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• W2051227696 abstract "Pertussis toxin ADP ribosylates G_i and G_o transducing proteins and functionally uncouples adenosine A₁ receptor (A₁AR) from its effectors. We hypothesized that this loss in receptor coupling could lead to de novo A₁AR synthesis by the cell in a futile attempt to re-establish normal receptor function. To test this hypothesis, we used hamster ductus deferens tumor (DDT₁ MF-2) cells, a cell culture model for studying A₁AR, and showed that pertussis toxin (100 ng/ml) produced a time-dependent loss in A₁AR-G_i interaction and abolished A₁AR activation of extracellular signal-regulated kinase 1/2. Interestingly, pertussis toxin increased the expression of A₁AR, as measured by real-time polymerase chain reaction, immunocytochemistry, and [³H]cyclopentyl-1,3-dipropylxanthine (DPCPX) binding, suggesting a compensatory response to G_i protein inactivation. DDT₁ MF-2 cells exposed to pertussis toxin demonstrated nuclear factor κB (NF-κB) activation within 30 min of exposure, a time point that preceded the loss of function of the A₁AR. Inhibition of NF-κB attenuated the increase in A₁AR induced by pertussis toxin. Cells exposed to B-oligomer subunit of pertussis toxin, devoid of significant ADP ribosyltransferase activity, showed increased A₁AR protein expression, preceded by activation of NF-κB. B-Oligomer increased intracellular Ca²⁺ in DDT₁ MF-2 cells. Chelation of intracellular Ca²⁺ with 1,2-bis(2-aminophenoxy)ethane-<i>N</i>,<i>N</i>,<i>N</i>′,<i>N</i>′-tetraacetic acid or inhibition of protein kinase C (PKC) with bisindolylmaleimide hydrochloride reduced the activation of NF-κB and [³H]DPCPX binding. We conclude that pertussis toxin promotes de novo A₁AR synthesis by activating NF-κB through an ADP ribosylation-independent mechanism involving intracellular Ca²⁺ release and PKC activation." @default.
• W2051227696 created "2016-06-24" @default.
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• W2051227696 date "2005-12-01" @default.
• W2051227696 modified "2023-09-26" @default.
• W2051227696 title "Induction of Adenosine A₁Receptor Expression by Pertussis Toxin via an Adenosine 5′-Diphosphate Ribosylation-Independent Pathway" @default.
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• W2051227696 doi "https://doi.org/10.1124/jpet.105.096255" @default.
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