Evidence map›Paper›PMID 7523660›Full record

ArticleThe Journal of physiology1994

Calcium channel subtypes in cat chromaffin cells.

A Albillos, A R Artalejo, M G López, L Gandía, A G García, E Carbone

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-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

22 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. L-type calcium channels in exocytosis and endocytosis of chromaffin cells.Pflugers Archiv : European journal of physiology · 2018
    Review
  3. Roles of NaPflugers Archiv : European journal of physiology · 2018
    Review
  4. Regulation by L-type calcium channels of endocytosis: an overview.Journal of molecular neuroscience : MN · 2012
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Calcium-dependent inhibition of L, N, and P/Q Ca2+ channels in chromaffin cells: role of mitochondria.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  13. R-Type Ca2+ channels are coupled to the rapid component of secretion in mouse adrenal slice chromaffin cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Modulation of calcium current by ATP in guinea-pig adrenal chromaffin cells.Pflugers Archiv : European journal of physiology · 1996
    Article
  19. Article
  20. Multiple calcium channel subtypes in isolated rat chromaffin cells.Pflugers Archiv : European journal of physiology · 1995
    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 1 institution in 1 country.

A AlbillosDepartamento de Farmacología, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.
A R Artalejo
M G López
L Gandía
A G García
E Carbone
Universidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. Using the patch-clamp technique we have investigated the kinetic and pharmacological properties of high-voltage-activated (HVA) Ca2+ channels in short-term-cultured cat chromaffin cells. 2. In 10 mM Ba2+, HVA currents activated around -40 mV, reached maximal amplitude at 0 mV and reversed at about +60 mV. At 0 mV, HVA current activation was fast (mean tau act, 2.45 ms), and followed by either an incomplete inactivation or by a second slow phase of activation (mean tau slow, 36.8 ms) that was lost when Ba2+ was replaced by Ca2+. HVA Ba2+ currents deactivate quickly on repolarization to -50 mV (mean tau deact, 0.36 ms). 3. In most cells, HVA currents were sensitive to common dihydropyridine (DHP) derivatives. Nisoldipine blocked the currents maximally at low membrane potentials (mean block 76% at -30 mV, 3 microM) and gradually less at higher voltages. Nisoldipine block was clearly time dependent (33 and 56% after 30 and 600 ms, respectively, to 0 mV). 4. Bay K 8644 (3 microM) action was variable and caused (1) a 2- to 4-fold increase of Ba2+ currents at -40 to -20 mV, (2) a -15 mV shift of the current-voltage relationship and (3) a 10- to 20-fold prolongation of HVA channel deactivation at -50 mV. 5. Nisoldipine block and Bay K 8644 potentiation of HVA currents increased markedly in omega-conotoxin GVIA (omega-CgTX)-pretreated cells, suggesting an increased fraction of DHP-sensitive currents in these cells. Nisoldipine block of residual omega-CgTX-resistant currents was almost complete (mean block, 82%) during pulses of 1 s to 0 mV. 6. The degree of inhibition produced by omega-CgTX (2 microM for 1 min) varied from cell to cell (mean block, 46%) and was partly reversible. Residual omega-CgTX-resistant currents exhibited faster activation-deactivation kinetics than control currents. 7. The slow phase of HVA current activation was abolished if a conditioning prepulse of 40 ms to +70 mV preceded a test pulse to 0 mV. Double-pulse protocols caused an average current increase (facilitation) of 37% that was voltage dependent and which correlated with the slow phase of Ca2+ channel activation. Facilitation was lost in most omega-CgTX-treated cells and was little affected by nisoldipine (3 microM) and Bay K 8644 (1 microM). Facilitation was potentiated in cells dialysed with 100 microM guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S) and fully prevented by 1 mM guanosine 5'-O-(2-thiodiphosphate) (GDP-beta-S).(ABSTRACT TRUNCATED AT 400 WORDS)

Indexed as

3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAdrenal MedullaAnimalsBariumCalcium ChannelsCatsCell Membrane PermeabilityCells, CulturedDihydropyridinesFemaleIon Channel GatingMaleMembrane PotentialsNisoldipineomega-Conotoxin GVIAPatch-Clamp Techniques1,4-dihydropyridine3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterBariumCalcium ChannelsDihydropyridinesNisoldipineomega-Conotoxin GVIAPeptides

Identifiers

PMID7523660
PMCPMC1155622
OpenAlexW2154518969

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.