Evidence map›Paper›PMID 19362144›Full record

ReviewFree radical biology & medicine2009

Heme oxygenase-1, a critical arbitrator of cell death pathways in lung injury and disease.

Danielle Morse, Ling Lin, Augustine M K Choi, Stefan W Ryter

Abstract readReview
In one paragraph

Review in Free radical biology & medicine, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

82 citing papers in PubMed, 181 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular Hydrogen in the Treatment of Respiratory Diseases.International journal of molecular sciences · 2025
    Review
  4. Article
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  7. Lipid Peroxidation-Related Redox Signaling in Osteosarcoma.International journal of molecular sciences · 2024
    Review
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22 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 1 country.

Danielle MorseDivision of Pulmonary and Critical Care Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Ling Lin
Augustine M K Choi
Stefan W Ryter
Harvard University · USBrigham and Women's Hospital · USUniversity of Pittsburgh Medical Center · US

Funding

NITRIC OXIDE AND METALLOTIONEIMP01HL070807 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KAGAN, VALERIAN E · 2003 to 2007
$8.1M
The Role of HEME Oxygenase in Hyperoxic Lung InjuryR01HL055330 · NHLBI · YALE UNIVERSITY · PI CHOI, AUGUSTINE M, CHOI, MARY E · 1998 to 2021
$6.6M
HEME OXYGENASE 1--LUNG VASCULAR CELL HYPOXIC RESPONSER01HL060234 · NHLBI · YALE UNIVERSITY · PI CHOI, AUGUSTINE M, CHOI, MARY E · 1999 to 2017
$5.8M
Heme oxygenase-1: Regulation and Function in CaveolaeR01HL079904 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI CHOI, MARY E · 2005 to 2014
$2.9M
NHLBI NIH HHS P01 HL070807NHLBI NIH HHS P01-HL70807NHLBI NIH HHS R01 HL055330NHLBI NIH HHS R01 HL060234NHLBI NIH HHS R01 HL079904NHLBI NIH HHS R01-HL079904NHLBI NIH HHS R01-HL55330NHLBI NIH HHS R01-HL60234
6 · The paper itself

Abstract

Increases in cell death by programmed (i.e., apoptosis, autophagy) or nonprogrammed mechanisms (i.e., necrosis) occur during tissue injury and may contribute to the etiology of several pulmonary or vascular disease states. The low-molecular-weight stress protein heme oxygenase-1 (HO-1) confers cytoprotection against cell death in various models of lung and vascular injury by inhibiting apoptosis, inflammation, and cell proliferation. HO-1 serves a vital metabolic function as the rate-limiting step in the heme degradation pathway and in the maintenance of iron homeostasis. The transcriptional induction of HO-1 occurs in response to multiple forms of chemical and physical cellular stress. The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO). Recent studies have demonstrated that HO-1 or CO inhibits stress-induced extrinsic and intrinsic apoptotic pathways in vitro. A variety of signaling molecules have been implicated in the cytoprotection conferred by HO-1/CO, including autophagic proteins, p38 mitogen-activated protein kinase, signal transducer and activator of transcription proteins, nuclear factor-kappaB, phosphatidylinositol 3-kinase/Akt, and others. Enhanced HO-1 expression or the pharmacological application of HO end-products affords protection in preclinical models of tissue injury, including experimental and transplant-associated ischemia/reperfusion injury, promising potential future therapeutic applications.

Indexed as

AnimalsApoptosisBiliverdineCarbon MonoxideCell ProliferationHemeHeme Oxygenase-1HumansIronLungOrgan TransplantationOxidative StressReperfusion InjurySignal TransductionSTAT Transcription FactorsBiliverdineCarbon MonoxideHemeHeme Oxygenase-1IronSTAT Transcription Factors

Identifiers

PMID19362144
PMCPMC3078523
OpenAlexW2038074738

What OpenQuestion holds

Textmetadata
LicenceTDM
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.