Evidence map›Paper›PMID 15020697›Full record

ArticleThe Journal of physiology2004

Altered properties of volume-sensitive osmolyte and anion channels (VSOACs) and membrane protein expression in cardiac and smooth muscle myocytes from Clcn3-/- mice.

Shintaro Yamamoto-Mizuma, Ge-Xin Wang, Luis L Liu, Kathleen Schegg, William J Hatton, Dayue Duan, The Late Burton Horowitz, Fred S Lamb, Joseph R Hume

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Molecular biomarkers in cardiac hypertrophy.Journal of cellular and molecular medicine · 2019
    Review
  6. Observational
  7. Cl⁻ channels in smooth muscle cells.Pflugers Archiv : European journal of physiology · 2014
    Review
  8. Phenomics of cardiac chloride channels.Comprehensive Physiology · 2013
    Review
  9. Article
  10. Review
  11. Activation of volume regulated chloride channels protects myocardium from ischemia/reperfusion damage in second-window ischemic preconditioning.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. ClC3 is a critical regulator of the cell cycle in normal and malignant glial cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Shintaro Yamamoto-MizumaDepartment of Pharmacology, University of Nevada School of Medicine, Reno, NV, USA.
Ge-Xin Wang
Luis L Liu
Kathleen Schegg
William J Hatton
Dayue Duan
The Late Burton Horowitz
Fred S Lamb
Joseph R Hume
Centre of Biomedical Research · INUniversity of Nevada, Reno · USUniversity of Iowa · US

Funding

UNDERGRADUATE RESEARCH AND TRAININGP20RR016464 · NCRR · UNIVERSITY OF NEVADA RENO · PI SCHLAUCH, KAREN · 2001 to 2011
$30.3M
Signal transduction pathways regulated by cell volumeP20RR015581 · NCRR · UNIVERSITY OF NEVADA RENO · PI BRITTON, FIONA CATHERINE · 2000 to 2009
$19.5M
IONIC AND PHARMACOLOGICAL REGULATION OF VASCULAR CELLSR37HL049254 · NHLBI · UNIVERSITY OF NEVADA RENO · PI HUME, JOSEPH R · 1998 to 2007
$2.7M
IONIC AND PHARMACOLOGICAL REGULATION OF VASCULAR CELLSR01HL049254 · NHLBI · UNIVERSITY OF NEVADA RENO · PI HUME, JOSEPH R · 1993 to 1998
–
NCRR NIH HHS P20 RR015581NCRR NIH HHS P20 RR016464NCRR NIH HHS P20RR15581NCRR NIH HHS P20RR16464NHLBI NIH HHS HL49254NHLBI NIH HHS R01 HL049254NHLBI NIH HHS R37 HL049254
6 · The paper itself

Abstract

ClC-3, a member of the large superfamily of ClC voltage-dependent Cl(-) channels, has been proposed as a molecular candidate responsible for volume-sensitive osmolyte and anion channels (VSOACs) in some cells, including heart and vascular smooth muscle. However, the reported presence of native VSOACs in at least two cell types from transgenic ClC-3 disrupted (Clcn3(-/-)) mice casts considerable doubt on this proposed role for ClC-3. We compared several properties of native VSOACs and examined mRNA transcripts and membrane protein expression profiles in cardiac and pulmonary arterial smooth muscle cells from Clcn3(+/+) and Clcn3(-/-) mice to: (1) test the hypothesis that native VSOACs are unaltered in cells from Clcn3(-/-) mice, and (2) test the possibility that targeted inactivation of the Clcn3 gene using a conventional murine global knock-out approach may result in compensatory changes in expression of other membrane proteins. Our experiments demonstrate that VSOAC currents in myocytes from Clcn3(+/+) and Clcn3(-/-) mice are remarkably similar in terms of activation and inactivation kinetics, steady-state current densities, rectification, anion selectivity (I(-) > Cl(-)>> Asp(-)) and sensitivity to block by glibenclamide, niflumic acid, DIDS and extracellular ATP. However, additional experiments revealed several significant differences in other fundamental properties of native VSOACs recorded from atrial and smooth muscle cells from Clcn3(-/-) mice, including: differences in regulation by endogenous protein kinase C, differential sensitivity to block by anti-ClC-3 antibodies, and differential sensitivities to [ATP](i) and free [Mg(2+)](i). These results suggest that in response to Clcn3 gene deletion, there may be compensatory changes in expression of other proteins that alter VSOAC channel subunit composition or associated regulatory subunits that give rise to VSOACs with different properties. Consistent with this hypothesis, in atria from Clcn3(-/-) mice compared to Clcn3(+/+) mice, quantitative analysis of ClC mRNA expression levels revealed significant increases in transcripts for ClC-1, ClC-2, and ClC-3, and protein expression profiles obtained using two-dimensional polyacrylamide gel electrophoresis revealed complex changes in at least 35 different unidentified membrane proteins in cells from Clcn3(-/-) mice. These findings emphasize that caution needs to be exercised in simple attempts to interpret the phenotypic consequences of conventional global Clcn3 gene inactivation.

Indexed as

Adenosine TriphosphateAnimalsAntibodiesBrainChloride ChannelsHeart AtriaIon ChannelsMagnesiumMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutMyocytes, CardiacMyocytes, Smooth MuscleProtein Kinase CPulmonary ArteryAdenosine TriphosphateAntibodiesChloride ChannelsClC-3 channelIon ChannelsMagnesiumMembrane ProteinsProtein Kinase CRNA, Messenger

Identifiers

PMID15020697
PMCPMC1665092
OpenAlexW1913801606

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Registered trials

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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.