MolPharm xPharm- The Comprehensive Pharmacology Reference

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by BROSTROM, M. A.
Right arrow Articles by BRECKENRIDGE, B. MCL.
Right arrow Search for Related Content
PubMed
Right arrow Articles by BROSTROM, M. A.
Right arrow Articles by BRECKENRIDGE, B. MCL.

Molecular Pharmacology, Vol 10, 711-720, Copyright © 1974 by the American Society for Pharmacology and Experimental Therapeutics

Adenosine 3',5'-Monophosphate in Glial Tumor Cells Treated with Glucocorticoids

MARGARET A. BROSTROM 1, CHRISTINE KON 1, DOUGLAS R. OLSON 1, and BRUCE MCL. BRECKENRIDGE 1

1 Department of Pharmacology, College of Medicine and Dentistry of New Jersey, Rutgers Medical School, Piscataway, New Jersey 08854

The effect of various steroids on adenosine 3',5'-monophosphate in C-6 glial tumor cell cultures was examined. Glucocorticoids increased basal and norepinephrine-stimulated concentrations of cyclic AMP in intact cells 2-fold. Exposure of cells to 2 µM corticosterone for at least 48 hr was required to obtain a maximal effect. The concentration of norepinephrine needed for half-maximal activation and the time course of the cyclic AMP response were unaltered. A 2-fold increase in adenylate cyclase activity of broken cell preparations similarly dependent upon corticosterone concentration and time was observed. The apparent Km for ATP was not changed but the maximum velocity was doubled, suggesting that the steroid induces the synthesis of additional adenylate cyclase. The activity of a second enzyme localized in the surface membrane, (Na+ + K+)-ATPase, was unaltered in glucocorticoid-treated cells. Also, no differences in the activities of cyclic nucleotide phosphodiesterases were detected.

Submitted on February 25, 1974







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
 Molecular Interventions Drug Metabolism and Disposition

Copyright © 1974 by the American Society for Pharmacology and Experimental Therapeutics