Evidence map›Paper›PMID 18443816›Full record

ArticlePflugers Archiv : European journal of physiology2008

Pharmacological and biophysical properties of Ca2+ channels and subtype distributions in human adrenal chromaffin cells.

Alberto Pérez-Alvarez, Alicia Hernández-Vivanco, María Cano-Abad, Almudena Albillos

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Roles of NaPflugers Archiv : European journal of physiology · 2018
    Review
  4. Human nicotinic receptors in chromaffin cells: characterization and pharmacology.Pflugers Archiv : European journal of physiology · 2018
    Review
  5. Article
  6. Native α6β4* nicotinic receptors control exocytosis in human chromaffin cells of the adrenal gland.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  7. 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

4 authors at 1 institution in 1 country.

Alberto Pérez-AlvarezDepartamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, c/ Arzobispo Morcillo 4, 28029, Madrid, Spain.
Alicia Hernández-Vivanco
María Cano-Abad
Almudena Albillos
Universidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we explored the pharmacological and biophysical properties of voltage-activated Ca2+ channels in human chromaffin cells using the perforated-patch configuration of the patch-clamp technique. According to their pharmacological sensitivity to Ca2+ channel blockers, cells could be sorted into two groups of similar size showing the predominance of either N- or P/Q-type Ca2+ channels. R-type Ca2+ channels, blocked by 77% with 20 muM Cd2+ and not affected by 50 muM Ni2+, were detected for the first time in human chromaffin cells. Immunocytochemical experiments revealed an even distribution of alpha (1E) Ca2+ channels in these cells. With regard to their biophysical properties, L- and R-type channels were activated at membrane potentials that were 15-20 mV more negative than P/Q- and N-type channels. Activation time constants showed no variation with voltage for the L-type channels, decreased with increasing potentials for the R- and P/Q-type channels, and displayed a bell shape with a maximum at 0 mV for the N-type channels. R-type channels were also the most inactivated channels. We thus show here that human chromaffin cells possess all the Ca2+ channel types described in neurons, L, N, P/Q, and R channels, but the relative contributions of N and P/Q channels differ among cells. Given that N- and P/Q-type Ca2+ channel types can be differentially modulated, these findings suggest the possibility of cell-specific regulation in human chromaffin cells.

Indexed as

Calcium Channel BlockersCalcium ChannelsCalcium Channels, R-TypeCation Transport ProteinsCells, CulturedChromaffin CellsDopamine beta-HydroxylaseElectrophysiologyHumansImmunohistochemistryPatch-Clamp TechniquesPhenylethanolamine N-MethyltransferaseCACNA1E protein, humanCalcium Channel BlockersCalcium ChannelsCalcium Channels, R-TypeCation Transport ProteinsDopamine beta-HydroxylasePhenylethanolamine N-Methyltransferase

Identifiers

PMID18443816
OpenAlexW2072155469

What OpenQuestion holds

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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.