Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?

Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin. HO-1 was originally shown to localize at the smooth endoplasmic reticulum membrane (sE...

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Detalles Bibliográficos
Autores principales: Mascaró, Marilina, Alonso, Eliana Noelia, Alonso, Exequiel G., Lacunza, Ezequiel, Curino, Alejandro Carlos, Facchinetti, María Marta
Formato: Articulo
Lenguaje:Inglés
Publicado: 2021
Materias:
Medicina
heme oxygenase-1
nucleus
cancer
oxidative stress
nuclear protein
nuclear localization
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/123761
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-123761
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Medicina
heme oxygenase-1
nucleus
cancer
oxidative stress
nuclear protein
nuclear localization
spellingShingle Medicina
heme oxygenase-1
nucleus
cancer
oxidative stress
nuclear protein
nuclear localization
Mascaró, Marilina
Alonso, Eliana Noelia
Alonso, Exequiel G.
Lacunza, Ezequiel
Curino, Alejandro Carlos
Facchinetti, María Marta
Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
topic_facet Medicina
heme oxygenase-1
nucleus
cancer
oxidative stress
nuclear protein
nuclear localization
description Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin. HO-1 was originally shown to localize at the smooth endoplasmic reticulum membrane (sER), although increasing evidence demonstrates that the protein translocates to other subcellular compartments including the nucleus. The nuclear translocation occurs after proteolytic cleavage by proteases including signal peptide peptidase and some cysteine proteases. In addition, nuclear translocation has been demonstrated to be involved in several cellular processes leading to cancer progression, including induction of resistance to therapy and enhanced metastatic activity. In this review, we focus on nuclear HO-1 implication in pathophysiological conditions with special emphasis on malignant processes. We provide a brief background on the current understanding of the mechanisms underlying how HO-1 leaves the sER membrane and migrates to the nucleus, the circumstances under which it does so and, maybe the most important and unknown aspect, what the function of HO-1 in the nucleus is.
format Articulo
Articulo
author Mascaró, Marilina
Alonso, Eliana Noelia
Alonso, Exequiel G.
Lacunza, Ezequiel
Curino, Alejandro Carlos
Facchinetti, María Marta
author_facet Mascaró, Marilina
Alonso, Eliana Noelia
Alonso, Exequiel G.
Lacunza, Ezequiel
Curino, Alejandro Carlos
Facchinetti, María Marta
author_sort Mascaró, Marilina
title Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
title_short Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
title_full Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
title_fullStr Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
title_full_unstemmed Nuclear Localization of Heme Oxygenase-1 in Pathophysiological Conditions: Does It Explain the Dual Role in Cancer?
title_sort nuclear localization of heme oxygenase-1 in pathophysiological conditions: does it explain the dual role in cancer?
publishDate 2021
url http://sedici.unlp.edu.ar/handle/10915/123761
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bdutipo_str Repositorios
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