ATP release due to Thy-1-integrin binding induces P2X7-mediated calcium entry required for focal adhesion formation
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Henríquez, Mauricio
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ATP release due to Thy-1-integrin binding induces P2X7-mediated calcium entry required for focal adhesion formation
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Thy-1, an abundant mammalian glycoprotein, interacts with avβ3 integrin and syndecan-4 in astrocytes and thus triggers signaling events that involve RhoA and its effector p160ROCK, thereby increasing astrocyte adhesion to the extracellular matrix. The signaling cascade includes calcium-dependent activation of protein kinase Cα upstream of Rho; however, what causes the intracellular calcium transients required to promote adhesion remains unclear. Purinergic P2X7 receptors are important for astrocyte function and form large non-selective cation pores upon binding to their ligand, ATP. Thus, we evaluated whether the intracellular calcium required for Thy-1-induced cell adhesion stems from influx mediated by ATP-activated P2X7 receptors. Results show that adhesion induced by the fusion protein Thy-1-Fc was preceded by both ATP release and sustained intracellular calcium elevation. Elimination of extracellular ATP with Apyrase, chelation of extracellular calcium with EGTA, or inhibition of
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URI: https://repositorio.uchile.cl/handle/2250/165213
DOI: 10.1242/jcs.073171
ISSN: 00219533
14779137
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Journal of Cell Science, Volumen 124, Issue 9, 2018, Pages 1581-1588
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