Use of adenoviruses to study isoform specificity of G-protein-receptor-coupled Ca2+ signaling in intact epithelial cells

Cell Biochemistry and Biophysics - Tập 36 - Trang 221-233 - 2002
Philip Poronnik1,2, Michelle M. Cummins1, Lauren M. O'Mullane1, David I. Cook1
1Department of Physiology (F13), University of Sydney, Syndney, Australia
2Department of Molecular Medicine, Kolling Institute, University of Sydney and Royal North Shore Hospital, St Leonards, Australia

Tóm tắt

It is firmly established that the activation of many heptahelical receptors by extracellular agonists leads to the activation of effectors such as phospholipase Cβ (PLCβ), the subsequent production of inositol-1,4,5-trisphosphate (IP3), and a resultant increase in intracellular free Ca2+. Heterotrimeric G-proteins have a critical role in transducing the signal from the hepthalelical receptor to PLCβ and in determining the specificity and duration of the cellular responses. There remain, however, a number of areas of uncertainty regarding the exact mechanisms involved in regulating G-protein-mediated receptor-effector coupling in different cell types. For example, the molecular identity of the G-protein involved and the degree of isoform specificity among G-proteins of the same family and their receptors remains unclear. It is also not known in many cell types whether it is the α-or the βλ-subunits of these G-proteins that activate PLCβ. In order to address these issues, we have used replication-deficient adenoviruses as a tool to deliver, into intact epithelial cells, transgenes coding for proteins involved in G-protein-couplied receptor signaling pathways.

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Cell Biochemistry and Biophysics

Tập 36

221-233

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