Evidence map›Paper›PMID 25448737›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2015

Membrane-mediated actions of 1,25-dihydroxy vitamin D3: a review of the roles of phospholipase A2 activating protein and Ca(2+)/calmodulin-dependent protein kinase II.

Maryam Doroudi, Zvi Schwartz, Barbara D Boyan

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
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  7. Article
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  10. Review
  11. Article
  12. Review
  13. Calcifediol: Why, When, How Much?Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. ERp57/PDIA3: new insight.Cellular & molecular biology letters · 2022
    Review
  20. 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

3 authors at 2 institutions in 1 country.

Maryam DoroudiSchool of Biology, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Zvi SchwartzDepartment of Biomedical Engineering, Virginia Commonwealth University, Richmond, VA 23284, USA; Department of Periodontics, University of Texas Health Science Center, San Antonio, TX 78284, USA.
Barbara D BoyanSchool of Biology, Georgia Institute of Technology, Atlanta, GA 30332, USA; Department of Biomedical Engineering, Virginia Commonwealth University, Richmond, VA 23284, USA; Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, GA 30332, USA.
Georgia Institute of Technology · USThe University of Texas Health Science Center at San Antonio · US

Funding

Atlanta Clinical and Translational Science Institute (ACTSI) RenewalUL1TR000454 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$25.8M
Mechanisms of Cell/Surface InteractionR01AR052102 · NIAMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI BOYAN, BARBARA D. · 2006 to 2015
$3.3M
Atlanta Clinical and Translational Science Institute (ACTSI) RenewalTL1TR000456 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$1.2M
NCATS NIH HHS TL1 TR000456NCATS NIH HHS UL1 TR000454NIAMS NIH HHS R01 AR052102
6 · The paper itself

Abstract

The secosteroid 1α,25-dihydroxy vitamin D3 [1α,25(OH)2D3] acts on cells via classical steroid hormone receptor-mediated gene transcription and by initiating rapid membrane-mediated signaling pathways. In its membrane-initiated pathway, after 1α,25(OH)2D3 interacts with protein disulfide isomerase, family A, member 3 (Pdia3) in caveolae, phospholipase A2 (PLA2) and protein kinase C (PKC) are activated. Recent efforts to determine the signaling proteins involved in the 1α,25(OH)2D3 signal from Pdia3 to PLA2 have indicated that phospholipase A2 activating protein (PLAA) and Ca(2+)/calmodulin-dependent kinase II (CaMKII) are required. PLAA is located in caveolae, where it interacts with Pdia3 and caveolin-1 (Cav-1) to initiate rapid signaling via CaMKII, activating PLA2, leading to activation of protein kinase C (PKC) and PKC-dependent responses.

Indexed as

AnimalsCalcitriolCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell MembraneEnzyme ActivationGene SilencingHumansPhospholipases A2Protein Kinase CProteinsSignal TransductionCalcitriolCalcium-Calmodulin-Dependent Protein Kinase Type 2phospholipase A2-activating proteinPhospholipases A2Protein Kinase CProteins1α,25(OH)(2)D(3)Ca(2+)/calmodulin-dependent protein kinase IIPDIA3PLA(2)PLAAProtein kinase C

Identifiers

PMID25448737
PMCPMC4323845
OpenAlexW2068049217

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.