Preprothyrotropin-releasing hormone mRNA in the rat central gray is strongly and persistently induced during morphine withdrawal.

In vivo evidence strongly implicates the central gray in expression of the physical symptoms of opiate withdrawal. Preprothyrotropin-releasing hormone (ppTRH) mRNA is highly expressed in the central gray. Furthermore, systemic administration of thyrotropin-releasing hormone (TRH) inhibits the development of opiate dependence in rats.

Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family.

Ionotropic glutamate receptors are composed of homomeric or heteromeric configurations of glutamate receptor subunits. We have cloned a member of a novel class of the rat ionotropic glutamate receptor family, termed chi-1. This subunit exhibits an average identity of 27% to NMDA subunits and 23% to non-NMDA subunits.

Thermal stability and CD analysis of rat tyrosine hydroxylase.

Tyrosine hydroxylase is the rate-limiting enzyme of catecholamine biosynthesis. It is a homotetramer made up of 56 kDa subunits. We examined the thermal stability of tyrosine hydroxylase purified from a rat pheochromocytoma cell line and investigated the relationship between enzyme activity and stability.

Farnesyl-protein transferase and geranylgeranyl-protein transferase assays using phosphocellulose paper absorption.

Farnesyl-protein transferase catalyzes the reaction of farnesyl pyrophosphate and its acceptors to yield farnesyl protein and pyrophosphate. Geranylgeranyl-protein transferases are distinct enzymes that catalyze the reaction of geranylgeranyl pyrophosphate and their acceptors. We used tritiated isoprenoid pyrophosphate donors and synthetic peptide acceptors to measure enzyme activities.

Inactivation of phosphorylated rat tyrosine hydroxylase by ascorbate in vitro.

Tyrosine hydroxylase activity is reversibly controlled by the actions of several protein kinases. Previous studies showed that, following phosphorylation by protein kinase A, physiological concentrations of ascorbate irreversibly inactivate tyrosine hydroxylase. Several studies were performed to establish the mechanism of inactivation.