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 Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by DAVIS, C. W.
Right arrow Articles by Daly, J. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DAVIS, C. W.
Right arrow Articles by Daly, J. W.

Molecular Pharmacology, Vol 17, 206-211, Copyright © 1980 by the American Society for Pharmacology and Experimental Therapeutics

Activation of Rat Cerebral Cortical 3',5'-Cyclic Nucleotide Phosphodiesterase Activity by Gangliosides

C. W. DAVIS 1 and J. W. Daly 1

1 Laboratory of Bioorganic Chemistry, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20205

Mixed brain gangliosides stimulated the activity of rat cerebral cortical calcium-dependent and calcium-independent cyclic nucleotide phosphodiesterases in a concentration-dependent manner. The extent of stimulation was similar with both enzymes, but calcium-dependent enzyme was at least 10 times more sensitive to gangliosides. Activation occurred rapidly and was readily reversible. The Vmax of the calcium-dependent enzyme was increased, while the Km was unaffected. Maximal activation of the calcium-dependent enzyme by gangliosides was only 50% of that elicited by lysolecithin or calcium-dependent activator protein. Activation by lysolecithin and gangliosides was apparently additive, while the activation by activator protein was slightly diminished in the presence of gangliosides. Trypsin pretreatment of the calcium-dependent enzyme resulted in a loss of sensitivity to subsequent activation by gangliosides or activator protein without altering the activation by lysolecithin. Potassium ions inhibited basal activity of the calcium-dependent phosphodiesterase but had no effect on enzyme activated by gangliosides, activator protein, or lysolecithin. Phosphodiesterase in the membrane-bound state did not appear to be affected by gangliosides.

Note:
ACKNOWLEDGMENT The authors wish to thank Dr. Cyrus R Creveling, NIAMDD, for electrophoretic analysis of purified calcium-dependent phosphodiesterase.

Submitted on July 2, 1979
Accepted on October 15, 1979




This article has been cited by other articles:


Home page
 GlycobiologyHome page
S. Sonnino, L. Mauri, V. Chigorno, and A. Prinetti
Gangliosides as components of lipid membrane domains
Glycobiology, January 1, 2007; 17(1): 1R - 13R.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
N. Kanda and S. Watanabe
Gangliosides GD1b, GT1b, and GQ1b Enhance IL-2 and IFN-{{gamma}} Production and Suppress IL-4 and IL-5 Production in Phytohemagglutinin-Stimulated Human T Cells
J. Immunol., January 1, 2001; 166(1): 72 - 80.
[Abstract] [Full Text] [PDF]


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

Copyright © 1980 by the American Society for Pharmacology and Experimental Therapeutics