Evidence map›Paper›PMID 19103198›Full record

ArticleExperimental eye research2009

Upregulation and maintenance of gap junctional communication in lens cells.

Bruce A Boswell, Anh-Chi N Le, Linda S Musil

Open access · greenAbstract read
In one paragraph

Article in Experimental eye research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 26% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. ErbBs in Lens Cell Fibrosis and Secondary Cataract.Investigative ophthalmology & visual science · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The effects of age on lens transport.Investigative ophthalmology & visual science · 2013
    Article
  19. Article
  20. The effect of size and species on lens intracellular hydrostatic pressure.Investigative ophthalmology & visual science · 2013
    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.

Bruce A BoswellDepartment of Biochemistry and Molecular Biology L224, Oregon Health and Science University, Portland, OR 97239, USA.
Anh-Chi N Le
Linda S Musil
Howard Hughes Medical Institute · USOregon Health & Science University · US

Funding

Regulation of Lens Cell Coupling and DifferentiationR01EY014622 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI MUSIL, LINDA S · 2003 to 2010
$2.3M
NEI NIH HHS EY014622NEI NIH HHS R01 EY014622
6 · The paper itself

Abstract

The cells of the lens are joined by an extensive network of gap junction intercellular channels consisting of connexins 43, 46, and 50. We have proposed, and experimentally supported, the hypothesis that fibroblast growth factor (FGF) signaling is required for upregulation of gap junction-mediated intercellular coupling (GJIC) at the lens equator. The ability of FGF to increase GJIC in cultured lens cells requires sustained activation of extracellular signal-regulated kinase (ERK). In other cell types, activation of ERK has been shown to block GJIC mediated by connexin43 (Cx43). Why ERK signaling does not block lens cell coupling is not known. Another unresolved issue in lens gap junction regulation is how connexins, synthesized before the loss of biosynthetic organelles in mature lens fiber cells, avoid degradation during formation of the organelle-free zone. We have addressed these questions using serum-free cultures (termed DCDMLs) of primary embryonic chick lens epithelial cells. We show that FGF stimulates ERK in DCDMLs via the canonical Ras/Raf1 pathway, and that the reason that neither basal nor growth factor-stimulated GJIC is blocked by activation of ERK is because it is not mediated by Cx43. In fibroblastic cells, the normally rapid rate of degradation of Cx43 after its transport to the plasma membrane is reduced by treatments that either directly (ALLN; epoxomicin) or indirectly (generation of oxidatively un/mis-folded proteins by arsenic compounds) prevent the ubiquitin/proteasome system (UPS) from acting on its normal substrates. We show here that Cx45.6 and Cx56, the chick orthologs of mammalian Cx50 and Cx46, behave similarly in DCDMLs. When organelles lyse during the maturation of fiber cells, they release into the cytosol a large amount of new proteins that have the potential to saturate the capacity, and/or compromise the function, of the UPS. This would serve to spare gap junctions from degradation during formation of the organelle-free zone, thereby preserving GJIC between mature fiber cells despite the lack of de novo connexin synthesis.

Indexed as

AnimalsCell CommunicationCells, CulturedChick EmbryoConnexin 43Culture Media, Serum-FreeEnzyme ActivationExtracellular Signal-Regulated MAP KinasesFibroblast Growth FactorsGap JunctionsLens, CrystallinePhosphorylationPlasmidsProteasome Endopeptidase ComplexTransfectionUbiquitinConnexin 43Culture Media, Serum-FreeExtracellular Signal-Regulated MAP KinasesFibroblast Growth FactorsProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID19103198
PMCPMC2853755
OpenAlexW2027049042

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.