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Vol. 62, Issue 6, 1339-1343, December 2002

Phospholipase D Activation by Endogenous 5-Hydroxytryptamine 2C Receptors Is Mediated by Galpha 13 and Pertussis Toxin-Insensitive Gbeta gamma Subunits

L. McGrew, M. S. S. Chang,1 and E. Sanders-Bush

Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee

Phospholipase D activation was measured in primary cultures of rat choroid plexus epithelial cells, which endogenously express the 5-hydroxytryptamine (5-HT) 2C receptor, as well as a heterologous cell line expressing the cloned receptor. In both systems, serotonin stimulation of the 5-HT2C receptor activates phospholipase D in addition to phospholipase C, the traditional effector. Specific inhibitors and membrane permeable blocking peptides were used to determine which heterotrimeric G-proteins were involved. Results suggest that both alpha  and free beta gamma subunits from G13 heterotrimers are responsible for phospholipase D activation.

1 Current address: Department of Chemistry, University of Florida, Gainesville, FL 32611

Copyright © 2002 by The American Society for Pharmacology and Experimental Therapeutics


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