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A Dual Role of Heme Oxygenase-1 in Tuberculosis

Iron metabolism is vital for the survival of both humans and microorganisms. Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological cond...

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Autores principales: Yang, Sen, Ouyang, Jing, Lu, Yanqiu, Harypursat, Vijay, Chen, Yaokai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913507/
https://www.ncbi.nlm.nih.gov/pubmed/35281042
http://dx.doi.org/10.3389/fimmu.2022.842858
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author Yang, Sen
Ouyang, Jing
Lu, Yanqiu
Harypursat, Vijay
Chen, Yaokai
author_facet Yang, Sen
Ouyang, Jing
Lu, Yanqiu
Harypursat, Vijay
Chen, Yaokai
author_sort Yang, Sen
collection PubMed
description Iron metabolism is vital for the survival of both humans and microorganisms. Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation. Ferrous iron (Fe(2+)) is an important raw material for the synthesis of hemoglobin in red blood cells, and patients with iron deficiency are often associated with decreased cellular immunity. CO and BR can inhibit oxidative stress and inflammation. Thus, HO-1 is regarded as a cytoprotective molecule during the infection process. However, recent study has unveiled new information regarding HO-1. Being a highly infectious pathogenic bacterium, Mycobacterium tuberculosis (MTB) infection causes acute oxidative stress, and increases the expression of HO-1, which may in turn facilitate MTB survival and growth due to increased iron availability. Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe(2+)) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis. Therefore, it is important to understand and illustrate the dual role of HO-1 in tuberculosis. Herein, we critically review the interplay among HO-1, tuberculosis, and the host, thus paving the way for development of potential strategies for modulating HO-1 and iron metabolism.
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spelling pubmed-89135072022-03-12 A Dual Role of Heme Oxygenase-1 in Tuberculosis Yang, Sen Ouyang, Jing Lu, Yanqiu Harypursat, Vijay Chen, Yaokai Front Immunol Immunology Iron metabolism is vital for the survival of both humans and microorganisms. Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation. Ferrous iron (Fe(2+)) is an important raw material for the synthesis of hemoglobin in red blood cells, and patients with iron deficiency are often associated with decreased cellular immunity. CO and BR can inhibit oxidative stress and inflammation. Thus, HO-1 is regarded as a cytoprotective molecule during the infection process. However, recent study has unveiled new information regarding HO-1. Being a highly infectious pathogenic bacterium, Mycobacterium tuberculosis (MTB) infection causes acute oxidative stress, and increases the expression of HO-1, which may in turn facilitate MTB survival and growth due to increased iron availability. Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe(2+)) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis. Therefore, it is important to understand and illustrate the dual role of HO-1 in tuberculosis. Herein, we critically review the interplay among HO-1, tuberculosis, and the host, thus paving the way for development of potential strategies for modulating HO-1 and iron metabolism. Frontiers Media S.A. 2022-02-25 /pmc/articles/PMC8913507/ /pubmed/35281042 http://dx.doi.org/10.3389/fimmu.2022.842858 Text en Copyright © 2022 Yang, Ouyang, Lu, Harypursat and Chen https://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) and the copyright owner(s) 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 Immunology
Yang, Sen
Ouyang, Jing
Lu, Yanqiu
Harypursat, Vijay
Chen, Yaokai
A Dual Role of Heme Oxygenase-1 in Tuberculosis
title A Dual Role of Heme Oxygenase-1 in Tuberculosis
title_full A Dual Role of Heme Oxygenase-1 in Tuberculosis
title_fullStr A Dual Role of Heme Oxygenase-1 in Tuberculosis
title_full_unstemmed A Dual Role of Heme Oxygenase-1 in Tuberculosis
title_short A Dual Role of Heme Oxygenase-1 in Tuberculosis
title_sort dual role of heme oxygenase-1 in tuberculosis
topic Immunology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913507/
https://www.ncbi.nlm.nih.gov/pubmed/35281042
http://dx.doi.org/10.3389/fimmu.2022.842858
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