Inhibition of mammalian protein kinase and phosphodiesterase activities by a cyclic AMP-like compound isolated from higher plants.
Open Access
- 1 September 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (9) , 4301-4305
- https://doi.org/10.1073/pnas.75.9.4301
Abstract
A cyclic AMP-like substance has been isolated from higher plant tissues which can be quantitated with the use of a radioimmunoassay similar to that described by A. L. Steiner, D. M. Kipnis, R. Utiger, and C. Parker [(1969) Proc. Natl. Acad. Sci. USA 64, 367-373]. This compound has been extensively purified and is chromatographically distinct from authentic cyclic AMP. This cyclic AMP-like compound inhibited beef heart 3':5'-cyclic-nucleotide phosphodietsterase (3':5'-cyclic-nucleotide 5'-nucleotidohydrolase, EC 3.1.4.17), with half-maximal inhibition occurring at a concentration of 7.6 X 10(-10) M cyclic AMP equivalents. The compound also inhibited cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase; EC 2.7.1.37) from bovine heart, with half-maximal inhibition of mixed histone phosphorylation occurring at 8.0 X 10(-11) M cyclic AMP equivalents. Equipotent inhibition of phosphorylation and associated trace ATPase activity were observed with the purified catalytic subunit of cyclic AMP-dependent protein kinase from calf thymus with a synthetic heptapeptide as substrate. Moreover, steady-state kinetic analysis of this inhibition in the latter system showed it to be nonlinear and noncompetitive versus MgATP.This publication has 13 references indexed in Scilit:
- Studies on the mechanism of phosphorylation of synthetic polypeptides by a calf thymus cyclic AMP-dependent protein kinaseProceedings of the National Academy of Sciences, 1977
- Protein PhosphorylationAnnual Review of Biochemistry, 1975
- Rapid protein kinase assay using phosphocellulose-paper absorptionAnalytical Biochemistry, 1975
- A Comparative Study of Cytokinesins I and II and Zeatin Riboside: A Reply to Carlos MillerProceedings of the National Academy of Sciences, 1974
- Interactions of a Photo-Affinity ATP Analog with Cation-Stimulated Adenosine Triphosphatases of Human Red Cell MembranesProceedings of the National Academy of Sciences, 1974
- Cyclic adenosine 3',5'-monophosphate and morphogenesis in Mucor racemosus.1974
- 8-Bromoadenosine 3′:5′-Cyclic Monophosphate as a Promoter of Cell Division in Excised Tobacco Pith Parenchyma TissueProceedings of the National Academy of Sciences, 1973
- The Inhibition of Plant and Animal Adenosine 3′:5′-Cyclic Monophosphate Phosphodiesterases by a Cell-Division-Promoting Substance from Tissues of Higher Plant SpeciesProceedings of the National Academy of Sciences, 1972
- CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASES, IV. WIDESPREAD OCCURRENCE OF ADENOSINE 3′,5′-MONOPHOSPHATE-DEPENDENT PROTEIN KINASE IN VARIOUS TISSUES AND PHYLA OF THE ANIMAL KINGDOMProceedings of the National Academy of Sciences, 1969
- RADIOIMMUNOASSAY FOR THE MEASUREMENT OF ADENOSINE 3′,5′-CYCLIC PHOSPHATEProceedings of the National Academy of Sciences, 1969