Evidence map›Paper›PMID 31548687›Full record

ArticleNature microbiology2019

A human antithrombin isoform dampens inflammatory responses and protects from organ damage during bacterial infection.

Praveen Papareddy, Madlen Rossnagel, Femke Doreen Hollwedel, Gülcan Kilic, Srinivas Veerla, Clément Naudin, Emanuel Smeds, Johannes Westman, Irene Martinez-Martinez, Arne Egesten and 10 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Antithrombin and Its Role in Host Defense and Inflammation.International journal of molecular sciences · 2021
    Review
  10. Anticoagulant and signaling functions of antithrombin.Journal of thrombosis and haemostasis : JTH · 2020
    Review
  11. Review
  12. Antithrombin: An anticoagulant, anti-inflammatory and antibacterial serpin.Journal of thrombosis and haemostasis : JTH · 2020
    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

20 authors at 4 institutions in 6 countries.

Praveen PapareddyDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.ORCID http://orcid.org/0000-0002-3872-478X
Madlen Rossnagel *Division of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Femke Doreen Hollwedel *Division of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Gülcan KilicBiotech Research and Innovation Center, University of Copenhagen, Copenhagen, Denmark.
Srinivas VeerlaDivision of Oncology and Pathology, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Clément NaudinDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.ORCID http://orcid.org/0000-0002-6777-9587
Emanuel SmedsDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Johannes WestmanDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.ORCID http://orcid.org/0000-0001-6998-3939
Irene Martinez-MartinezServicio de Hematología y Oncología Médica, Hospital Universitario Morales Meseguer, Centro Regional de Hemodonación, IMIB-Arrixaca, CIBERER, Universidad de Murcia, Murcia, Spain.
Arne EgestenDivision of Respiratory Medicine and Allergology, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Maria Eugenia de la Morena-BarrioServicio de Hematología y Oncología Médica, Hospital Universitario Morales Meseguer, Centro Regional de Hemodonación, IMIB-Arrixaca, CIBERER, Universidad de Murcia, Murcia, Spain.ORCID http://orcid.org/0000-0001-7426-4947
Javier CorralServicio de Hematología y Oncología Médica, Hospital Universitario Morales Meseguer, Centro Regional de Hemodonación, IMIB-Arrixaca, CIBERER, Universidad de Murcia, Murcia, Spain.
Adam LinderDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Andrea ArtoniAngelo Bianchi Bonomi Haemophilia and Thrombosis Centre, Fondazione IRCCS Ca' Granda-Ospedale Maggiore Policlinico, Milan, Italy.
Maria AbbattistaAngelo Bianchi Bonomi Haemophilia and Thrombosis Centre, Fondazione IRCCS Ca' Granda-Ospedale Maggiore Policlinico, Milan, Italy.
Cristina NovembrinoAngelo Bianchi Bonomi Haemophilia and Thrombosis Centre, Fondazione IRCCS Ca' Granda-Ospedale Maggiore Policlinico, Milan, Italy.
Cord Herbert BrakebuschBiotech Research and Innovation Center, University of Copenhagen, Copenhagen, Denmark.
Ida MartinelliAngelo Bianchi Bonomi Haemophilia and Thrombosis Centre, Fondazione IRCCS Ca' Granda-Ospedale Maggiore Policlinico, Milan, Italy.
Gopinath KasettyDivision of Respiratory Medicine and Allergology, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden.
Heiko HerwaldDivision of Infection Medicine, Lund, Department of Clinical Sciences, Lund University, Lund, Sweden. heiko.hewald@med.lu.se.ORCID http://orcid.org/0000-0002-8111-2842
Lund University · SEFondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico · ITCentro Regional de Hemodonación · ESUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe infectious diseases are often characterized by an overwhelming and unbalanced systemic immune response to microbial infections. Human antithrombin (hAT) is a crucial coagulation inhibitor with anti-inflammatory activities. Here we identify three hAT-binding proteins (CD13, CD300f and LRP-1) on human monocytes that are involved in blocking the activity of nuclear factor-κB. We found that the modulating effect is primarily restricted to the less abundant β-isoform (hβAT) of hAT that lacks N-glycosylation at position 135. Individuals with a mutation at this position have increased production of hβAT and analysis of their blood, which was stimulated ex vivo with lipopolysaccharide, showed a decreased inflammatory response. Similar findings were recorded when heterozygotic mice expressing hAT or hβAT were challenged with lipopolysaccharide or infected with Escherichia coli bacteria. Our results finally demonstrate that in a lethal E. coli infection model, survival rates increased when mice were treated with hβAT one hour and five hours after infection. The treatment also resulted in a reduction of the inflammatory response and less severe organ damage.

Indexed as

AnimalsAntithrombinsBacterial InfectionsChemokinesCytokinesDisease Models, AnimalEscherichia coliEscherichia coli InfectionsHumansLipopolysaccharidesMaleMiceMice, TransgenicMonocytesMutationNF-kappa BAntithrombinsChemokinesCytokinesLipopolysaccharidesNF-kappa BProtein Isoforms

Identifiers

PMID31548687
OpenAlexW2973640281

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.