Evidence map›Paper›PMID 22183030›Full record

ReviewBiochimica et biophysica acta2012

S-nitrosylation of surfactant protein D as a modulator of pulmonary inflammation.

Elena N Atochina-Vasserman

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023
    Article
  4. Article
  5. Genetic Association WithFrontiers in immunology · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Protective Role of Surfactant Protein-D Against Lung Injury and Oxidative Stress Induced by Nitrogen Mustard.Toxicological sciences : an official journal of the Society of Toxicology · 2018
    Article
  10. Article
  11. Article
  12. Review
  13. Editor's Highlight: Role of Spleen-Derived Macrophages in Ozone-Induced Lung Inflammation and Injury.Toxicological sciences : an official journal of the Society of Toxicology · 2017
    Article
  14. Article
  15. Role of nitric oxide in immune responses against viruses: beyond microbicidal activity.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2015
    Review
  16. Surfactant dysfunction and lung inflammation in the female mouse model of lymphangioleiomyomatosis.American journal of respiratory cell and molecular biology · 2015
    Article
  17. Radiation-induced lung injury and inflammation in mice: role of inducible nitric oxide synthase and surfactant protein D.Toxicological sciences : an official journal of the Society of Toxicology · 2015
    Article
  18. Eosinophil-associated lung diseases. A cry for surfactant proteins A and D help?American journal of respiratory cell and molecular biology · 2014
    Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Elena N Atochina-VassermanPulmonary, Allergy and Critical Care Division, Department of Medicine University of Pennsylvania, Vernon and Shirley Hill Pavilion, #H410C, 380 S. University Ave., Philadelphia, PA 19104-4539, USA. atochina@mail.med.upenn.edu
University of Pennsylvania · US

Funding

Translational Research Support CoreP30ES005022 · NIEHS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ROBERT John LAUMBACH · 1988 to 2026
$47.4M
Translational Research Support CoreP30ES013508 · NIEHS · UNIVERSITY OF PENNSYLVANIA · PI Rebecca A Simmons · 2006 to 2026
$35.3M
Models of P. carinii infections SP-A and SP-D null miceR01HL064520 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI BEERS, MICHAEL FRANCIS · 1999 to 2009
$3.3M
NO-Modified Biomolecules and Pulmonary SignalingR01HL086621 · NHLBI · RUTGERS, THE STATE UNIV OF N.J. · PI GOW, ANDREW J · 2008 to 2016
$2.8M
NHLBI NIH HHS HL-086621NHLBI NIH HHS HL-64520NHLBI NIH HHS R01 HL064520NHLBI NIH HHS R01 HL086621NIEHS NIH HHS ES-005022NIEHS NIH HHS ES P30-013508NIEHS NIH HHS P30 ES005022
6 · The paper itself

Abstract

backgroundSurfactant protein D (SP-D) is a member of the family of proteins termed collagen-like lectins or "collectins" that play a role in non-antibody-mediated innate immune responses [1]. The primary function of SP-D is the modulation of host defense and inflammation [2]. SCOPE OF REVIEW: This review will discuss recent findings on the physiological importance of SP-D S-nitrosylation in biological systems and potential mechanisms that govern SP-D mediated signaling. MAJOR

conclusionsSP-D appears to have both pro- and anti-inflammatory signaling functions. SP-D multimerization is a critical feature of its function and plays an important role in efficient innate host defense. Under baseline conditions, SP-D forms a multimer in which the N-termini are hidden in the center and the C-termini are on the surface. This multimeric form of SP-D is limited in its ability to activate inflammation. However, NO can modify key cysteine residues in the hydrophobic tail domain of SP-D resulting in a dissociation of SP-D multimers into trimers, exposing the S-nitrosylated N-termini. The exposed S-nitrosylated tail domain binds to the calreticulin/CD91 receptor complex and initiates a pro-inflammatory response through phosphorylation of p38 and NF-κB activation [3,4]. In addition, the disassembled SP-D loses its ability to block TLR4, which also results in activation of NF-κB. GENERAL SIGNIFICANCE: Recent studies have highlighted the capability of NO to modify SP-D through S-nitrosylation, causing the activation of a pro-inflammatory role for SP-D [3]. This represents a novel mechanism both for the regulation of SP-D function and NO's role in innate immunity, but also demonstrates that the S-nitrosylation can control protein function by regulating quaternary structure. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.

Indexed as

AnimalsCalreticulinGene Expression RegulationHumansImmunity, InnateInflammationLow Density Lipoprotein Receptor-Related Protein-1MacrophagesMiceNF-kappa BNitric OxideNitrosationp38 Mitogen-Activated Protein KinasesPhosphorylationPneumoniaProtein Structure, QuaternaryCalreticulinLow Density Lipoprotein Receptor-Related Protein-1NF-kappa BNitric Oxidep38 Mitogen-Activated Protein KinasesPulmonary Surfactant-Associated Protein DTLR4 protein, humanToll-Like Receptor 4

Identifiers

PMID22183030
PMCPMC4013789
OpenAlexW2000019799

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.