Evidence map›Paper›PMID 22896706›Full record

ArticleThe Journal of biological chemistry2012

Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions.

Haitao Li, Craig Hemann, Tamer M Abdelghany, Mohamed A El-Mahdy, Jay L Zweier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 131 citations in OpenAlex.

  1. Trial
  2. Cytochrome bFree radical biology & medicine · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Insights into the function of cytoglobin.Biochemical Society transactions · 2023
    Review
  10. Review
  11. Review
  12. Review
  13. Nitrite Reductase Activity of Ferrous Nitrobindins: A Comparative Study.International journal of molecular sciences · 2023
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

17 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

5 authors at 1 institution in 1 country.

Haitao LiCenter for Biomedical EPR Spectroscopy and Imaging, the Davis Heart and Lung Research Institute and Division of Cardiovascular Medicine, Department of Internal Medicine, Ohio State University College of Medicine, Columbus, Ohio 43210, USA.
Craig Hemann
Tamer M Abdelghany
Mohamed A El-Mahdy
Jay L Zweier
The Ohio State University · US

Funding

Stat3 in Post-Ischemic Myocardial InflammationP01HL065608 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI BECKER, LEWIS C · 2000 to 2011
$22.0M
OXYGEN RADICALS AND NITRIC OXIDE IN POSTISCHEMIC INJURYR01HL063744 · NHLBI · OHIO STATE UNIVERSITY · PI ZWEIER, JAY LOUIS · 2000 to 2009
$5.2M
MEASURE OF FREE RADICAL GENERATION IN HEARTR01HL038324 · NHLBI · OHIO STATE UNIVERSITY · PI ZWEIER, JAY LOUIS · 1992 to 2010
$3.5M
MEASUREMENT OF FREE RADICAL GENERATION IN THE HEARTR29HL038324 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ZWEIER, JAY LOUIS · 1987 to 1991
–
NHLBI NIH HHS HL38324NHLBI NIH HHS HL63744NHLBI NIH HHS HL65608NHLBI NIH HHS P01 HL065608NHLBI NIH HHS R01 HL038324NHLBI NIH HHS R01 HL063744
6 · The paper itself

Abstract

Cytoglobin (Cygb) is a recently discovered cytoplasmic heme-binding globin. Although multiple hemeproteins have been reported to function as nitrite reductases in mammalian cells, it is unknown whether Cygb can also reduce nitrite to nitric oxide (NO). The mechanism, magnitude, and quantitative importance of Cygb-mediated nitrite reduction in tissues have not been reported. To investigate this pathway and its quantitative importance, EPR spectroscopy, spectrophotometric measurements, and chemiluminescence NO analyzer studies were performed. Under anaerobic conditions, mixing nitrite with ferrous-Cygb triggered NO formation that was trapped and detected using EPR spin trapping. Spectrophotometric studies revealed that nitrite binding to ferrous-Cygb is followed by formation of ferric-Cygb and NO. The kinetics and magnitude of Cygb-mediated NO formation were characterized. It was observed that Cygb-mediated NO generation increased linearly with the increase of nitrite concentration under anaerobic conditions. This Cygb-mediated NO production greatly increased with acidosis and near-anoxia as occur in ischemic conditions. With the addition of nitrite, soluble guanylyl cyclase activation was significantly higher in normal smooth muscle cells compared with Cygb knocked down cells with Cygb accounting for ∼40% of the activation in control cells and ∼60% in cells subjected to hypoxia for 48 h. Overall, these studies show that Cygb-mediated nitrite reduction can play an important role in NO generation and soluble guanylyl cyclase activation under hypoxic conditions, with this process regulated by pH, oxygen tension, nitrite concentration, and the redox state of the cells.

Indexed as

AnaerobiosisCell HypoxiaCells, CulturedCytoglobinElectron Spin Resonance SpectroscopyGlobinsGuanylate CyclaseHumansHydrogen-Ion ConcentrationKineticsLuminescent MeasurementsMyocytes, Smooth MuscleNitric OxideNitritesOxidation-ReductionOxygenCYGB protein, humanCytoglobinGlobinsGuanylate CyclaseNitric OxideNitritesOxygen

Identifiers

PMID22896706
PMCPMC3476328
OpenAlexW2066546505

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.