PROTEIN KINASES ACTIVATED BY cAMP IN THE GENITAL TRACT OF SPAYED MICE TREATED WITH OESTRADIOL-17

Døskeland, Stein Ove; Kvinnsland, Stener; Ueland, Per Magne

doi:10.1530/jrf.0.0440207

Cited by 17 publications

(3 citation statements)

References 13 publications

(11 reference statements)

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“…Several workers (Corbin et al, 1975;Tao & Hackett, 1973;Kumon et al, 1972), including ourselves (D0skeland et al, 1975;D0skeland & Ueland, 1975a), have found that isoenzyme PK II is less dependent than isoenzyme PK I on cyclic AMP for activity under standard assay conditions. On this basis one might speculate whether isoenzyme PK1 II accounts for a continuous cyclic AMP-independent phosphorylation in the cell (D0skeland et al, 1975).…”

Section: Discussionmentioning

confidence: 99%

“…Two main forms of cyclic AMP-dependent protein kinase seem to be widely distributed in mammalian tissue (Corbin et al, 1975;D0skeland et al, 1975); their properties have been compared (Corbin et al, 1975;Hofmann et al, 1975). Evidence has been presented that the isoenzymes differ in their regulatory subunit, whereas the catalytic subunit seems to be the same (Bechtel etal., 1975;Fakunding & Means, 1975;Kumon et al, 1972).…”

Section: Discussionmentioning

confidence: 99%

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

Ueland¹,

Døskeland²

1976

Biochemical Journal

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Conditions influencing the cyclic AMP-dependence of protein kinase (ATP-protein phosphotransferase, EC 2.7.1.37) during the phosphorylation of histone were studied. Protein kinase from mouse liver cytosol and the two isoenzymes [PK (protein kinase) I and PK II] isolated from the cytosol by DEAE-cellulose chromatography were tested. A relation between concentration of enzyme and cyclic AMP-dependence was observed for both isoenzymes. Moderate dilution of isoenzyme PK II decreased the stimulation of the enzyme by cyclic AMP. Isoenzyme PK I could be diluted 200 times more than isoenzyme PK II before the same decrease in cyclic AMP-dependence appeared. Long-term incubation with high concentrations of histone increased the activity in the absence of cyclic AMP relative to the activity in the presence of the nucleotide. This was more pronounced for isoenzyme PK II than for isoenzyme PK I. The cyclic AMP concentration needed to give half-maximal binding of the nucleotide was the same as the cyclic AMP concentration (Ka) at which the protein kinase had 50% of its maximal activity. The close correlation between binding and activation is also found in the presence of KCl, which increased the apparent activation constant (Ka) for cyclic AMP. With increasing [KCl], a progressively higher proportion of the histone phosphorylation observed in cytosol was due to cyclic AMP-independent (casein) kinases, leading to an overestimation of the degree of activation of the cyclic AMP-dependent protein kinases present. The relative contributions of cyclic AMP-dependent and -independent kinases to histone phosphorylation at different ionic strengths was determined by use of heat-stable inhibitor and phospho-cellulose chromatography.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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

Ueland¹,

Døskeland²

1976

Biochemical Journal

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“…Multiple protein kinases are regulated in association with growth, proliferation and differentiation of cells (Gaballah et al, 1971;Lee et al, 1975;Doskeland et al, 1975;Costa et al,1976;Skala and Knight, 1977;Lohmann et al, 1978;Miyamoto et al, 1980). We have previously shown that both activities of types I and II cyclic AMP-dependent protein kinases in the endometrium are altered by the administration of hormones including estrogen, progesterone and chorionic gonadotropin (Miyazaki et al, 1980a;Miyazaki et al, 1981) and during the menstrual cycle (Miyazaki et al, 1980b).…”

mentioning

confidence: 99%

Dissociation of alterations in levels of myosin light chain kinase and cyclic AMP-dependent protein kinase in rabbit myometrium during pregnancy.

et al. 1982

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Cyclic AMP-dependent protein kinases and cAMP-binding proteins in human mammary tumor MCF-7 cells

1984

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Two isoenzymes of cAMP-dependent protein kinases were found in MCF-7 cytosol. The regulatory (cAMP-binding) subunit of protein kinase I (predominant form) has an apparent molecular weight (MW) of 49,000 and the two forms of regulatory subunits of protein kinase II have MWs of 52,000 and 54,000. Substantial amounts of the 49,000 protein cochromatographed on DEAE cellulose with protein kinase II. The quantities of protein kinase holoenzyme activity are strongly influenced by extraction procedures: the use of EDTA and of the protease inhibitor benzamidine can lead to extensive dissociation. On the other hand, high yields of cAMP-dependent protein kinase holoenzyme activity were consistently obtained with 150 mM KCl.

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PROTEIN KINASES ACTIVATED BY cAMP IN THE GENITAL TRACT OF SPAYED MICE TREATED WITH OESTRADIOL-17

Cited by 17 publications

References 13 publications

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

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

Dissociation of alterations in levels of myosin light chain kinase and cyclic AMP-dependent protein kinase in rabbit myometrium during pregnancy.

Cyclic AMP-dependent protein kinases and cAMP-binding proteins in human mammary tumor MCF-7 cells

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