493096/ https://www.ncbi.nlm.nih.gov/pubmed/26148207 http://dx.doi.org/10.1371/journal.pone.0132389 |
work_keys_str_mv | AT shangchenjing thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT chenqiushi thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT dellanne thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT haslamstuartm thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT devoswinnokh thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT vandammeelsjm thecytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT shangchenjing cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT chenqiushi cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT dellanne cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT haslamstuartm cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT devoswinnokh cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity AT vandammeelsjm cytotoxicityofelderberryribosomeinactivatingproteinsisnotsolelydeterminedbytheirproteintranslationinhibitionactivity |