Adenosine 3':5'-cyclic monophosphate-dependence of protein kinase isoenzymes from mouse liver

Ueland, Per Magne; Døskeland, Stein Ove

doi:10.1042/bj1570117

Cited by 27 publications

(1 citation statement)

References 21 publications

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“…Partially purified protein kinase inhibitor was prepared by a modification (Ueland & Doskeland, 1976) of the procedure of Walsh et al (1971).…”

Section: Preparation Of Rf With C[3h]amp Preferentially Boundmentioning

confidence: 99%

Release of [3H]adenosine cyclic 3',5'-phosphate bound to the regulatory moiety of protein kinase I in the presence of magnesium(2+), ATP and the catalytic subunit of the kinase

Øgreid¹,

Døskeland²

1983

Biochemistry

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The rate of release of bound c[3H]AMP from the two types (A and B) of cAMP binding sites on the regulatory subunit dimer (R2I) of rabbit muscle protein kinase I was studied in the presence of the catalytic (C) subunit of protein kinase. Rebinding of released c[3H]AMP was avoided by using highly diluted reactants or adding unlabeled cAMP or its analogues. No significant C-induced dissociation of R2I-(c[3H]AMP)4 occurred in the absence of Mg2+-ATP. Of the two options that one or two molecules of C are required to induce the release of c[3H]AMP bound to R2I, only the first one was compatible with the first-order dependence on [C] of the rate of release of c[3H]AMP observed over a wide range of C concentrations. In the absence of added unlabeled cyclic nucleotide, the rate of the C-induced release of c[3H]AMP was the same from site A and site B. The apparent second-order rate constant for the association of C to R2I(c[3H]AMP)4 was 6 X 10(6) M-1 s-1 (37 degrees C, 0.15 M KCl). Raising the concentration of unlabeled cAMP in the medium up to 1 microM decreased by up to 50% the rate of the C-induced release of bound c[3H]AMP from both sites. This is explained by assuming that the association of one molecule of C to R2I(c-[3H]AMP)4 leads to the release of c[3H]AMP first from one R subunit and subsequently, by a process that can be blocked by about 1 microM cAMP, from the other R subunit. A further rise of the cAMP concentration decreased the rate of release from site B only, so that the C-induced release of c[3H]AMP occurred almost exclusively from site A at very high concentrations of cAMP. This suggests that c[3H]AMP is released first from site A and that this vacant site by interacting with cAMP inhibits the release of c[3H]AMP from site B of the same R subunit. The role of site A in controlling the C-induced release was further supported by the finding that several cAMP analogues inhibited the release with potencies correlating with their affinities for site A. The C-induced release of c[3H]AMP from aged R2I was about 10 times slower than that from fresh R2I. No significant C-induced release of c[3H]AMP was observed from the monomeric fragment obtained by limited trypsin treatment of R2(1).

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“…Partially purified protein kinase inhibitor was prepared by a modification (Ueland & Doskeland, 1976) of the procedure of Walsh et al (1971).…”

Section: Preparation Of Rf With C[3h]amp Preferentially Boundmentioning

confidence: 99%

Release of [3H]adenosine cyclic 3',5'-phosphate bound to the regulatory moiety of protein kinase I in the presence of magnesium(2+), ATP and the catalytic subunit of the kinase

Øgreid¹,

Døskeland²

1983

Biochemistry

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Protein kinase A activity is associated with metacyclogenesis in Leishmania amazonensis

Genestra

Cysne-Finkelstein

Leon

2004

Cell Biochemistry & Function

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Because of the importance of cell signalling processes in proliferation and differentiation, the adenylate cyclase pathway was studied, specifically the protein kinase A (PKA) in Leishmania amazonensis. The PKAs of soluble (SF) and enriched membrane fractions (MF) from infective/non-infective promastigotes and axenic amastigotes were assayed. In order to purify the PKA molecule, fractions were chromatographed on DEAE-cellulose columns and the phosphorylative activity was evaluated using [gamma(32)P]-ATP as the phosphate source. These experiments were performed in the presence of cyclic adenosine monophosphate (cAMP) and an inhibitor of PKA. Our data demonstrated that the PKA activity was significantly higher (about two times) in SF from promastigotes with a high concentration of metacyclic forms, when compared with the non-infective promastigotes, suggesting an association of this activity and the metacyclogenesis process. A discrete phosphorylative activity in axenic amastigotes was observed. As the adenylate cyclase/cAMP pathway would be involved in the parasite-host interiorization, the PKA activity may constitute a good intracellular target for studies of leishmanicidal drugs.

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Properties of the cyclic AMP-dependent protein kinases in mouse mastocytoma cells

Smart

Ralph

1983

Mol Cell Biochem

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The properties of type I and type II protein kinases in PY815 mouse mastocytoma cells were shown to change following growth inhibition by prostaglandin E1 and 3-isobutyl-1-methylxanthine. These changes included a large reduction in type I protein kinase consistent with a role for this isoenzyme as a positive effector of growth, a decrease in free cyclic AMP binding protein and an increase in type II protein kinase. Some properties of the fully activated isoenzymes are presented that may be important in determining their activity in vivo.

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Adenosine 3':5'-cyclic monophosphate-dependence of protein kinase isoenzymes from mouse liver

Cited by 27 publications

References 21 publications

Release of [3H]adenosine cyclic 3',5'-phosphate bound to the regulatory moiety of protein kinase I in the presence of magnesium(2+), ATP and the catalytic subunit of the kinase

Release of [3H]adenosine cyclic 3',5'-phosphate bound to the regulatory moiety of protein kinase I in the presence of magnesium(2+), ATP and the catalytic subunit of the kinase

Protein kinase A activity is associated with metacyclogenesis in Leishmania amazonensis

Properties of the cyclic AMP-dependent protein kinases in mouse mastocytoma cells

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