Abstract
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-HT(2C) 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 betagamma subunits from G(13) heterotrimers are responsible for phospholipase D activation.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
3T3 Cells
-
Animals
-
DNA-Binding Proteins / metabolism*
-
Enzyme Activation
-
GTP-Binding Protein alpha Subunits, G12-G13
-
Mice
-
Pertussis Toxin / pharmacology
-
Phospholipase D / metabolism*
-
Protein Subunits / drug effects
-
Rats
-
Rats, Sprague-Dawley
-
Receptor, Serotonin, 5-HT2C
-
Receptors, Serotonin / metabolism*
-
Serotonin / chemistry
-
Serotonin / metabolism
-
Signal Transduction / physiology*
-
Type C Phospholipases
-
rho GTP-Binding Proteins / metabolism
Substances
-
DNA-Binding Proteins
-
Protein Subunits
-
Receptor, Serotonin, 5-HT2C
-
Receptors, Serotonin
-
Serotonin
-
Pertussis Toxin
-
Type C Phospholipases
-
Phospholipase D
-
GTP-Binding Protein alpha Subunits, G12-G13
-
rho GTP-Binding Proteins