Evidence map›Paper›PMID 19796812›Full record

ArticleCell calcium2009

The alpha(2)delta subunit augments functional expression and modifies the pharmacology of Ca(V)1.3 L-type channels.

Arturo Andrade, Alejandro Sandoval, Ricardo González-Ramírez, Diane Lipscombe, Kevin P Campbell, Ricardo Felix

Open access · bronzeAbstract read
In one paragraph

Article in Cell calcium, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Review
  3. The Leucine-Rich Repeat Kinase 2 Variant LRRK2International journal of molecular sciences · 2025
    Article
  4. Article
  5. Article
  6. Ion channel long non-coding RNAs in neuropathic pain.Pflugers Archiv : European journal of physiology · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Regulation of high-voltage-activated CaWiley interdisciplinary reviews. Membrane transport and signaling · 2013
    Article
  14. Review
  15. Review
  16. Article
  17. 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 5 institutions in 2 countries.

Arturo AndradeDepartment of Physiology, Biophysics and Neuroscience, Center for Research and Advanced Studies of the National Polytechnic Institute, Cinvestav-IPN, Mexico City, Mexico.
Alejandro Sandoval
Ricardo González-Ramírez
Diane Lipscombe
Kevin P Campbell
Ricardo Felix
Center for Research and Advanced Studies of the National Polytechnic Institute · MXBrown University · USInstituto Politécnico Nacional · MXUniversidad Nacional Autónoma de México · MXUniversity of Iowa · US

Funding

NEURONAL CALCIUM CHANNELS--REGULATION AND FUNCTIONR01NS029967 · NINDS · BROWN UNIVERSITY · PI LIPSCOMBE, DIANE · 1997 to 2009
$3.0M
Howard Hughes Medical InstituteNINDS NIH HHS R01 NS029967
6 · The paper itself

Abstract

The auxiliary Ca(V)alpha(2)delta-1 subunit is an important component of voltage-gated Ca(2+) (Ca(V)) channel complexes in many tissues and of great interest as a drug target. Nevertheless, its exact role in specific cell functions is still unknown. This is particularly important in the case of the neuronal L-type Ca(V) channels where these proteins play a key role in the secretion of neurotransmitters and hormones, gene expression, and the activation of other ion channels. Therefore, using a combined approach of patch-clamp recordings and molecular biology, we studied the role of the Ca(V)alpha(2)delta-1 subunit on the functional expression and the pharmacology of recombinant L-type Ca(V)1.3 channels in HEK-293 cells. Co-expression of Ca(V)alpha(2)delta-1 significantly increased macroscopic currents and conferred the Ca(V)1.3alpha(1)/Ca(V)beta(3) channels sensitivity to the antiepileptic/analgesic drugs gabapentin and AdGABA. In contrast, Ca(V)alpha(2)delta-1 subunits harboring point mutations in N-glycosylation consensus sequences or the proteolytic site as well as in conserved cysteines in the transmembrane delta domain of the protein, reduced functionality in terms of enhancement of Ca(V)1.3alpha(1)/Ca(V)beta(3) currents. In addition, co-expression of the delta domain drastically inhibited macroscopic currents through recombinant Ca(V)1.3 channels possibly by affecting channel synthesis. Together these results provide several lines of evidence that the Ca(V)alpha(2)delta-1 auxiliary subunit may interact with Ca(V)1.3 channels and regulate their functional expression.

Indexed as

AcetatesAminesAnimalsCalciumCalcium Channel BlockersCalcium ChannelsCalcium Channels, L-TypeCell LineCyclohexanecarboxylic AcidsGabapentingamma-Aminobutyric AcidHumansPatch-Clamp TechniquesRabbitsRatsRecombinant Fusion Proteins2-aminomethyl-2-tricyclo(3.3.1.1(1,7))decaneacetic acid hydrochlorideAcetatesAminesCacna1d protein, ratCacna2d1 protein, ratCalciumCalcium Channel BlockersCalcium ChannelsCalcium Channels, L-TypeCyclohexanecarboxylic AcidsGabapentingamma-Aminobutyric AcidRecombinant Fusion Proteins

Identifiers

PMID19796812
PMCPMC7178495
OpenAlexW2142593292

What OpenQuestion holds

Textmetadata
LicenceTDM
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.