Cargando…
A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major
Apoptosis is a cell death process generally described as involving a cascade of caspase activation, death receptors and/or pro- and antiapoptotic molecules from the BcL-2 family. But about 20 years ago, a caspase-independent apoptotic pathway has been described. Regarding this pathway, we can learn...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6534544/ https://www.ncbi.nlm.nih.gov/pubmed/31149349 http://dx.doi.org/10.1038/s41420-019-0178-2 |
_version_ | 1783421428616396800 |
---|---|
author | Basmaciyan, Louise Jacquet, Pauline Azas, Nadine Casanova, Magali |
author_facet | Basmaciyan, Louise Jacquet, Pauline Azas, Nadine Casanova, Magali |
author_sort | Basmaciyan, Louise |
collection | PubMed |
description | Apoptosis is a cell death process generally described as involving a cascade of caspase activation, death receptors and/or pro- and antiapoptotic molecules from the BcL-2 family. But about 20 years ago, a caspase-independent apoptotic pathway has been described. Regarding this pathway, we can learn a lot from Leishmania parasites. Indeed, these parasitic protozoa enter, in response to different stimuli, in a form of cell death phenotypically similar to mammalian apoptosis but without involving caspases or death receptors. So far, only two proteins have been clearly identified as being involved in Leishmania-regulated cell death: the metacaspase and the endonuclease G. We report here the identification of a new protein modeled as a potential hydrolase, highly conserved among Leishmania species and absent in the very close parasite Trypanosoma brucei. This protein is involved in L. major-regulated cell death induced by curcumin, miltefosine and pentamidine, after gene overexpression and/or protein translocation to the nucleus. The identification of proteins involved in Leishmania-regulated cell death will provide a better understanding of nonconventional apoptotic pathways in higher eukaryotes. It will also allow the development of new therapeutic tools via the identification of new specific targets. |
format | Online Article Text |
id | pubmed-6534544 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65345442019-05-30 A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major Basmaciyan, Louise Jacquet, Pauline Azas, Nadine Casanova, Magali Cell Death Discov Review Article Apoptosis is a cell death process generally described as involving a cascade of caspase activation, death receptors and/or pro- and antiapoptotic molecules from the BcL-2 family. But about 20 years ago, a caspase-independent apoptotic pathway has been described. Regarding this pathway, we can learn a lot from Leishmania parasites. Indeed, these parasitic protozoa enter, in response to different stimuli, in a form of cell death phenotypically similar to mammalian apoptosis but without involving caspases or death receptors. So far, only two proteins have been clearly identified as being involved in Leishmania-regulated cell death: the metacaspase and the endonuclease G. We report here the identification of a new protein modeled as a potential hydrolase, highly conserved among Leishmania species and absent in the very close parasite Trypanosoma brucei. This protein is involved in L. major-regulated cell death induced by curcumin, miltefosine and pentamidine, after gene overexpression and/or protein translocation to the nucleus. The identification of proteins involved in Leishmania-regulated cell death will provide a better understanding of nonconventional apoptotic pathways in higher eukaryotes. It will also allow the development of new therapeutic tools via the identification of new specific targets. Nature Publishing Group UK 2019-05-24 /pmc/articles/PMC6534544/ /pubmed/31149349 http://dx.doi.org/10.1038/s41420-019-0178-2 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Review Article Basmaciyan, Louise Jacquet, Pauline Azas, Nadine Casanova, Magali A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title | A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title_full | A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title_fullStr | A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title_full_unstemmed | A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title_short | A novel hydrolase with a pro-death activity from the protozoan parasite Leishmania major |
title_sort | novel hydrolase with a pro-death activity from the protozoan parasite leishmania major |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6534544/ https://www.ncbi.nlm.nih.gov/pubmed/31149349 http://dx.doi.org/10.1038/s41420-019-0178-2 |
work_keys_str_mv | AT basmaciyanlouise anovelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT jacquetpauline anovelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT azasnadine anovelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT casanovamagali anovelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT basmaciyanlouise novelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT jacquetpauline novelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT azasnadine novelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor AT casanovamagali novelhydrolasewithaprodeathactivityfromtheprotozoanparasiteleishmaniamajor |