Cyclic Nucleotides and Changes in Protein Kinase Activity Ratio in the Ischemic and Nonischemic Myocardium

1983 ◽  
pp. 521-530
Author(s):  
E.-G. Krause ◽  
S. Bartel ◽  
P. Karczewski ◽  
K.-F. Lindenau
Keyword(s):  
Protein Kinase ◽  
Cyclic Nucleotides ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Protein Kinase Activity

Involvement of cAMP-dependent protein kinase in the regulation of heart contractile force. II

1979 ◽  
Vol 236 (1) ◽  
pp. H84-H91
Author(s):  
S. L. Keely ◽  
A. Eiring
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Contractile Force ◽  
Protein Kinase Activity ◽  
Phosphorylase Activity ◽  
Dependent Protein Kinase ◽  
Guinea Pig Heart ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

The effects of histamine on heart cAMP-dependent protein kinase activity, cAMP levels, phosphorylase activity, and contractile force was investigated in the perfused guinea pig heart. To accurately determine the protein kinase activity ratio in guinea pig heart, it was necessary to measure kinase activity in whole homogenates immediately after homogenization of the tissue. Histamine produced a rapid dose-dependent increase in cAMP and the protein kinase activity ratio followed by increased in contractile force and phosphorylase activity. There was a good correlation between the degree of protein kinase activation and the increase in phosphorylase and force. The beta-adrenergic blocking agent propranolol did not reduce the effects of histamine, but metiamide, a potent H2-receptor antagonist, greatly attenuated all the effects of histamine. The data support the hypothesis that increases in heart cAMP-dependent protein kinase activity produce corresponding increases in contractile force and phosphorylase activity.

scholarly journals Ovarian adenosine 3′:5′-cyclic monophosphate-dependent protein kinase(s). Regulation by choriogonadotropin and lutropin in rat ovarian cells

1976 ◽  
Vol 158 (2) ◽  
pp. 175-182 ◽  
Author(s):  
M R Clark ◽  
S Azhar ◽  
K M J Menon
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Gel Filtration ◽  
Supernatant Fraction ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Ovarian Cells ◽  
Dependent Protein

Choriogonadotropin and lutropin have been found to activate cyclic AMP-dependent protein kinase in ovarian cells isolated by collagenase dispersion from immature rats. The stimulatory effect of gonadotropins was dependent on both hormone concentration and incubation time. Choriogonadotropin at 1 mug/ml fully stimulated the protein kinase activity within 5 min of incubation, and this effect was specific for choriogonadotropin and lutropin-like activity. In addition, protein kinase activity has been characterized with respect to salt sensitivity, cyclic AMP binding, and its responsiveness to gonadotropins and other peptide hormones. Ovarian protein kinase was susceptible to high salt concentrations. The addition of 0.3-1.0 M-NaCl in incubation medium increased the activity ratio with a concomitant decrease in cycle AMP-dependence. The salt effect on protein kinase was observed both from hormone-treated and untreated cells. The hormone-stimulated and unstimulated protein kinase activity was completely stable in the absence of NaCl. No change in the activity ratio was observed when cellular extracts were assayed for protein kinase activity either immediately or after 2 h in the absence of added salt. Gel filtration in the absence of NaCl of cellular extracts prepared from choriogonadotropin-treated and untreated cells showned only a single peak of protein kinase activity that was sensitive to exogenously added cyclic AMP. By contrast, when 0.5 M-NaCl was included in the column buffer, the chromatography of untreated extract showed two peaks of protein kinase activity. The first peak was sensitive to added cyclic AMP, whereas the second peak was insensitive to it. Under identical experimental conditions, protein kinase from gonadotropin-treated cells showed, on gel filtration, only one peak of activity that was totally insensitive to added cyclic AMP. DEAE-cellulose column chromatography of a 20000 g supernatant fraction resulted in a peak of kinase activity that eluted in approx. 0.15 M-NaCl, similar to the similar to the elution of type II protein kinases as described by Corbin et al. (1975) (J. Biol. Chem. 250, 218-225). Choriogonadotropin stimulation produced a decrease in the capacity of protein kinase to bind exogenous cyclic [3H]AMP, with a concomitant increase in the kinase activity ratio. These results are consistent with the notion that cyclic AMP, GENERATED IN SITU Under hormonal stimulation, binds tot he regulatory subunit of protein kinase with subsequent dissociation of the active catalytic subunit from the holoenzyme.

