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Open Access research with a European policy impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the European Policies Research Centre (EPRC).

EPRC is a leading institute in Europe for comparative research on public policy, with a particular focus on regional development policies. Spanning 30 European countries, EPRC research programmes have a strong emphasis on applied research and knowledge exchange, including the provision of policy advice to EU institutions and national and sub-national government authorities throughout Europe.

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Mechanisms of phospholipase C activation by the vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide type 2 receptor

MacKenzie, C. and Lutz, E. and Johnson, M.S. and Robertson, D.N. and Holland, P.J. and Mitchell, R. (2001) Mechanisms of phospholipase C activation by the vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide type 2 receptor. Endocrinology, 142 (3). pp. 1209-1217. ISSN 0013-7227

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Abstract

The vasoactive intestinal polypeptide/pituitary adenylate cyclase-activating polypeptide type 2 (VPAC2) receptor was shown to induce both [3H]inositol phosphate ([3H]InsP)and cAMP production in transfected COS7 cells and in GH3 cells where it is natively expressed. Neither cholera toxin nor forskolin could elicit an equivalent [3H]InsP response, suggesting independent coupling of the two pathways. The VPAC2 receptor-mediated [3H]InsP response was partially inhibited by pertussis toxin (Ptx) and by the G{beta}{gamma}-sequestering C-terminal fragment of GRK2 (GRK2-ct) in COS7 and GH3 cells, whereas responses of control receptors were unaffected. Blockers of receptor-activated Ca2+ influx pathways (Co2+ and SKF 96365) also partially inhibited VPAC2 receptor-mediated [3H]InsP responses. This inhibition was not present in the component of the response remaining after Ptx treatment. A range of blockers of voltage-sensitive Ca2+ channels were ineffective, consistent with the reported lack of these channels in COS7 cells. The data suggest that the VPAC2 receptor may couple to phospholipase C through both Ptx-insensitive and Ptx-sensitive G proteins (Gq/11 and Gi/o, respectively) to generate [3H]InsP. In addition to G{beta}{gamma}, Gi/o activation appears to require receptor-activated Ca2+ entry. This is consistent with the possibility that not only G{alpha}q/11-responsive and G{beta}{gamma}-responsive isoforms of phospholipase C but also Ca2+-responsive forms may contribute to the overall [3H]InsP response.