Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P21554 (cannabinoid receptor)
 3,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Brain-type cannabinoid receptor (CB1) mRNA has been demonstrated in several peripheral tissues; however, the function of this message is not clear. In the present study, we examined the levels of CB1 mRNA and receptor protein in stimulated immune cells to link message and protein expression with cell activation. Consistent with previous reports, immune cell lines from human and mouse were positive by reverse transcription-polymerase chain reaction for CB1 mRNA; however, one cell line, Jurkat, was only weakly positive. Mitogen activation of Jurkat cells, however, increased CB1 mRNA within 2 hr after stimulation and equilibrium binding studies, using Jurkat membranes, showed [3H]CP55,940 specific binding was negative early after mitogen stimulation but positive at 40 hr poststimulation. To investigate whether this observed increase in CB1 mRNA and specific binding activity was associated with expression of the CB1 protein, polyclonal antibodies were produced to a fusion protein consisting of glutathione S-transferase and a 342 amino acid portion (residues 33 through 374) of the CB1 protein. Western blotting analysis showed expression of several immunoreactive proteins on membranes from mitogen-activated Jurkat cells, but not on membranes from unstimulated cells. These results demonstrate a link between the level of CB1 mRNA and surface protein in activated immune cells, suggesting the possibility of a functional role of CB1 in immune cell activation.
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PMID:Cannabinoid receptor proteins are increased in Jurkat, human T-cell line after mitogen activation. 863 50

MRL-1, a cannabinoid receptor-1 inverse agonist, was a member of a lead candidate series for the treatment of obesity. In rats, MRL-1 is eliminated mainly via metabolism, followed by excretion of the metabolites into bile. The major metabolite M1, a glutathione conjugate of MRL-1, was isolated and characterized by liquid chromatography/mass spectrometry and NMR spectroscopic methods. The data suggest that the t-butylsulfonyl group at C-2 of furopyridine was displaced by the glutathionyl group. In vitro experiments using rat and monkey liver microsomes in the presence of reduced glutathione (GSH) showed that the formation of M1 was independent of NADPH and molecular oxygen, suggesting that this reaction was not mediated by an oxidative reaction and a glutathione S-transferase (GST) was likely involved in catalyzing this reaction. Furthermore, a rat hepatic GST was capable of catalyzing the conversion of MRL-1 to M1 in the presence of GSH. When a close analog of MRL-1, a p-chlorobenzenesulfonyl furopyridine derivative (MRL-2), was incubated with rat liver microsomes in the presence of GSH, p-chlorobenzene sulfinic acid (M2) was also identified as a product in addition to the expected M1. Based on these data, a mechanism is proposed involving direct nucleophilic addition of GSH to sulfonylfuropyridine, resulting in an unstable adduct that spontaneously decomposes to form M1 and M2.
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PMID:Glutathione S-transferase catalyzed desulfonylation of a sulfonylfuropyridine. 1979 5