The effect of methacholine and histamine on cyclic AMP-dependent protein kinase activity in the guinea-pig isolated trachea

1992 ◽  
Vol 70 (3) ◽  
pp. 344-348 ◽  
Author(s):  
J. M. Langlands ◽  
I. W. Rodger
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Guinea Pig ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Kinase Assay ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Isolated Trachea ◽  
Dependent Protein

The effects of methacholine and histamine were examined on cyclic AMP-dependent protein kinase (A-kinase) activity in guinea-pig isolated trachea, using kemptide as a substrate for phosphorylation during the determination of the enzyme activity. Methacholine (EC90, 10 μM) induced a rapid reduction in the basal A-kinase activity ratio, which was maximal after 30 s. This initial reduction coincided with the early phase of isometric tension development, and returned to control levels 4 min after the addition of methacholine. Pretreatment with atropine inhibited the methacholine response. In contrast, histamine (EQ90, 30 μM) was without effect upon A-kinase activity ratio. The results establish the sensitivity of the A-kinase assay using kemptide and demonstrate that not all contractile agonists have the capacity to inhibit basal activity of A-kinase in airway smooth muscle.Key words: A-kinase, cholinomimetics, guinea-pig trachealis, smooth muscle contraction.

Measurement of cyclic-AMP-dependent protein kinase activity ratio in heart by use of a synthetic peptide

1988 ◽  
Vol 16 (3) ◽  
pp. 355-355 ◽  
Author(s):  
KENNETH J. MURRAY ◽  
PAUL J. ENGLAND ◽  
JAMES A. LYNHAM ◽  
DAVID MILLS ◽  
MARTIN L. REEVES
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Synthetic Peptide ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Inhibition of cerebral protein kinase activity and cyclic AMP-dependent ribosomal-protein phosphorylation in experimental hyperphenylalaninaemia

1982 ◽  
Vol 202 (2) ◽  
pp. 343-351 ◽  
Author(s):  
Sidney Roberts ◽  
Beatrice S. Morelos
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Ribosomal Protein ◽  
Protein Phosphorylation ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Protein Kinase Activity ◽  
Control Infant ◽  
Infant Rats ◽  
Dependent Protein

Studies were carried out to elucidate the mechanisms underlying the diminished phosphorylation of cerebral ribosomal protein in experimental hyperphenylalaninaemia [Roberts & Morelos (1980) Biochem. J.190, 405–419]. Administration of N6,O2′-dibutyryl cyclic AMP or 3-isobutyl-1-methylxanthine, which increased phosphorylation of the S6 protein of cerebral 40S ribosomal subunits in control infant rats, did not counteract the decreased phosphorylation of this ribosomal protein resulting from intraperitoneal administration of a loading dose of l-phenylalanine. N2,O2′-Dibutyryl cyclic GMP had no effect on cerebral ribosomal-protein phosphorylation in either control or hyperphenylalaninaemic animals. The phenylalanine-induced decrease in ribosomal-protein phosphorylation was associated with decreased protein kinase activity in cerebral cytosolic and microsomal preparations. However, the maximal protein kinase response to cyclic AMP added in vitro was unaltered by prior administration of phenylalanine in vivo. The heat-stable protein inhibitor of cyclic AMP-dependent protein kinases decreased the activity of these enzymes by about 90% and eliminated the phenylalanine-induced difference in protein kinase activity in the absence of added cyclic AMP. Intracisternal administration of doses of dibutyryl cyclic AMP or 3-isobutyl-1-methylxanthine which increased the cyclic AMP-dependent protein kinase activity ratio in control infant rats was without effect on this index in phenylalanine-treated animals. Dibutyryl cyclic GMP had no effect on the protein kinase activity ratio in either group of animals. These results suggest that inhibition of cerebral cyclic AMP-dependent protein kinases by abnormally high concentrations of phenylalanine may contribute to the decrease in cerebral ribosomal-protein phosphorylation in experimental hyperphenylalaninaemia.

