Thrombin activates pore forming channel protein Orai1 resulting in store operated Ca²⁺ entry (SOCE) with Ca²⁺ dependent release of platelet granules, activation of integrin a_IIbb₃, adhesion, aggregation and thrombus formation. Platelets lack nuclei and are thus unable to modify protein abundance by transcriptional regulation. Nevertheless, they still contain pre-mRNA and mRNA and are thus able to express protein by stimulation of translation. The translation is sensitive to phosphoinositide-3-kinase (PI3K) and actin polymerization. The present study explored whether thrombin modifies Orai1 protein abundance. According to RT-PCR platelets contain pre-mRNA and mRNA encoding Orai1. Activation with thrombin (0.1 U) resulted in a significant decline of pre-mRNA, which was, according to Western blotting and confocal microscopy, paralleled by a marked and statistically significant increase of Orai1 protein abundance. The increase of Orai1 protein abundance was insensitive to inhibition of transcription with actinomycin (4 mg/ml), but was significantly blunted by inhibition of translation with puromycin (100 mM), by inhibition of PI3-K with wortmannin (100 nM), and by depolymerization of the cytoskeleton with cytochalasin D (1 mM). In conclusion, activation of platelets stimulates the expression of Orai, thus augmenting the power of Ca²⁺ signalling.