Evidence map›Paper›PMID 21457702›Full record

ArticleArchives of biochemistry and biophysics2011

Nitric oxide reduces sickle hemoglobin polymerization: potential role of nitric oxide-induced charge alteration in depolymerization.

Tohru Ikuta, Hemant S Thatte, Jay X Tang, Ishita Mukerji, Kelly Knee, Kenneth R Bridges, Sabina Wang, Pedro Montero-Huerta, Ratan Mani Joshi, C Alvin Head

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.6field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. The Evolving Pharmacotherapeutic Landscape for the Treatment of Sickle Cell Disease.Mediterranean journal of hematology and infectious diseases · 2020
    Review
  6. cGMP modulation therapeutics for sickle cell disease.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
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

10 authors at 6 institutions in 1 country.

Tohru IkutaDepartment of Anesthesiology and Perioperative Medicine, Georgia Health Sciences University, Augusta, 30912, United States.
Hemant S Thatte
Jay X Tang
Ishita Mukerji
Kelly Knee
Kenneth R Bridges
Sabina Wang
Pedro Montero-Huerta
Ratan Mani Joshi
C Alvin Head
Augusta University Health · USAmgen (United States) · USBrown University · USMassachusetts Institute of Technology · USVA Boston Healthcare System · USWesleyan University · US

Funding

Training/Education CoreP20MD003383 · NIMHD · AUGUSTA UNIVERSITY · PI IKUTA, TOHRU · 2009 to 2013
$6.8M
NIMHD NIH HHS P20 MD003383
6 · The paper itself

Abstract

We previously demonstrated that inhaling nitric oxide (NO) increases the oxygen affinity of sickle red blood cells (RBCs) in patients with sickle cell disease (SCD). Our recent studies found that NO lowered the P(50) values of sickle hemoglobin (HbS) hemolysates but did not increase methemoglobin (metHb) levels, supporting the role of NO, but not metHb, in the oxygen affinity of HbS. Here we examine the mechanism by which NO increases HbS oxygen affinity. Because anti-sickling agents increase sickle RBC oxygen affinity, we first determined whether NO exhibits anti-sickling properties. The viscosity of HbS hemolysates, measured by falling ball assays, increased upon deoxygenation; NO treatment reduced the increment. Multiphoton microscopic analyses showed smaller HbS polymers in deoxygenated sickle RBCs and HbS hemolysates exposed to NO. These results suggest that NO inhibits HbS polymer formation and has anti-sickling properties. Furthermore, we found that HbS treated with NO exhibits an isoelectric point similar to that of HbA, suggesting that NO alters the electric charge of HbS. NO-HbS adducts had the same elution time as HbA upon high performance liquid chromatography analysis. This study demonstrates that NO may disrupt HbS polymers by abolishing the excess positive charge of HbS, resulting in increased oxygen affinity.

Indexed as

Anemia, Sickle CellAntisickling AgentsErythrocytesHemoglobin, SickleHumansMethemoglobinNitric OxideOxygenPolymerizationViscosityAntisickling AgentsHemoglobin, SickleMethemoglobinNitric OxideOxygen

Identifiers

PMID21457702
PMCPMC3889650
OpenAlexW2001096364

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.