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Science 3 March 1972:
Vol. 175. no. 4025, pp. 1014 - 1015
DOI: 10.1126/science.175.4025.1014
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Articles

Phosphodiesterase in Dictyostelium discoideum and the Chemotactic Response to Cyclic Adenosine Monophosphate

R. G. Pannbacker 1 and L. J. Bravard 1

1 Charles F. Kettering Research Laboratory, Yellow Springs, Ohio 34587

A phosphodiesterase with a low Michaelis constant for cyclic adenosine monophosphate was found in the membrane fraction of the cellular slime mold. This activity was highest during the aggregation stage. Enzyme with similar properties was also secreted by the cells. Dithiothreitol inhibited both enzymes and potentiated the cellular response to cyclic adenosine monophosphate.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Characterization of a cAMP-stimulated cAMP Phosphodiesterase in Dictyostelium discoideum.
M. E. Meima, K. E. Weening, and P. Schaap (2003)
J. Biol. Chem. 278, 14356-14362
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The regulation of chemotaxis and chemokinesis in Dictyostelium amoebae by temporal signals and spatial gradients of cyclic AMP.
M. Vicker (1994)
J. Cell Sci. 107, 659-667
   Abstract »    PDF »
Cyclic Nucleotide Phosphodiesterase in Dictyostelium discoideum: Interconversion of Two Enzyme Forms.
B. M. Chassy (1972)
Science 175, 1016-1018
   Abstract »    PDF »


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