Evidence map›Paper›PMID 25238780›Full record

ArticleCellular and molecular life sciences : CMLS2015

Endogenous animal toxin-like human β-defensin 2 inhibits own K(+) channels through interaction with channel extracellular pore region.

Weishan Yang, Jing Feng, Fang Xiang, Zili Xie, Guoyi Zhang, Jean-Marc Sabatier, Zhijian Cao, Wenxin Li, Zongyun Chen, Yingliang Wu

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Fibrinogen and tumors.Frontiers in oncology · 2024
    Review
  2. Article
  3. Antimicrobial Mechanism of pBD2 againstMolecules (Basel, Switzerland) · 2020
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Construction ofAsian-Australasian journal of animal sciences · 2017
    Article
  11. Article
  12. Article
  13. Why do we study animal toxins?Dong wu xue yan jiu = Zoological research · 2015
    Review
  14. Article
  15. 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

10 authors at 3 institutions in 2 countries.

Weishan YangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Jing Feng
Fang Xiang
Zili Xie
Guoyi Zhang
Jean-Marc Sabatier
Zhijian Cao
Wenxin Li
Zongyun Chen
Yingliang Wu
Wuhan University · CNCentre d’Immunologie de Marseille-Luminy · FRChinese Academy of Medical Sciences Dermatology Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human potassium channels are widely inhibited by peptide toxins from venomous animals. However, no human endogenous peptide inhibitor has been discovered so far. In this study, we demonstrate for the first time using electrophysiological techniques, that endogenous human β-defensin 2 (hBD2) is able to selectively and dose-dependently inhibit the human voltage-gated Kv1.3 channel at picomolar peptide concentration. The co-immunoprecipitation assays further supported the selective binding of hBD2 to Kv1.3 channel. Using mutagenesis experiments, we found that the outer pore domain of Kv1.3 channel was the binding site of hBD2, which is similar to the interacting site of Kv1.3 channel recognized by animal toxin inhibitors. The hBD2 was able to suppress IL-2 production through inhibition of Kv1.3 channel currents in human Jurkat cells, which was further confirmed by the lack of hBD2 activity on IL-2 production after Kv1.3 knockdown in these cells. More interestingly, hBD2 was also found to efficiently inhibit Kv1.3 channel currents and suppress IL-2 production in both human primary CD3(+) T cells and peripheral mononuclear cells from either healthy donors or psoriasis patients. Our findings not only evidenced hBD2 as the first characterized endogenous peptide inhibitor of human potassium channels, but also paved a promising avenue to investigate newly discovered function of hBD2 as Kv1.3 channel inhibitor in the immune system and other fields.

Indexed as

Amino Acid SequenceAnimalsbeta-DefensinsBinding SitesCells, CulturedHumansInterleukin-2Jurkat CellsKv1.3 Potassium ChannelLeukocytes, MononuclearMolecular Sequence DataMutagenesisPatch-Clamp TechniquesProtein BindingRNA InterferenceRNA, Small Interferingbeta-DefensinsDEFB4A protein, humanInterleukin-2Kv1.3 Potassium ChannelRNA, Small InterferingToxins, Biological

Identifiers

PMID25238780
PMCPMC11113244
OpenAlexW1997550667

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.