Evidence map›Paper›PMID 22796188›Full record

ReviewBiochimica et biophysica acta2013

Paracrine signaling through plasma membrane hemichannels.

Nan Wang, Marijke De Bock, Elke Decrock, Mélissa Bol, Ashish Gadicherla, Mathieu Vinken, Vera Rogiers, Feliksas F Bukauskas, Geert Bultynck, Luc Leybaert

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

120 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Noncanonical functions of adhesion proteins in inflammation.American journal of physiology. Cell physiology · 2024
    Review
  10. Review
  11. Measurement of CaMethods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Article
  13. A Chemical Chaperone Restores Connexin 26 Mutant Activity.ACS pharmacology & translational science · 2023
    Article
  14. Article
  15. Article
  16. A Quantitative Assay for CaInternational journal of molecular sciences · 2022
    Article
  17. Article
  18. Review
  19. Review
  20. Frontiers in molecular neuroscience · 2022
    Article

60 more citing papers are in PubMed but not listed here.

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 4 institutions in 2 countries.

Nan WangDepartment of Basic Medical Sciences, Ghent University, Ghent, Belgium.
Marijke De Bock
Elke Decrock
Mélissa Bol
Ashish Gadicherla
Mathieu Vinken
Vera Rogiers
Feliksas F Bukauskas
Geert Bultynck
Luc Leybaert
Ghent University · BEVrije Universiteit Brussel · BEAlbert Einstein College of Medicine · USKU Leuven · BE

Funding

Connexins and Heart FunctionR01HL084464 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2007 to 2010
$1.7M
Gating of Connexin-Based Gap Junction Channels and HemichannelsR01NS072238 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2010 to 2013
$1.4M
NHLBI NIH HHS R01 HL084464NHLBI NIH HHS R01HL084464NINDS NIH HHS R01 NS072238NINDS NIH HHS R01NS072238
6 · The paper itself

Abstract

Plasma membrane hemichannels composed of connexin (Cx) proteins are essential components of gap junction channels but accumulating evidence suggests functions of hemichannels beyond the communication provided by junctional channels. Hemichannels not incorporated into gap junctions, called unapposed hemichannels, can open in response to a variety of signals, electrical and chemical, thereby forming a conduit between the cell's interior and the extracellular milieu. Open hemichannels allow the bidirectional passage of ions and small metabolic or signaling molecules of below 1-2kDa molecular weight. In addition to connexins, hemichannels can also be formed by pannexin (Panx) proteins and current evidence suggests that Cx26, Cx32, Cx36, Cx43 and Panx1, form hemichannels that allow the diffusive release of paracrine messengers. In particular, the case is strong for ATP but substantial evidence is also available for other messengers like glutamate and prostaglandins or metabolic substances like NAD(+) or glutathione. While this field is clearly in expansion, evidence is still lacking at essential points of the paracrine signaling cascade that includes not only messenger release, but also downstream receptor signaling and consequent functional effects. The data available at this moment largely derives from in vitro experiments and still suffers from the difficulty of separating the functions of connexin-based hemichannels from gap junctions and from pannexin hemichannels. However, messengers like ATP or glutamate have universal roles in the body and further defining the contribution of hemichannels as a possible release pathway is expected to open novel avenues for better understanding their contribution to a variety of physiological and pathological processes. This article is part of a Special Issue entitled: The Communicating junctions, roles and dysfunctions.

Indexed as

Paracrine CommunicationAdenosine TriphosphateAnimalsCell MembraneConnexin 26ConnexinsDinoprostoneGlutamic AcidGlutathioneHumansMembrane PotentialsNADProtein Processing, Post-TranslationalAdenosine TriphosphateConnexin 26ConnexinsDinoprostoneGJB2 protein, humanGlutamic AcidGlutathioneNAD

Identifiers

PMID22796188
PMCPMC3666170
OpenAlexW2173583071

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.