Point-mutated p21ras couples a muscarinic receptor to calcium channels and polyphosphoinositide hydrolysis.

Abstract

A high-affinity muscarinic receptor is detectable both in normal 3T3 mouse fibroblasts and in their transformed counterpart obtained by transfection with the oncogene EJ/T24-H-ras. However, only the transformed cell line is responsive to muscarinic agonist carbamylcholine in terms of Ca2+ influx and polyphosphoinositide hydrolysis, whereas the normal cell line is unresponsive. Using a point-mutated p21ras protein and monoclonal antibodies anti-p21ras, we provide evidences that p21ras couples to receptor-operating calcium channels and to polyphosphoinositide hydrolysis a muscarinic receptor which is uncoupled in normal mouse fibroblasts.

Cite this paper

@article{Chiarugi1986PointmutatedPC, title={Point-mutated p21ras couples a muscarinic receptor to calcium channels and polyphosphoinositide hydrolysis.}, author={Vincenzo P. Chiarugi and Franca Pasquali and Simonetta Vannucchi and Marco Ruggiero}, journal={Biochemical and biophysical research communications}, year={1986}, volume={141 2}, pages={591-9} }