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Biochem Biophys Res Commun ; 168(2): 823-9, 1990 Apr 30.
Article in English | MEDLINE | ID: mdl-1970728

ABSTRACT

The effect of sphingosine, a known selective inhibitor of protein kinase C, on the induction of tyrosine aminotransferase (TAT) and tryptophan oxygenase (TO) by dexamethasone was studied in the primary culture of rat hepatocytes to determine the possible involvement of protein kinase C in the expression of glucocorticoid action. Sphingosine inhibits the induction of TAT by dexamethasone in a concentration- and time-dependent manner in primary culture of rat hepatocytes. It does not inhibit the induction of TAT by Bt2cAMP. Sphingosine inhibits also the induction of TO by dexamethasone in a manner similar to TAT inhibition. It has no effect on the activity of lactate dehydrogenase, a cytosolic marker enzyme and on the protein content of the cultured hepatocytes. These findings indicate that endogenous modulator of protein kinase C, such as sphingosine, may influence the expression of glucocorticoid action in rat hepatocytes.


Subject(s)
Dexamethasone/pharmacology , Liver/enzymology , Sphingosine/pharmacology , Tryptophan Oxygenase/biosynthesis , Tyrosine Transaminase/antagonists & inhibitors , Animals , Bucladesine/pharmacology , Cells, Cultured , Dose-Response Relationship, Drug , L-Lactate Dehydrogenase/metabolism , Protein Kinase C/metabolism , Rats , Time Factors
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