Evidence map›Paper›PMID 12885640›Full record

ArticleBiophysical journal2003

Regulation of calcium channel activity by lipid domain formation in planar lipid bilayers.

Brian Cannon, Martin Hermansson, Sandor Györke, Pentti Somerharju, Jorma A Virtanen, Kwan Hon Cheng

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

19 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  5. Pneumolysin-damaged cells benefit from non-homogeneous toxin binding to cholesterol-rich membrane domains.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018
    Article
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  7. Review
  8. Neuronal porosome lipidome.Journal of cellular and molecular medicine · 2014
    Article
  9. Article
  10. Halothane changes the domain structure of a binary lipid membrane.Langmuir : the ACS journal of surfaces and colloids · 2012
    Article
  11. Article
  12. Article
  13. Membranes: a meeting point for lipids, proteins and therapies.Journal of cellular and molecular medicine · 2008
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

6 authors at 3 institutions in 2 countries.

Brian CannonDepartment of Physics, Texas Tech University, Lubbock, Texas 79409, USA.
Martin Hermansson
Sandor Györke
Pentti Somerharju
Jorma A Virtanen
Kwan Hon Cheng
Texas Tech University · USUniversity of Helsinki · FIUniversity of Jyväskylä · FI

Funding

ADAPTATION--CONTROL MECHANISM OF CA2 RELEASE IN HEARTR29HL052620 · NHLBI · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GYORKE, SANDOR · 1995 to 1998
–
NHLBI NIH HHS HL-52620
6 · The paper itself

Abstract

The sarcoplasmic reticulum channel (ryanodine receptor) from cardiac myocytes was reconstituted into planar lipid bilayers consisting of 1-palmitoyl-2-oleoyl-phosphatidylethanolamine (POPE) and 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) in varying ratios. The channel activity parameters, i.e., open probability and average open time and its resolved short and long components, were determined as a function of POPE mole fraction (X(PE)) at 22.4 degrees C. Interestingly, all of these parameters exhibited a narrow and pronounced peak at X(PE) approximately 0.80. Differential scanning calorimetric measurements on POPE/POPC liposomes with increasing X(PE) indicated that the lipid bilayer enters a composition-driven transition from the liquid-crystalline state to the gel state at 22.4 degrees C when X(PE) approaches 0.80. Thus, the peaking of the reconstituted channel activity at X(PE) approximately 0.80 in the planar bilayer could result from the appearance of gel/liquid-crystalline domain boundaries at this POPE content. Lipid packing at domain boundaries is known to be looser as compared to the homogenous gel or liquid-crystalline state. We propose that the attractive potential of packing defects at lipid domain boundaries and entropic excluded-volume effects could result in the direct interactions of the transmembrane region of the channel protein with the lipid-packing defects at the lipid/protein interface, which could thus provide a favorable environment for the open state of the protein. The present findings indicate that the activity of the sarcoplasmic reticulum calcium channel could be modulated by lipid domain formation upon slight changes in membrane lipid composition in vivo.

Indexed as

Membrane FluidityMembrane PotentialsCalcium ChannelsElectric CapacitanceIon Channel GatingLipid BilayersMembrane MicrodomainsMembranes, ArtificialMolecular ConformationPhosphatidylcholinesPhosphatidylethanolaminesProtein ConformationRyanodine Receptor Calcium Release ChannelStructure-Activity Relationship1-palmitoyl-2-oleoylphosphatidylcholine1-palmitoyl-2-oleoylphosphatidylethanolamineCalcium ChannelsLipid BilayersMembranes, ArtificialPhosphatidylcholinesPhosphatidylethanolaminesRyanodine Receptor Calcium Release Channel

Identifiers

PMID12885640
PMCPMC1303214
OpenAlexW2080185346

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.