CYCLIC NUCLEOTIDES and PROTEIN KINASE ACTIVITY IN THE RAT BRAIN POSTMORTEM

1978 ◽  
Vol 31 (2) ◽  
pp. 427-431 ◽  
Author(s):  
Michael J. Schmidt ◽  
Lewis L. Truex ◽  
John F. Thornberry
Keyword(s):  
Protein Kinase ◽  
Rat Brain ◽  
Cyclic Nucleotides ◽  
Kinase Activity ◽  
Protein Kinase Activity

scholarly journals Use of a synthetic dodecapeptide (malantide) to measure the cyclic AMP-dependent protein kinase activity ratio in a variety of tissues

1990 ◽  
Vol 267 (3) ◽  
pp. 703-708 ◽  
Author(s):  
K J Murray ◽  
P J England ◽  
J A Lynham ◽  
D Mills ◽  
C Schmitz-Peiffer ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Exogenous Enzyme ◽  
Activity Ratios ◽  
Measured Activity ◽  
Dependent Protein

1. The cyclic AMP-dependent protein kinase activity-ratio assay was investigated by comparing histone and a synthetic peptide, malantide [Malencik & Anderson (1983) Anal. Biochem. 132, 32-40], as substrates. 2. In several tissues the activity ratio was higher when assayed with histone as the substrate; this result was obtained in control tissues and also in those incubated with agents known to increase cyclic AMP. The effect of these agents to increase the activity ratio was more clearly demonstrated with malantide. 3. The higher activity ratios observed with histone are due to: (a) measurement of phosphorylation not catalysed by cyclic AMP-dependent protein kinase; (b) activation of cyclic AMP-dependent protein kinase by histone during the assay. 4. When tissues were homogenized in buffers without NACl, lower activity ratios were found, owing to the catalytic subunit being artifactually removed from the supernatant. 5. We conclude that the measured activity ratio more faithfully reflects that in the tissue when NaCl is included in the homogenization buffer and malantide is used in the assay. This was confirmed in experiments where cyclic AMP-dependent protein kinase was added to the tissue before homogenization, and no dissociation of the exogenous enzyme was observed.

scholarly journals Differential Effects of Carcinogens on Hepatic Cytosolic Cyclic AMP-dependent Protein Kinase Activity

1986 ◽  
Vol 5 (4) ◽  
pp. 267-273
Author(s):  
C. Timchalk ◽  
A. K. Charles
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Cell Membrane Permeability ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Differential Effects ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

Differential effects of epigenetic tumor promoters and a genotoxic carcinogen on hepatic cytosolic cyclic adenosine 3′,5′-monophosphate-dependent protein kinase (CAMP-PK) were studied in vitro, since this enzyme is one of the major mediators of cell membrane permeability. Mirex (dodecachlorooctahydro-1,3,4-metheno-2H-cyclobuto[cd]pentalene), like phorbol ester TPA (12-0-tetradecanoylphorbol-13-acetste), caused significant inhibition of cAMP-dependent protein kinase activity ratio, whereas DDT [p, p′-trichlorobis(p-chlorophenyl)ethane] produced concentration-dependent changes. Diethylnitrosamine (DEN) and phenobarbitol (PB), however, showed a significant enhancement of the activity ratio. Interestingly, combinations of mirex, DDT with PB or DEN resulted in the potentiation of CAMP-dependent protein kinase activity in contrast to their effects when used separately. The results suggest that the influences of mirex and TPA in vitro on CAMP-PK are different from those observed in other cell and intact animal systems.

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