Evidence map›Paper›PMID 19261907›Full record

ArticleAmerican journal of physiology. Cell physiology2009

Dynamic interactions between L-type voltage-sensitive calcium channel Cav1.2 subunits and ahnak in osteoblastic cells.

Ying Shao, Kirk J Czymmek, Patricia A Jones, Victor P Fomin, Kamil Akanbi, Randall L Duncan, Mary C Farach-Carson

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

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  14. Association of the α(2)δ(1) subunit with Ca(v)3.2 enhances membrane expression and regulates mechanically induced ATP release in MLO-Y4 osteocytes.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2011
    Article
  15. Review
  16. Ahnak1 modulates L-type Ca(2+) channel inactivation of rodent cardiomyocytes.Pflugers Archiv : European journal of physiology · 2010
    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

7 authors at 1 institution in 1 country.

Ying ShaoDept. of Biological Sciences, University of Delaware, Newark, DE 19716, USA.
Kirk J Czymmek
Patricia A Jones
Victor P Fomin
Kamil Akanbi
Randall L Duncan
Mary C Farach-Carson
University of Delaware · US

Funding

VALGUS BRACING FOR MEDIAL LAXITY IN PATIENTS WITH OSTEOARTHRITISP20RR016458 · NCRR · UNIVERSITY OF DELAWARE · PI SNYDER-MACKLER, LYNN · 2002 to 2011
$18.9M
PTH REDUCES THE MECHANICAL THRESHOLD IN OSTEOBLASTSR01DK058246 · NIDDK · UNIVERSITY OF DELAWARE · PI DUNCAN, RANDALL L · 2000 to 2009
$2.4M
Mechanotransduction: Puringergic Signaling in BoneR01AR051901 · NIAMS · UNIVERSITY OF DELAWARE · PI DUNCAN, RANDALL L · 2005 to 2009
$1.6M
REGULATION OF CALCIUM CHANNEL EXPRESSION IN OSTEOBLASTSR01DE012641 · NIDCR · UNIVERSITY OF DELAWARE · PI FARACH-CARSON, MARY C · 1999 to 2003
$1.2M
STRETCH CHANNEL FUNCTION IN THE UNLOADED OSTEOBLASTR01AR043222 · NIAMS · UNIVERSITY OF DELAWARE · PI DUNCAN, RANDALL L · 1996 to 2006
$1.2M
NCRR NIH HHS P20 RR-016458NIAMS NIH HHS AR-043222NIAMS NIH HHS AR-051901NIDCR NIH HHS DE-012641NIDDK NIH HHS DK-058246
6 · The paper itself

Abstract

Voltage-sensitive Ca(2+) channels (VSCCs) mediate Ca(2+) permeability in osteoblasts. Association between VSCC alpha(1)- and beta-subunits targets channel complexes to the plasma membrane and modulates function. In mechanosensitive tissues, a 700-kDa ahnak protein anchors VSCCs to the actin cytoskeleton via the beta(2)-subunit of the L-type Ca(v)1.2 (alpha(1C)) VSCC complex. Ca(v)1.2 is the major alpha(1)-subunit in osteoblasts, but the cytoskeletal complex and subunit composition are unknown. Among the four beta-subtypes, the beta(2)-subunit and, to a lesser extent, the beta(3)-subunit coimmunoprecipitated with the Ca(v)1.2 subunit in MC3T3-E1 preosteoblasts. Fluorescence resonance energy transfer revealed a complex between Ca(v)1.2 and beta(2)-subunits and demonstrated their association in the plasma membrane and secretory pathway. Western blot and immunohistochemistry showed ahnak association with the channel complex in the plasma membrane via the beta(2)-subunit. Cytochalasin D exposure disrupted the actin cytoskeleton but did not disassemble or disrupt the function of the complex of L-type VSCC Ca(v)1.2 and beta(2)-subunits and ahnak. Similarly, small interfering RNA knockdown of ahnak did not disrupt the actin cytoskeleton but significantly impaired Ca(2+) influx. Collectively, we showed that Ca(v)1.2 and beta(2)-subunits and ahnak form a stable complex in osteoblastic cells that permits Ca(2+) signaling independently of association with the actin cytoskeleton.

Indexed as

3T3 CellsActin CytoskeletonAnimalsCalciumCalcium Channels, L-TypeCalcium SignalingCell LineCytoskeletonFluorescence Resonance Energy TransferGene Knockdown TechniquesMembrane ProteinsMiceNeoplasm ProteinsOsteoblastsRNA, Small InterferingAhnak protein, mouseCACNA1C protein, mouseCalciumCalcium Channels, L-TypeMembrane ProteinsNeoplasm ProteinsRNA, Small Interfering

Identifiers

PMID19261907
PMCPMC2681378
OpenAlexW1989611419

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.