Evidence map›Paper›PMID 20308059›Full record

ArticleThe Journal of biological chemistry2010

Midkine and pleiotrophin have bactericidal properties: preserved antibacterial activity in a family of heparin-binding growth factors during evolution.

Sara L Svensson, Mukesh Pasupuleti, Björn Walse, Martin Malmsten, Matthias Mörgelin, Camilla Sjögren, Anders I Olin, Mattias Collin, Artur Schmidtchen, Ruth Palmer and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Designed Multifunctional Peptides for Intracellular Targets.Antibiotics (Basel, Switzerland) · 2022
    Review
  8. Midkine-A novel player in cardiovascular diseases.Frontiers in cardiovascular medicine · 2022
    Review
  9. Review
  10. Pleiotrophin: Activity and mechanism.Advances in clinical chemistry · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Midkine in host defence.British journal of pharmacology · 2014
    Review
  19. Article
  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

11 authors at 4 institutions in 1 country.

Sara L SvenssonSection for Respiratory Medicine & Allergology, Department of Clinical Sciences Lund, Lund University, University Hospital, SE-221 85 Lund, Sweden.
Mukesh Pasupuleti
Björn Walse
Martin Malmsten
Matthias Mörgelin
Camilla Sjögren
Anders I Olin
Mattias Collin
Artur Schmidtchen
Ruth Palmer
Arne Egesten
Lund University · SEUmeå University · SESARomics Biostructures (Sweden) · SEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibacterial peptides of the innate immune system combat pathogenic microbes, but often have additional roles in promoting inflammation and as growth factors during tissue repair. Midkine (MK) and pleiotrophin (PTN) are the only two members of a family of heparin-binding growth factors. They show restricted expression during embryogenesis and are up-regulated in neoplasia. In addition, MK shows constitutive and inflammation-dependent expression in some non-transformed tissues of the adult. In the present study, we show that both MK and PTN display strong antibacterial activity, present at physiological salt concentrations. Electron microscopy of bacteria and experiments using artificial lipid bilayers suggest that MK and PTN exert their antibacterial action via a membrane disruption mechanism. The predicted structure of PTN, employing the previously solved MK structure as a template, indicates that both molecules consist of two domains, each containing three antiparallel beta-sheets. The antibacterial activity was mapped to the unordered C-terminal tails of both molecules and the last beta-sheets of the N-terminals. Analysis of the highly conserved MK and PTN orthologues from the amphibian Xenopus laevis and the fish Danio rerio suggests that they also harbor antibacterial activity in the corresponding domains. In support of an evolutionary conserved function it was found that the more distant orthologue, insect Miple2 from Drosophila melanogaster, also displays strong antibacterial activity. Taken together, the findings suggest that MK and PTN, in addition to their earlier described activities, may have previously unrealized important roles as innate antibiotics.

Indexed as

Evolution, MolecularAnimalsAnti-Bacterial AgentsCarrier ProteinsCytokinesDrosophila melanogasterDrosophila ProteinsEmbryonic DevelopmentGene Expression Regulation, DevelopmentalGene Expression Regulation, NeoplasticHumansLipid BilayersMidkineNeoplasmsNerve Growth FactorsPeptide MappingAnti-Bacterial AgentsCarrier ProteinsCytokinesDrosophila ProteinsLipid BilayersMDK protein, humanMidkineMiple2 protein, DrosophilaNerve Growth Factorspleiotrophin

Identifiers

PMID20308059
PMCPMC2871479
OpenAlexW2066649437

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.