Evidence map›Paper›PMID 9490822›Full record

ArticleThe Journal of physiology1998

Facilitation by the beta2a subunit of pore openings in cardiac Ca2+ channels.

J Costantin, F Noceti, N Qin, X Wei, L Birnbaumer, E Stefani

Abstract read
In one paragraph

Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Mapping the interaction surface between CaNature communications · 2025
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  3. Review
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  8. Membrane-associated guanylate kinase-like properties of beta-subunits required for modulation of voltage-dependent Ca2+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2004
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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

6 authors.

J CostantinDepartment of Anesthesiology, UCLA School of Medicine, UCLA, Los Angeles, CA 90095, USA. jcostant@ucla.edu
F Noceti
N Qin
X Wei
L Birnbaumer
E Stefani

Funding

VOLTAGE GATED CALCIUM CHANNELS--STRUCTURE/FUNCTIONR01AR038970 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI STEFANI, ENRICO · 1987 to 1998
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STRUCTURE/FUNCTION ANALYSIS OF VOLTAGE-GATED CA CHANNELSR01AR043411 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BIRNBAUMER, LUTZ · 1994 to 1998
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NIAMS NIH HHS AR38970NIAMS NIH HHS AR43411
6 · The paper itself

Abstract

1. Single channel recordings were performed on the cardiac calcium channel (alpha1C) in order to study the effect of coexpression of the accessory beta2a subunit. On-cell patch clamp recordings were performed after expression of these channels in Xenopus oocytes. 2. The alpha1C subunit, when expressed alone, had similar single channel properties to native cardiac channels. Slow transitions between low and high open probability (Po) gating modes were found as well as fast gating transitions between the open and closed states. 3. Coexpression of the beta2a subunit caused changes in the fast gating during high Po mode. In this mode, open time distributions reveal at least three open states and the beta2a subunit favours the occupancy of the longest, 10-15 ms open state. No effect of the beta2a subunit was found when the channel was gating in the low Po mode. 4. Slow gating transitions were also affected by the beta2a subunit. The high Po mode was maintained for the duration of the depolarizing pulse in the presence of the beta2a subunit; while the alpha1C channel when expressed alone, frequently switched into and out of the high Po mode during the course of a sweep. 5. The beta2a subunit also affected mode switching that occurred between sweeps. Runs analysis revealed that the alpha1C subunit has a tendency toward non-random mode switching. The beta2a subunit increased this tendency. A chi2 analysis of contingency tables indicated that the beta2a subunit caused the alpha1C channel to gain 'intrinsic memory', meaning that the mode of a given sweep can be non-independent of the mode of the previous sweep. 6. We conclude that the beta2a subunit causes changes to the alpha1C channel in both its fast and slow gating behaviour. The beta2a subunit alters fast gating by facilitating movement of the channel into an existing open state. Additionally, the beta2a subunit decreases the slow switching between low and high Po modes.

Indexed as

3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAnimalsCalcium Channel AgonistsCalcium ChannelsFemaleIon Channel GatingMyocardiumOocytesPatch-Clamp TechniquesProbabilityXenopus3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterCalcium Channel AgonistsCalcium Channels

Identifiers

PMID9490822
PMCPMC2230783

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.