Evidence map›Paper›PMID 16439426›Full record

ArticleThe Journal of physiology2006

Human TRPC6 expressed in HEK 293 cells forms non-selective cation channels with limited Ca2+ permeability.

Mark Estacion, William G Sinkins, Stephen W Jones, Milana A B Applegate, William P Schilling

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.8field-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

57 citing papers in PubMed, 115 citations in OpenAlex.

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  14. Transmembrane insertases andThe Journal of biological chemistry · 2019
    Article
  15. -254C>G SNP in theInternational journal of genomics · 2019
    Article
  16. Trpc6 inactivation confers protection in a model of severe nephrosis in rats.Journal of molecular medicine (Berlin, Germany) · 2018
    Article
  17. Review
  18. Article
  19. Review
  20. Review
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

5 authors at 3 institutions in 1 country.

Mark EstacionRammelkamp Center for Education and Research, MetroHealth Medical Center, Cleveland, OH 44109-1998, USA.
William G Sinkins
Stephen W Jones
Milana A B Applegate
William P Schilling
Case Western Reserve University · USMetroHealth · USMetroHealth Medical Center · US

Funding

CALCIUM CHANNELS IN NONEXCITABLE CELLSR01GM052019 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI SCHILLING, WILLIAM P · 1995 to 2006
$2.5M
NIGMS NIH HHS GM52019NIGMS NIH HHS R01 GM052019
6 · The paper itself

Abstract

TRPC6 is thought to be a Ca(2+)-permeable cation channel activated following stimulation of G-protein-coupled membrane receptors linked to phospholipase C (PLC). TRPC6 current is also activated by exogenous application of 1-oleoyl-acetyl-sn-glycerol (OAG) or by inhibiting 1,2-diacylglycerol (DAG) lipase activity using RHC80267. In the present study, both OAG and RHC80267 increased whole-cell TRPC6 current in cells from a human embryonic kidney cell line (HEK 293) stably expressing TRPC6, but neither compound increased cytosolic free Ca(2+) concentration ([Ca(2+)](i)) when the cells were bathed in high-K(+) buffer to hold the membrane potential near 0 mV. These results suggested that TRPC6 channels have limited Ca(2+) permeability relative to monovalent cation permeability and/or that Ca(2+) influx via TRPC6 is greatly attenuated by depolarization. To evaluate Ca(2+) permeability, TRPC6 currents were examined in extracellular buffer in which Ca(2+) was varied from 0.02 to 20 mm. The results were consistent with a pore-permeation model in which Ca(2+) acts primarily as a blocking ion and contributes only a small percentage ( approximately 4%) to whole-cell currents in the presence of extracellular Na(+). Measurement of single-cell fura-2 fluorescence during perforated-patch recording of TRPC6 currents showed that OAG increased [Ca(2+)](i) 50-100 nm when the membrane potential was clamped at between -50 and -80 mV, but had little or no effect if the membrane potential was left uncontrolled. These results suggest that in cells exhibiting a high input resistance, the primary effect of activating TRPC6 will be membrane depolarization. However, in cells able to maintain a hyperpolarized potential (e.g. cells with a large inwardly rectifying or Ca(2+)-activated K(+) current), activation of TRPC6 will lead to a sustained increase in [Ca(2+)](i). Thus, the contribution of TRPC6 current to both the kinetics and magnitude of the Ca(2+) response will be cell specific and dependent upon the complement of other channel types.

Indexed as

CalciumCell LineCell Membrane PermeabilityCyclohexanonesDiglyceridesElectrophysiologyEstrenesHumansKidneyMembrane PotentialsModels, BiologicalPatch-Clamp TechniquesPhosphodiesterase InhibitorsPotassiumProtease InhibitorsPyrrolidinones1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione1,6-bis(cyclohexyloximinocarbonyl)hexane1-oleoyl-2-acetylglycerolCalciumCyclohexanonesDiglyceridesEstrenesPhosphodiesterase InhibitorsPotassiumProtease InhibitorsPyrrolidinonesSodiumTRPC6 Cation ChannelTRPC6 protein, humanTRPC Cation ChannelsU 73343

Identifiers

PMID16439426
PMCPMC1779672
OpenAlexW1587254203

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.