Evidence map›Paper›PMID 16219803›Full record

ArticleBlood2006

Regulation of LIM-kinase 1 and cofilin in thrombin-stimulated platelets.

Dharmendra Pandey, Pankaj Goyal, James R Bamburg, Wolfgang Siess

Open access · hybridAbstract read
In one paragraph

Article in Blood, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

32 citing papers in PubMed, 62 citations in OpenAlex.

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  19. Article
  20. Rho GTPases in platelet function.Journal of thrombosis and haemostasis : JTH · 2013
    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.

Dharmendra PandeyInstitute for Prevention of Cardiovascular Diseases, University of Munich, Germany.
Pankaj Goyal
James R Bamburg
Wolfgang Siess
Colorado State University · US

Funding

ADF/cofilin-actin rods in neurodegenerative diseasesR01NS040371 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BAMBURG, JAMES R · 2002 to 2009
$2.3M
STRUCTURE/FUNCTION OF ACTIN DEPOLYMERIZING FACTORR01GM035126 · NIGMS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BAMBURG, JAMES R · 1985 to 2003
$1.1M
NIGMS NIH HHS GM35126NINDS NIH HHS NS40371
6 · The paper itself

Abstract

Cofilin is a regulator of actin filament dynamics. We studied whether during platelet activation Rho kinase stimulates LIM kinase (LIMK) leading to subsequent phosphorylation and inactivation of cofilin. Platelet shape change and aggregation/secretion were induced by low and high concentrations of thrombin, respectively. We found that during these platelet responses Rho kinase activation was responsible for mediating rapid Thr508 phosphorylation and activation of LIMK-1 and for the F-actin increase during shape change and, in part, during secretion. Surprisingly, during shape change cofilin phosphorylation was unaltered, and during aggregation/secretion cofilin was first rapidly dephosphorylated by an okadaic acid-insensitive phosphatase and then slowly rephosphorylated by LIMK-1. LIMK-1 phosphorylation and cofilin dephosphorylation and rephosphorylation during aggregation were independent of integrin alpha(IIb)beta(3) engagement. Cofilin phosphorylation did not regulate cofilin association with F-actin and was unrelated to the F-actin increase in thrombin-activated platelets. Our study identifies LIMK-1 as being activated by Rho kinase in thrombin-stimulated platelets. Two counteracting pathways, a cofilin phosphatase and LIMK-1, are activated during platelet aggregation/secretion regulating cofilin phosphorylation sequentially and independently of integrin alpha(IIb)beta(3) engagement. Rho kinase-mediated F-actin increase during platelet shape change and secretion involves a mechanism other than LIMK-1-mediated cofilin phosphorylation, raising the possibility of another LIMK substrate regulating platelet actin assembly.

Indexed as

Gene Expression RegulationPlatelet ActivationActin Depolymerizing FactorsActinsAdenosine TriphosphateEnzyme ActivationGreen Fluorescent ProteinsHemostaticsHumansLim KinasesPhosphoprotein PhosphatasesPlatelet AggregationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein Kinasesrho GTP-Binding ProteinsThreonineActin Depolymerizing FactorsActinsAdenosine Triphosphateenhanced green fluorescent proteinGreen Fluorescent ProteinsHemostaticsLIMK1 protein, humanLim KinasesPhosphoprotein PhosphatasesPlatelet Glycoprotein GPIIb-IIIa ComplexProtein Kinasesrho GTP-Binding ProteinsThreonineThrombin

Identifiers

PMID16219803
PMCPMC1895613
OpenAlexW1965424067

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.