P2Y receptor subtypes differentially couple to inwardly‐rectifying potassium channels

FEBS Letters

Bilbe, G¹  Crespo, J¹  Fakler, B²  Maier, R¹  Mosbacher, J¹  Glatz, A¹ 

[1] Novartis Pharma A.G., CH-4002 Basel, Switzerland;Dept. of Physiology II, University of Tübingen, 72074 Tübingen, Germany

关键词: P2Y;    Purinoceptor;    Pertussis toxin;    G-protein activated Kir;    Xenopus oocyte;    G protein;    GPCR;    G-protein-coupled receptor;    Kir3.0;    G-protein modulated inwardly rectifying potassium channels;    PLC;    phospholipase C;    I Cl(Ca);    Ca2+-dependent Cl−-current;    I Kir;    current mediated by Kir channels;    Gβ/γ;    G-protein β/γ subunit complex;    Gα;    G-protein α subunit;    2MeATP;    2-methylthioadenosine 5′-triphosphate;    mBS;    modified Barth's solution;    NFR;    normal frog Ringer;    KFR;    high-K′ frog Ringer;    I-V;    current-voltage relationship;   

DOI  :  10.1016/S0014-5793(98)01066-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subtypes of P2Y receptors are well characterized with respect to their agonist profile but little is known about differences in their intracellular signalling properties. When expressed in Xenopus oocytes, both P2Y₂ and P2Y₆ receptors effectively couple to endogenous Ca²⁺-dependent Cl⁻-channels. However, only P2Y₂ receptors increased currents mediated by inward-rectifier K⁺ channels of the Kir3.0 subfamily. This incrase in Kir-current was sensitive to pertussis toxin, while activation of Ca²⁺-dependent Cl⁻-channels was not. In contrast, suramin, a P2 receptor antagonist, inhibited activation of both channels. These observations suggest that, in contrast to P2Y₆, P2Y₂ receptors couple to two different classes of G proteins.

【 授权许可】

Unknown