Evidence map›Paper›PMID 39978176›Full record

ReviewJournal of inorganic biochemistry2025

Heme and immunity: The heme oxygenase dichotomy.

Melissa Perry, Iqbal Hamza

Abstract readReview
In one paragraph

Review in Journal of inorganic biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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

2 authors.

Melissa PerryGraduate Program in Biological Sciences, University of Maryland, College Park, MD 20742, USA; Center for Blood Oxygen Transport and Hemostasis, Department of Pediatrics, School of Medicine, University of Maryland, Baltimore, MD 21201, USA.
Iqbal HamzaCenter for Blood Oxygen Transport and Hemostasis, Department of Pediatrics, School of Medicine, University of Maryland, Baltimore, MD 21201, USA; Department of Animal and Avian Sciences, University of Maryland, College Park, MD 20742, USA. Electronic address: ihamza@som.umaryland.edu.

Funding

The Biological Role of Heme in NutritionR01DK074797 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI Iqbal Hamza · 2006 to 2026
$5.4M
The Transport of Nutritional Heme in Animal DevelopmentR01DK085035 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI HAMZA, IQBAL · 2010 to 2019
$3.6M
Heme trafficking and recycling in iron metabolismR01DK125740 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI HAMZA, IQBAL · 2020 to 2023
$1.9M
Lifespan Regulation by Inter-Organellar Heme SignalingR01AG082807 · NIA · GEORGIA INSTITUTE OF TECHNOLOGY · PI Iqbal Hamza, Amit Ram Reddi · 2023 to 2026
$1.5M
NIA NIH HHS R01 AG082807NIDDK NIH HHS R01 DK074797NIDDK NIH HHS R01 DK085035NIDDK NIH HHS R01 DK125740
6 · The paper itself

Abstract

Heme, an iron containing organic ring, is required for a diverse range of biological processes across all forms of life. Although this nutrient is essential, its pro-inflammatory and cytotoxic properties can lead to cellular damage. Heme oxygenase 1 (HO-1) is an endoplasmic reticulum (ER)-anchored enzyme that degrades heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron. The induction of HO-1 by heme presents an interesting dichotomy in the cell: CO and BV possess anti-inflammatory and antioxidant properties while free iron can be detrimental as it can generate hydroxyl radicals through the Fenton reaction. The heme/HO-1 axis is tightly regulated, and can influence cell fate, local tissue environments, and disease outcomes during pathogen infection. In this review we explore the role of heme during macrophage polarization and its ability to act as an immune activator while also examining the contribution of HO-1 and heme during infections with intracellular and extracellular pathogens. We highlight work from the emerging field of nutritional immunity of heme and iron, and how the substrates and byproducts of heme metabolism via HO-1 can be beneficial to the host or the pathogen depending on the context.

Indexed as

HemeHeme Oxygenase-1Heme Oxygenase (Decyclizing)AnimalsCarbon MonoxideHumansIronMacrophagesCarbon MonoxideHemeHeme Oxygenase-1Heme Oxygenase (Decyclizing)IronHemeHeme oxygenaseironMacrophagesNutritional immunity

Identifiers

PMID39978176
PMCPMC12744766

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.