Evidence map›Paper›PMID 27604527›Full record

ReviewPhysiological reviews2016

Heme Oxygenases in Cardiovascular Health and Disease.

Anita Ayer, Abolfazl Zarjou, Anupam Agarwal, Roland Stocker

Open access · bronzeAbstract readReview
In one paragraph

Review in Physiological reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
8.7field-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

134 citing papers in PubMed, 242 citations in OpenAlex.

  1. Article
  2. Intracellular Crosstalk of the Gasotransmitter Trio (NO, CO, HInternational journal of molecular sciences · 2026
    Review
  3. CD73Nature communications · 2026
    Article
  4. Article
  5. Review
  6. Article
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  18. Article
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74 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 2 institutions in 2 countries.

Anita AyerVascular Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia; and Nephrology Research and Training Center, University of Alabama at Birmingham, Birmingham Veterans Administration Medical Center, Birmingham, Alabama.
Abolfazl ZarjouVascular Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia; and Nephrology Research and Training Center, University of Alabama at Birmingham, Birmingham Veterans Administration Medical Center, Birmingham, Alabama.
Anupam AgarwalVascular Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia; and Nephrology Research and Training Center, University of Alabama at Birmingham, Birmingham Veterans Administration Medical Center, Birmingham, Alabama.
Roland StockerVascular Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia; and Nephrology Research and Training Center, University of Alabama at Birmingham, Birmingham Veterans Administration Medical Center, Birmingham, Alabama.
University of Alabama at Birmingham · USBirmingham VA Medical Center · US

Funding

UAB-UCSD O'Brien Core Center for Acute Kidney Injury ResearchP30DK079337 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI AGARWAL, ANUPAM · 2008 to 2022
$18.3M
Human Heme Oxygenase-1 Gene Regulation in Renal InjuryR01DK059600 · NIDDK · UNIVERSITY OF FLORIDA · PI AGARWAL, ANUPAM, GEORGE, JAMES F · 2002 to 2019
$4.5M
NIDDK NIH HHS P30 DK079337NIDDK NIH HHS R01 DK059600
6 · The paper itself

Abstract

Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. While initially considered to be waste products, CO and biliverdin/bilirubin have been shown over the last 20 years to modulate key cellular processes, such as inflammation, cell proliferation, and apoptosis, as well as antioxidant defense. This shift in paradigm has led to the importance of heme oxygenases and their products in cell physiology now being well accepted. The identification of the two human cases thus far of heme oxygenase deficiency and the generation of mice deficient in Hmox1 or Hmox2 have reiterated a role for these enzymes in both normal cell function and disease pathogenesis, especially in the context of cardiovascular disease. This review covers the current knowledge on the function of both Hmox1 and Hmox2 at both a cellular and tissue level in the cardiovascular system. Initially, the roles of heme oxygenases in vascular health and the regulation of processes central to vascular diseases are outlined, followed by an evaluation of the role(s) of Hmox1 and Hmox2 in various diseases such as atherosclerosis, intimal hyperplasia, myocardial infarction, and angiogenesis. Finally, the therapeutic potential of heme oxygenases and their products are examined in a cardiovascular disease context, with a focus on how the knowledge we have gained on these enzymes may be capitalized in future clinical studies.

Indexed as

AnimalsBiliverdineCarbon MonoxideCardiovascular DiseasesCardiovascular SystemHemeHeme Oxygenase (Decyclizing)HumansIronBiliverdineCarbon MonoxideHemeHeme Oxygenase (Decyclizing)Iron

Identifiers

PMID27604527
PMCPMC5504454
OpenAlexW2509748070

What OpenQuestion holds

Textmetadata
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.