Evidence map›Paper›PMID 21907716›Full record

ArticleGeneral and comparative endocrinology2011

Characterization of novel Pannexin 1 isoforms from rat pituitary cells and their association with ATP-gated P2X channels.

Shuo Li, Melanija Tomić, Stanko S Stojilkovic

Open access · greenAbstract read
In one paragraph

Article in General and comparative endocrinology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.3field-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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Contribution of pannexin channels to afterimage signals in the amphibian retina.American journal of physiology. Cell physiology · 2025
    Article
  2. Review
  3. Review
  4. Pannexin1 channels in the liver: an open enemy.Frontiers in cell and developmental biology · 2023
    Review
  5. Functional Coupling between the P2XInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. ATP release into ADPKD cysts via pannexin-1/P2X7 channels decreases ENaC activity.Biochemical and biophysical research communications · 2019
    Article
  8. Review
  9. P2X7 Interactions and Signaling - Making Head or Tail of It.Frontiers in molecular neuroscience · 2019
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Pannexin1 as mediator of inflammation and cell death.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  17. Article
  18. Review
  19. Review
  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

3 authors at 2 institutions in 1 country.

Shuo LiSection on Cellular Signaling, Program in Developmental Neuroscience, NICHD, National Institutes of Health, Bethesda, MD 20892-4510, USA. lishuo@mail.nih.gov
Melanija Tomić
Stanko S Stojilkovic
National Institutes of Health · USEunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Intracellular Signaling In Endocrine CellsZIAHD000195 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STOJILKOVIC, STANKO S. · 2009 to 2025
$18.8M
Intramural NIH HHS ZIA HD000195
6 · The paper itself

Abstract

Our previous studies have showed that Pannexin 1 (Panx1), a member of a recently discovered family of gap junction proteins, is expressed in the pituitary gland. Here we investigated the presence and expression pattern of Panx1 isoforms in pituitary cells, their roles in ATP release, and their association with purinergic P2X receptor subtypes that are native to pituitary cells. In addition to the full-size Panx1, termed Panx1a, pituitary cells also express two novel shorter isoforms, termed Panx1c and Panx1d, which formation reflects the existence of alternative splicing sites in exons 2 and 4, respectively. Panx1c is lacking the Phe108-Gln180 sequence and P2X1d is missing the Val307-Cys426 C-terminal end sequence. Confocal microscopy and biotin labeling revealed that Panx1a is expressed in the plasma membrane, whereas Panx1c and Panx1d show the cytoplasmic localization when expressed as homomeric proteins. The three Panx1 isoforms and Panx2 form homomeric and heteromeric complexes in any combination. These splice forms can also physically associate with ATP-gated P2X2, P2X3, P2X4, and P2X7 receptor channels. The Panx1a-mediated ATP release in AtT-20 immortalized pituitary cells is attenuated when co-expressed with Panx1c or Panx1d. These results suggest that Panx1c and Panx1d may serve as dominant-negative effectors to modulate the functions of Panx1a through formation of heteromeric channels. The complex patterns of Panx1 expression and association could also define the P2X-dependent roles of these channels in cell types co-expressing both proteins.

Indexed as

AnimalsBlotting, WesternCell LineCells, CulturedConnexinsFemaleHumansImmunoprecipitationNerve Tissue ProteinsPituitary GlandProtein BindingRatsRats, Sprague-DawleyReceptors, Purinergic P2XConnexinsNerve Tissue Proteinspannexin 1, ratReceptors, Purinergic P2X

Identifiers

PMID21907716
PMCPMC3195874
OpenAlexW2074354465

What OpenQuestion holds

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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.