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• W2029751479 abstract "Proteinase-activated receptors 1 and 4 (PAR₁ and PAR₄) are the major receptors mediating thrombin-induced NO production in endothelial cells. The intracellular signaling following their activation still remains to be elucidated. The present study provides the first evidence for the distinct Ca²⁺ requirement for the NO production between PAR₁ and PAR₄. The activation of PAR₁ by the activating peptide (PAR₁-AP) elevated cytosolic Ca²⁺ concentrations ([Ca²⁺]_i) and activated NO production in porcine aortic and human umbilical vein endothelial cells, whereas it had little effect on bovine aortic endothelial cells. PAR₄ activation by PAR₄-AP consistently induced NO production without an appreciable [Ca²⁺]_i elevation in three types of endothelial cells. The PAR₁-mediated NO production was significantly inhibited by 1,2-bis(2-aminophenoxy)ethane-<i>N</i>,<i>N</i>,<i>N</i>′,<i>N</i>′-tetraacetic acid (BAPTA), whereas the PAR₄-mediated NO production was resistant. NO production following the PAR₁ and PAR₄ activation was significantly inhibited by pertussis toxin, but it was resistant to a Gα_q/11 inhibitor, YM254890 [(1<i>R</i>)-1-{(3<i>S</i>,6<i>S</i>,9<i>S</i>,12<i>S</i>,18<i>R</i>,21<i>S</i>,22<i>R</i>)-21-acetamido-18-benzyl-3-[(1<i>R</i>)-1-methoxyethyl]-4,9,10,12,16,22-hexamethyl-15-methylene-2,5,8,11,14,17,20-heptaoxo-1,19-dioxa-4,7,10,13,16-pentaazacyclodocosan-6-yl}-2-methylpropyl rel-(2<i>S</i>,3<i>R</i>)-2-acetamido-3-hydroxy-4-methylpentanoate]. However, YM254890 abrogated the PAR₁-mediated Ca²⁺ signal. PAR₄-mediated NO production was substantially inhibited by the inhibitors of phosphotidylinositol-3 kinase (PI3K) and Akt, as well as by the dominant negative mutant of Akt. The PAR₁-mediated NO production was relatively resistant to inhibitors of PI3K. An immunoblot analysis revealed a transient increase in the phosphorylation of Akt and endothelial NO synthase following the PAR₄ stimulation. In conclusion, PAR₁ and PAR₄ engage distinct signal transduction mechanisms to activate NO production in vascular endothelial cells. PAR₄ preferably activates Gα_i/o and induced NO production in a manner mostly independent of Ca²⁺ but dependent on the PI3K/Akt pathway, whereas PAR₁ activates both the Ca²⁺-dependent and -independent mechanisms." @default.
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• W2029751479 date "2007-05-09" @default.
• W2029751479 modified "2023-10-10" @default.
• W2029751479 title "Distinct Ca²⁺ Requirement for NO Production between Proteinase-Activated Receptor 1 and 4 (PAR₁ and PAR₄) in Vascular Endothelial Cells" @default.
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• W2029751479 doi "https://doi.org/10.1124/jpet.107.121038" @default.
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