Paxillin is an intrinsic negative regulator of platelet activation in mice View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-01-02

AUTHORS

Asuka Sakata, Tsukasa Ohmori, Satoshi Nishimura, Hidenori Suzuki, Seiji Madoiwa, Jun Mimuro, Kazuomi Kario, Yoichi Sakata

ABSTRACT

BackgroundPaxillin is a LIM domain protein localized at integrin-mediated focal adhesions. Although paxillin is thought to modulate the functions of integrins, little is known about the contribution of paxillin to signaling pathways in platelets. Here, we studied the role of paxillin in platelet activation in vitro and in vivo.Methods and resultsWe generated paxillin knockdown (Pxn-KD) platelets in mice by transplanting bone marrow cells transduced with a lentiviral vector carrying a short hairpin RNA sequence, and confirmed that paxillin expression was significantly reduced in platelets derived from the transduced cells. Pxn-KD platelets showed a slight increased in size and augmented integrin αIIbβ3 activation following stimulation of multiple receptors including glycoprotein VI and G protein-coupled receptors. Thromboxane A2 biosynthesis and the release of α-granules and dense granules in response to agonist stimulation were also enhanced in Pxn-KD platelets. However, Pxn-KD did not increase tyrosine phosphorylation or intracellular calcium mobilization. Intravital imaging confirmed that Pxn-KD enhanced thrombus formation in vivo.ConclusionsOur findings suggest that paxillin negatively regulates several common platelet signaling pathways, resulting in the activation of integrin αIIbβ3 and release reactions. More... »

PAGES

1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1477-9560-12-1

DOI

http://dx.doi.org/10.1186/1477-9560-12-1

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https://app.dimensions.ai/details/publication/pub.1000194248

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24383745


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