Evidence map›Paper›PMID 23710929›Full record

ArticleThe FEBS journal2013

Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles.

Xiaoping Liu, Jianjing Tong, Joseph R Zweier, Douglas Follmer, Craig Hemann, Raed S Ismail, Jay L Zweier

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Insights into the function of cytoglobin.Biochemical Society transactions · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. The Zebrafish CytochromeBiochemistry · 2019
    Article
  19. Review
  20. 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

7 authors at 1 institution in 1 country.

Xiaoping LiuDepartment of Internal Medicine, Davis Heart and Lung Research Institute, The Ohio State University College of Medicine, Columbus, OH 43210, USA. Xiaoping.liu@osumc.edu
Jianjing Tong
Joseph R Zweier
Douglas Follmer
Craig Hemann
Raed S Ismail
Jay L Zweier
Lung Institute · 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 HL063744NHLBI NIH HHS HL065608NHLBI NIH HHS HL38324NHLBI NIH HHS P01 HL065608NHLBI NIH HHS R01 HL038324NHLBI NIH HHS R01 HL063744
6 · The paper itself

Abstract

The endogenous vasodilator nitric oxide (NO) is metabolized in tissues in an oxygen-dependent manner. In skeletal and cardiac muscle, high concentrations of myoglobin (Mb) function as a potent NO scavenger. However, the Mb concentration is very low in vascular smooth muscle, where low concentrations of cytoglobin (Cygb) may play a major role in metabolizing NO. Questions remain regarding how low concentrations of Cygb and Mb differ in terms of NO metabolism, and the basis for their different cellular roles and functions. In this study, electrode techniques were used to perform comparative measurements of the kinetics of NO consumption by Mb and Cygb. UV/Vis spectroscopic methods and computer simulations were performed to study the reaction of Mb and Cygb with ascorbate (Asc) and the underlying mechanism. It was observed that the initial rate of Cygb(3+) reduction by Asc was 415-fold greater than that of Mb(3+). In the low [O2] range (0-50 μM), the Cygb-mediated NO consumption rate is ~ 500 times more sensitive to changes in O2 concentration than that of Mb. The reduction of Cygb(3+) by Asc follows a reversible kinetic model, but that of Mb(3+) is irreversible. A reaction mechanism for Cygb(3+) reduction by Asc is proposed, and the reaction equilibrium constants are determined. Our results suggest that the rapid reduction of Cygb by cellular reductants enables Cygb to efficiently regulate NO metabolism in the vascular wall in an oxygen-dependent manner, but the slow rate of Mb reduction does not show this oxygen dependence.

Indexed as

AlgorithmsAscorbic AcidComputer SimulationCytoglobinGlobinsHumansKineticsModels, ChemicalMyoglobinNitric OxideOxidantsOxidation-ReductionOxygenAscorbic AcidCYGB protein, humanCytoglobinGlobinsMyoglobinNitric OxideOxidantsOxygencytoglobinmetabolism kineticsmyoglobinnitric oxideoxygen

Identifiers

PMID23710929
PMCPMC4138062
OpenAlexW2026492470

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.