Evidence map›Paper›PMID 9806963›Full record

ArticleThe Journal of general physiology1998

In intact cone photoreceptors, a Ca2+-dependent, diffusible factor modulates the cGMP-gated ion channels differently than in rods.

T I Rebrik, J I Korenbrot

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of general physiology, 1998. 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 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

36 citing papers in PubMed, 73 citations in OpenAlex.

  1. Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  5. EML1 (CNG-modulin) controls light sensitivity in darkness and under continuous illumination in zebrafish retinal cone photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  6. Review
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  9. CNG-modulin: a novel Ca-dependent modulator of ligand sensitivity in cone photoreceptor cGMP-gated ion channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  10. Review
  11. Article
  12. Article
  13. Structure of cone photoreceptors.Progress in retinal and eye research · 2009
    Review
  14. Article
  15. How vision begins: an odyssey.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Review
  16. Article
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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

2 authors at 1 institution in 1 country.

T I RebrikDepartment of Physiology, School of Medicine, University of California at San Francisco, San Francisco, California 94143, USA.
J I Korenbrot
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We investigated the modulation of cGMP-gated ion channels in single cone photoreceptors isolated from a fish retina. A new method allowed us to record currents from an intact outer segment while controlling its cytoplasmic composition by superfusion of the electropermeabilized inner segment. The sensitivity of the channels to agonists in the intact outer segment differs from that measured in membrane patches detached from the same cell. This sensitivity, measured as the ligand concentration necessary to activate half-maximal currents, K1/2, also increases as Ca2+ concentration decreases. In electropermeabilized cones, K1/2 for cGMP is 335.5 +/- 64.4 microM in the presence of 20 microM Ca2+, and 84.3 +/- 12.6 microM in its absence. For 8Br-cGMP, K1/2 is 72.7 +/- 11.3 microM in the presence of 20 microM Ca2+ and 15.3 +/- 4.5 microM in its absence. The Ca2+-dependent change in agonist sensitivity is larger in extent than that measured in rods. In electropermeabilized tiger salamander rods, K1/2 for 8Br-cGMP is 17.9 +/- 3.8 microM in the presence of 20 microM Ca2+ and 7.2 +/- 1.2 microM in its absence. The Ca2+-dependent modulation is reversible in intact cone outer segments, but is progressively lost in the absence of divalent cations, suggesting that it is mediated by a diffusible factor. Comparison of data in intact cells and detached membrane fragments from cones indicates that this factor is not calmodulin. At 40 microM 8Br-cGMP, the Ca2+-dependent change in sensitivity in cones is half-maximal at KCa = 286 +/- 66 nM Ca2+. In rods, by contrast, KCa is approximately 50 nM Ca2+. The difference in magnitude and Ca2+ dependence of channel modulation between photoreceptor types suggests that this modulation may play a more significant role in the regulation of photocurrent gain in cones than in rods.

Indexed as

Adaptation, OcularAnimalsBassCalciumCyclic GMPDark AdaptationElectrophysiologyIon Channel GatingIon ChannelsMembrane ProteinsRetinal Cone Photoreceptor CellsRetinal Rod Photoreceptor CellsVision, Ocular8-bromocyclic GMPCalciumCyclic GMPIon ChannelsMembrane Proteins

Identifiers

PMID9806963
PMCPMC2229438
OpenAlexW2111855919

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.