FEBS Letters | |
Glucagon‐like peptide‐1 receptor expression in Xenopus oocytes stimulates inositol trisphosphate‐dependent intracellular Ca2+ mobilization | |
Gromada, Jesper1  Anker, Charlotte2  Wahl, Philip2  Bokvist, Krister1  Knudsen, Lotte B2  | |
[1] Department of Islet Cell Physiology, Novo Nordisk A/S, Symbion, Fruebjergvej 3, DK-2100 Copenhagen, Denmark;Department of Molecular Pharmacology, Novo Nordisk A/S, Copenhagen, Denmark | |
关键词: Glucagon-like peptide-1; Calcium; Inositol trisphosphate; Xenopus oocyte; Cyclic adenosine monophosphate; [Ca2+]i; intracellular free Ca2+ concentration; GLP-1; glucagon-like peptide-1; GLP-1(7–36)amide; glucagon-like peptide-1(7–36)amide; Ins(1; 4; 5)P3; inositol 1; 4; 5-trisphosphate; PKA; protein kinase A; PACAP; pituitary adenylate cyclase-activating polypeptide; PLC; phospholipase C; VIP; vasoactive intestinal peptide; | |
DOI : 10.1016/S0014-5793(98)00254-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The signal transduction pathway of the cloned human glucagon-like peptide-1 (GLP-1) receptor was studied in voltage-clamped Xenopus oocytes. Binding of GLP-1(7–36)amide was associated with cAMP production, increased [Ca2+]i and activation of Ca2+-dependent Cl− current. The effect of GLP-1(7–36)amide reflects intracellular Ca2+ mobilization and was suppressed by injection of the Ca2+ chelator BAPTA and the inositol trisphosphate receptor antagonist heparin. The responses were not mimicked by the adenylate cyclase activator forskolin and unaffected by the protein kinase A (PKA) inhibitor Rp-cAMPS. We conclude that GLP-1 receptor expression in Xenopus oocytes evokes inositol trisphosphate-dependent intracellular Ca2+ mobilization independent of the cAMP/PKA signaling pathway.
【 授权许可】
Unknown
【 预 览 】
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