Studies on a cyclic AMP-dependent protein kinase from rat thyroid gland

Leonard, Jack L.; Rosenberg, Lawson L.

doi:10.1016/0005-2744(77)90089-4

Cited by 11 publications

(2 citation statements)

References 25 publications

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“…Histone H I kinase activity measured in the presence of 2 pM cyclic-AMP and [3H]-cyclic-AMP binding occurs predominantly as a single peak at 155 mM KC1 (range 145-163 mM; n = 3). This finding is in agreement with Leonard et a1 [24] and Combest et a1 [27], but is in some disagreement with other findings [25]. Polyamine inhibition of the partially purified enzyme is qualitatively similar to studies performed using the crude supernatant fraction (data not shown).…”

Section: Resultssupporting

confidence: 92%

“…Polyamines have been shown to augment incorporation of 32P into nonhistone chromatin proteins in several systems , and there are several lines of evidence that strongly support reversible phosphorylation as an important mechanism in the regulation of transcription. The reported alterations in the number of initiation sites [32], as well as RNA polymerase I [24,33,34] and RNA polymerase I1 [35] activities, suggest that control of transcription by reversible phosphorylation may be operative at several levels. Although our data suggests that the term polyamine-dependent protein kinase may be appropriate to describe, at least in part, messenger-independent protein kinase activity, Cochet and Chambaz have, in a recent review [9], suggested that, because polyamines may interact primarily with substrate, the term "polyaminemediated phosphorylation" may be more appropriate.…”

Section: Discussionmentioning

confidence: 99%

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Differential effects of polyamines on rat thyroid protein kinase activities

Levasseur

Henricks

Poleck

et al. 1985

J of Cellular Biochemistry

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Ornithine decarboxylase, the rate-limiting enzyme in polyamine biosynthesis, has been shown to be regulated in thyroid by thyrotropin both in vivo and in vitro. Little, however, is known of the role of polyamines in thyroid cell function. Since studies in other tissues suggest that polyamines may influence protein phosphorylation, we studied the effect of the polyamines on various protein kinase activities in rat thyroid. Putrescine, spermidine, and spermine inhibit cyclic-AMP-dependent histone H1 kinase activity when measured in the cytosol fraction of rat thyroid; this effect is largely reproduced by NaCl concentrations of equivalent ionic strength. Both spermidine and spermine effect a 1.6-2.4-fold increase in cytosolic cyclic-AMP-independent (messenger-independent) casein kinase activity; stimulation by both polyamines is maximal at 5mM. A similar profile of stimulation is observed for messenger-independent casein kinase activity in crude nuclear preparations. Sodium chloride fails to stimulate both cytosolic and nuclear messenger-independent casein kinase activities at ionic strength equivalent to the spermine concentrations used. Spermine, but not putrescine, spermidine, or sodium chloride, inhibits calcium/phospholipid-dependent protein kinase C activity in cytosol extracts partially purified by DEAE chromatography. These findings suggest that regulation of protein kinase(s) by polyamines may represent a proximal locus (i) of action of thyrotropin-regulated ornithine decarboxylase activity in thyroid.

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Section: Resultssupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Differential effects of polyamines on rat thyroid protein kinase activities

Levasseur

Henricks

Poleck

et al. 1985

J of Cellular Biochemistry

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Cyclic AMP-dependent protein kinase from Ustilago maydis

Passeron

1984

Mol Cell Biochem

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Ustilago maydis was surveyed for cyclic AMP-dependent protein kinase activity. Using a combination of ion-exchange and molecular filtration techniques, we demonstrate that there is only one form of cyclic AMP-dependent protein kinase in the cytosolic fraction of the fungus. The kinase activity is specifically activated by cyclic AMP and utilizes protamine and kemptide as substrates. Most, if not all, of the cyclic AMP binding detected in the soluble fraction is associated with the protein kinase activity. Cyclic AMP-dependent protein kinase is completely dissociated by cyclic AMP into catalytic and regulatory subunits having an apparent molecular weight of 35 000 daltons as judged by sucrose gradient centrifugation.

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Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii

Moreno

Passeron

1980

Archives of Biochemistry and Biophysics

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Studies on a cyclic AMP-dependent protein kinase from rat thyroid gland

Cited by 11 publications

References 25 publications

Differential effects of polyamines on rat thyroid protein kinase activities

Differential effects of polyamines on rat thyroid protein kinase activities

Cyclic AMP-dependent protein kinase from Ustilago maydis

Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii

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