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Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance
Heme oxygenase (HO-1) mediates the enzymatic cleavage of heme, a molecule with proinflammatory and prooxidant properties. HO-1 activity deeply impacts host capacity to tolerate infection through reduction of tissue damage or affecting resistance, the ability of the host to control pathogen loads. In...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7373268/ https://www.ncbi.nlm.nih.gov/pubmed/32692767 http://dx.doi.org/10.1371/journal.ppat.1008599 |
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author | Silva, Rafael C. M. C. Travassos, Leonardo H. Paiva, Claudia N. Bozza, Marcelo T. |
author_facet | Silva, Rafael C. M. C. Travassos, Leonardo H. Paiva, Claudia N. Bozza, Marcelo T. |
author_sort | Silva, Rafael C. M. C. |
collection | PubMed |
description | Heme oxygenase (HO-1) mediates the enzymatic cleavage of heme, a molecule with proinflammatory and prooxidant properties. HO-1 activity deeply impacts host capacity to tolerate infection through reduction of tissue damage or affecting resistance, the ability of the host to control pathogen loads. In this Review, we will discuss the contribution of HO-1 in different and complex protozoan infections, such as malaria, leishmaniasis, Chagas disease, and toxoplasmosis. The complexity of these infections and the pleiotropic effects of HO-1 constitute an interesting area of study and an opportunity for drug development. |
format | Online Article Text |
id | pubmed-7373268 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-73732682020-07-29 Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance Silva, Rafael C. M. C. Travassos, Leonardo H. Paiva, Claudia N. Bozza, Marcelo T. PLoS Pathog Review Heme oxygenase (HO-1) mediates the enzymatic cleavage of heme, a molecule with proinflammatory and prooxidant properties. HO-1 activity deeply impacts host capacity to tolerate infection through reduction of tissue damage or affecting resistance, the ability of the host to control pathogen loads. In this Review, we will discuss the contribution of HO-1 in different and complex protozoan infections, such as malaria, leishmaniasis, Chagas disease, and toxoplasmosis. The complexity of these infections and the pleiotropic effects of HO-1 constitute an interesting area of study and an opportunity for drug development. Public Library of Science 2020-07-21 /pmc/articles/PMC7373268/ /pubmed/32692767 http://dx.doi.org/10.1371/journal.ppat.1008599 Text en © 2020 Silva 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Review Silva, Rafael C. M. C. Travassos, Leonardo H. Paiva, Claudia N. Bozza, Marcelo T. Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title | Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title_full | Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title_fullStr | Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title_full_unstemmed | Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title_short | Heme oxygenase-1 in protozoan infections: A tale of resistance and disease tolerance |
title_sort | heme oxygenase-1 in protozoan infections: a tale of resistance and disease tolerance |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7373268/ https://www.ncbi.nlm.nih.gov/pubmed/32692767 http://dx.doi.org/10.1371/journal.ppat.1008599 |
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