Nuclear protein-kinase activity in perfused rat liver stimulated with dibutyryl-adenosine cyclic 3':5'-monophosphate
- PMID: 170096
- DOI: 10.1111/j.1432-1033.1975.tb02151.x
Nuclear protein-kinase activity in perfused rat liver stimulated with dibutyryl-adenosine cyclic 3':5'-monophosphate
Abstract
Cytoplasmic and nuclear protein kinase activities from perfused rat liver have been studied in response to dibutyryl-adenosine cyclic 3':5'-monophosphate added at a concentration that stimulates hepatic gluconeogenesis (100 muM). Total nuclear protein kinase, as assayed using a mixed histone fraction as phosphate acceptor, is increased by 5-fold within 8 min of the addition of cyclic nucleotide to the perfusate. In contrast the total cytoplasmic protein kinase activity is decreased to 50% of the control value. The protein substrate specificity of the protein kinase that is present in the nucleus in response to dibutyryl-adenosine cyclic 3':5'-monophosphate stimulation is similar to that of cytoplasmic, adenosine cyclic 3':5'-monophosphate-dependent, protein kinase but is distinct from that of the enzyme(s) present in control nuclei. The predominant species to protein kinase from stimulated nuclei has a sedimentation constant of 3.9 S. This value is identical to that of the catalytic subunit of cytoplasmic adenosine 3':5'-monophosphate-dependent protein kinase. These data suggest that some of the effects of adenosine 3':5'-monophosphate on nuclear events may be mediated through its interaction with the inactive protein kinase holoenzyme in the cytoplasm and the subsequent redistribution of the active catalytic subunits generated by this interaction.
Similar articles
-
Cyclic AMP-dependent histone-specific nucleoplasmic protein kinase from rat liver.Biochem J. 1978 Apr 1;171(1):123-35. doi: 10.1042/bj1710123. Biochem J. 1978. PMID: 206265 Free PMC article.
-
Activity and subcellular distribution of protein kinase dependent on adenosine 3':5'-monophosphate in liver from normal and adrenalectomized rats.Eur J Biochem. 1976 Jul 15;66(3):499-506. doi: 10.1111/j.1432-1033.1976.tb10575.x. Eur J Biochem. 1976. PMID: 182492
-
Evidence for the identity of nuclear and cytoplasmic adenosine-3':5'-monophosphate-dependent protein kinase from porcine ovaries and nuclear translocation of the cytoplasmic enzyme.Eur J Biochem. 1977 Feb 15;73(1):199-212. doi: 10.1111/j.1432-1033.1977.tb11308.x. Eur J Biochem. 1977. PMID: 190008
-
Direct cytochemical localization of catalytic subunits dissociated from cAMP-dependent protein kinase in Reuber H-35 hepatoma cells. II. Temporal and spatial kinetics.J Cell Biol. 1982 Jun;93(3):727-34. doi: 10.1083/jcb.93.3.727. J Cell Biol. 1982. PMID: 6288733 Free PMC article.
-
Cyclic AMP, cyclic AMP-dependent protein kinase, and the regulation of gene expression.Life Sci. 1977 Jun 1;20(11):1787-97. doi: 10.1016/0024-3205(77)90213-2. Life Sci. 1977. PMID: 195171 Review. No abstract available.
Cited by
-
Specific nuclear binding of adenosine 3',5'-monophosphate-binding protein complex with subsequent poly(A) RNA synthesis in embryonic chick cartilage.J Clin Invest. 1980 Sep;66(3):532-42. doi: 10.1172/JCI109885. J Clin Invest. 1980. PMID: 6156954 Free PMC article.
-
Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus.EMBO J. 1985 Nov;4(11):2801-6. doi: 10.1002/j.1460-2075.1985.tb04006.x. EMBO J. 1985. PMID: 2998755 Free PMC article.
-
Adenylate cyclase activity in lymphocyte subcellular fractions. Characterization of a nuclear adenylate cyclase.Biochem J. 1977 Mar 15;162(3):483-91. doi: 10.1042/bj1620483. Biochem J. 1977. PMID: 194578 Free PMC article.
-
In vivo phosphorylation of a synthetic peptide substrate of cyclic AMP-dependent protein kinase.Proc Natl Acad Sci U S A. 1978 Jan;75(1):248-51. doi: 10.1073/pnas.75.1.248. Proc Natl Acad Sci U S A. 1978. PMID: 203933 Free PMC article.
-
Cyclic AMP-dependent histone-specific nucleoplasmic protein kinase from rat liver.Biochem J. 1978 Apr 1;171(1):123-35. doi: 10.1042/bj1710123. Biochem J. 1978. PMID: 206265 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources