Biopolym. Cell. 1997; 13(2):116-120.
http://dx.doi.org/10.7124/bc.000472
Structure and Function of Biopolymers
Identification of Ca2+ and calmoduline sensitive cAMP phosphodiesterase (PDE) and its possible role in the interaction of adenylate cyclase system with phytohormones
1Dragovoz I. V., 1Javorska V. K., 1Melnichuk Yu. P.
  1. Institute of Plant Physiology and Genetics, NAS of Ukraine
    31/17, Vasylkivska, Kyiv, Ukraine, 03022

Abstract

cAMP PDE sensitive to methylxanthine, Ca2+ ions and calmoduline and similar to animal PDE has been identificated in 2 days old rye seedlings (Secale cereate). The regulatory effect of cytokinins and abscisic acid on rye PDE has been shown in vitro. The conclusion is made on the possible role of cAMP metabolism enzyme in the interrelation of adenylate cyclase system with phytohormones.
Full text: (PDF, in Russian)

References

[1] Itkes AV, Tunitskaya VL, Severin ES. Regulation of the biological activity of a cell second messenger systems: cAMP, 2, 5'-oligoadenylate and calcium. Usp biol khim. 1985; 26: 125-52.
[2] Severin ES, Kochetkova YaM. The phosphorylation role in the regulation of cellular activity. M.: Nauka, 1985. 287 p.
[3] Ranjeva R, Boudet AM. Phosphorylation of Proteins in Plants: Regulatory Effects and Potential Involvement in Stimulus/Response Coupling. Annu Rev Plant Physiol. 1987;38(1):73–94.
[4] Newton RP, Brown EG. The biochemistry and physiology of cyclic AMP in higher plants. Hormones, receptors and cellular interaction in plants. Ed. C. M. Chadvik, D. R. Garrod. Cambridg, 1986: 115-153.
[5] Grigorovitch YuA. Calmodulin-Ca2 + -dependent activator protein and other PDE enzyme systems. Usp biol khim. 1982; 22:76-99.
[6] Ivanov GG, Vyskrebentseva EI. Isolation and partial characterization of cAMP-phosphodiesterase and its Ca-dependent protein activator from sugar-beet root. Fiziologiia rasteniy. 1986;33(1):5-9.
[7] Yavorska VK, Dragovoz IV et al. Identification of cAMP phosphodiesterase, sensitive to calcium ions and calmodulin, and its possible role in the malignant transformation of plant cells. Fiziologiya i biokhimiya kul'turnykh rasteniy. 1994; 26: 136-41.
[8] Guliev NM, Fedenko EP, Doman NG. [cAMP phosphodiesterase from phototrophic bacteria Rhodospirillum rubrum]. Biokhimiia. 1976;41(11):2043-6.
[9] Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193(1):265-75.
[10] Dupon M, Onckelen HA, Greef JA. Characterization of cyclic nucleotide phosphodiesterase activity in Phaseolus vulgaris. Physiol Plant. 1987;69(2):361–5.
[11] Etingof RN, Dumler IL. [Phosphodiesterase of cyclic nucleotides]. Ukr Biokhim Zh. 1981;53(2):28-43.
[12] Fedenko EP, Doman NG, Yavorskaya VK, Poiser E. Characteristics of two factions of cyclic AMP phosphodiesterase from maize seedlings and their relationship with calmodulin. Fiziologiia rasteniy. 1988; 35(1):98-105.
[13] Page A. A non-linear regression program in BASIC for estimating K m and V max . Bioinformatics. 1987;3(1):49–51.
[14] Dieter P. Calmodulin and calmodulin-mediated processes in plants. Plant Cell Environ.1984;7(6):371–80.
[15] Van Staden J, Boss? CA. Cytokinins in cut carnation flowers. VI. The transport and metabolism of zeatin and dihydrozeatin. J Plant Physiol. 1989;135(2):160–3.
[16] Chiatante D, Portello C, Levi M, Sgorbati S, Sparvoli E. Inhibition by cytokinins of the activity of a multifunctional phosphodiesterase purified from cotyledons of lactuca sativa. Plant Physiol Biochem. 1988; 26(3): 297-301.
[17] Chiatante D, Newton RP, Crignola S, Levi M, Brown EG. The 3?,5?-cyclic nucleotide phosphodiesterases of meristematic and differentiated tissues of pea roots. Phytochemistry. 1990;29(9):2815–20.
[18] Brown EG, Al-Najafi T, Newton RP. Cyclic nucleotide phosphodiesterase activity in Phaseolus vulgaris. Phytochemistry. 1977;16(9):1333–7.