Evidence map›Paper›PMID 33440611›Full record

ReviewAntioxidants (Basel, Switzerland)2021

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

Marilina Mascaró, Eliana N Alonso, Exequiel G Alonso, Ezequiel Lacunza, Alejandro C Curino, María Marta Facchinetti

Open access · goldAbstract readReview
In one paragraph

Review in Antioxidants (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Heme oxygenase-1 in thyroid cancer: a context-dependent regulator.Journal of endocrinological investigation · 2026
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  17. Life (Basel, Switzerland) · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Marilina MascaróLaboratorio de Biología del Cáncer, Instituto de Investigaciones Bioquímicas de Bahía Blanca (INIBIBB), Dpto. de Biología, Bioquímica y Farmacia (UNS), Universidad Nacional del Sur (UNS)-CONICET, Bahía Blanca 8000, Argentina.ORCID 0000-0001-7610-5886
Eliana N AlonsoLaboratorio de Biología del Cáncer, Instituto de Investigaciones Bioquímicas de Bahía Blanca (INIBIBB), Dpto. de Biología, Bioquímica y Farmacia (UNS), Universidad Nacional del Sur (UNS)-CONICET, Bahía Blanca 8000, Argentina.
Exequiel G AlonsoLaboratorio de Biología del Cáncer, Instituto de Investigaciones Bioquímicas de Bahía Blanca (INIBIBB), Dpto. de Biología, Bioquímica y Farmacia (UNS), Universidad Nacional del Sur (UNS)-CONICET, Bahía Blanca 8000, Argentina.
Ezequiel LacunzaCentro de Investigaciones Inmunológicas Básicas y Aplicadas (CINIBA), Facultad de Ciencias Médicas, Universidad Nacional de La Plata, La Plata CP1900, Argentina.
Alejandro C CurinoLaboratorio de Biología del Cáncer, Instituto de Investigaciones Bioquímicas de Bahía Blanca (INIBIBB), Dpto. de Biología, Bioquímica y Farmacia (UNS), Universidad Nacional del Sur (UNS)-CONICET, Bahía Blanca 8000, Argentina.
María Marta FacchinettiLaboratorio de Biología del Cáncer, Instituto de Investigaciones Bioquímicas de Bahía Blanca (INIBIBB), Dpto. de Biología, Bioquímica y Farmacia (UNS), Universidad Nacional del Sur (UNS)-CONICET, Bahía Blanca 8000, Argentina.
Centro Científico Tecnológico - Bahía Blanca · ARUniversidad Nacional de La Plata · AR

Funding

Agencia Nacional de Promoción Científica y Tecnológica PICT 2016-4454Agencia Nacional de Promoción Científica y Tecnológica PICT 2018-01678Consejo Nacional de Investigaciones Científicas y Técnicas PIP 1122015 0100068Instituto Nacional del Cáncer INC 2018-2019Secretaría General de Ciencia y Tecnología , Universidad Nacional del Sur PGI 24/B220Secretaría General de Ciencia y Tecnología , Universidad Nacional del Sur PGI 24/B285
6 · The paper itself

Abstract

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.

Indexed as

cancerheme oxygenase-1nuclear localizationnuclear proteinnucleusoxidative stress

Identifiers

PMID33440611
PMCPMC7826503
OpenAlexW3120553787

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.