The Role of the Cyclic AMP-Dependent Protein Phosphorylations and Microtubules in the Cellular Action of Vasopressin in Mammalian Kidney

2015 ◽  
pp. 220-235 ◽  
Author(s):  
Thomas P. Dousa ◽  
Larry D. Barnes ◽  
Jin K. Kim
Keyword(s):  
Cyclic Amp ◽  
Mammalian Kidney ◽  
Dependent Protein

scholarly journals Activation of cyclic AMP-dependent kinase is required but may not be sufficient to mimic cyclic AMP-dependent DNA synthesis and thyroglobulin expression in dog thyroid cells.

1997 ◽  
Vol 17 (11) ◽  
pp. 6717-6726 ◽  
Author(s):  
S Dremier ◽  
V Pohl ◽  
C Poteet-Smith ◽  
P P Roger ◽  
J Corbin ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Dna Synthesis ◽  
Regulatory Subunit ◽  
Thyroid Cells ◽  
Morphological Effect ◽  
Heat Stable ◽  
Proliferation And Differentiation ◽  
C Subunit ◽  
Dependent Protein

Thyrotropin (TSH), via a cyclic AMP (cAMP)-dependent pathway, induces cytoplasmic retractions, proliferation, and differentiation expression in dog thyroid cells. The role of cAMP-dependent protein kinase (PKA) in the induction of these events was assessed by microinjection into living cells. Microinjection of the heat-stable inhibitor of PKA (PKI) inhibited the effects of TSH, demonstrating that activation of PKA was required in this process. Overexpression of the catalytic (C) subunit of PKA brought about by microinjection of the expression plasmid pC alpha ev or of purified C subunit itself was sufficient to mimic the cAMP-dependent cytoplasmic changes and thyroperoxidase mRNA expression but not to induce DNA synthesis and thyroglobulin (Tg) expression. The cAMP-dependent morphological effect was not observed when C subunit was coinjected with the regulatory subunit (RI or RII subunit) of PKA. To mimic the cAMP-induced PKA dissociation into free C and R subunits, the C subunit was coinjected with the regulation-deficient truncated RI subunit (RIdelta1-95) or with wild-type RI or native RII subunits, followed by incubation with TSH at a concentration too low to stimulate the cAMP-dependent events by itself. Although the cAMP-dependent morphology changes were still observed, neither DNA synthesis nor Tg expression was stimulated in these cells. Taken together, these data suggest that in addition to PKA activation, another cAMP-dependent mechanism could exist and play an important role in the transduction of the cAMP signal in thyroid cells.

Fructose 2,6-bisphosphate biosynthesis and regulation of carbohydrate metabolism in Aspergillus oryzae

1998 ◽  
Vol 44 (1) ◽  
pp. 6-11
Author(s):  
Gandhi Rádis-Baptista ◽  
David N. Urquizo Valdivia ◽  
José Abrahão-Neto
Keyword(s):  
Cyclic Amp ◽  
Carbohydrate Metabolism ◽  
Aspergillus Oryzae ◽  
Culture Conditions ◽  
Dependent Protein Kinase ◽  
Fructose 1,6 Bisphosphatase ◽  
Dependent Protein ◽  
Regulation Of Carbohydrate Metabolism

The biosynthesis and role of fructose 2,6-bisphosphate (Fru-2,6-P2) in carbohydrate metabolism during induction of an amylolytic system in Aspergillus oryzae was studied. Fluctuations in Fru-2,6-P2 were not dependent on the external glucose concentration during induction, whereas the level of Fru-2,6-P2 increased significantly when the oxygen concentration was diminished. Phosphofructokinase II (PFK II) of A. oryzae was sensitive to phosphorylation in vitro by the catalytic subunit of cyclic AMP dependent protein kinase, which increased the Vmax (twofold), although the Km (0.7 mM) remained unchanged. Phosphofructokinase I was neither activated by micromolar Fru-2,6-P2 nor inhibited by high ATP concentrations. The activity of fructose-1,6-bisphosphatase (FBPase) was subject to strong inhibition by Fru-2,6-P2. Addition of glucose to cultures under gluconeogenic conditions caused a decrease of approximately 40% in the FBPase activity within 4 min. These results indicate that the effect of Fru-2,6-P2 in A. oryzae could preferentially control gluconeogenesis. The addition of 0.1 M glucose under gluconeogenic culture conditions also showed that Fru-2,6-P2 fluctuations appeared to be, at least in short term, more closely related to temporal changes in the hexose-6-phosphate concentration.Key words: Aspergillus oryzae; fructose-2,6-bisphosphate; phosphofructokinase II (PFK II); cyclic AMP; gluconeogenesis control.

scholarly journals Role of the Cyclic AMP-dependent Protein Kinase in Homologous Resensitization of the β1-Adrenergic Receptor

2004 ◽  
Vol 279 (20) ◽  
pp. 21135-21143 ◽  
Author(s):  
Lidia A. Gardner ◽  
Noel M. Delos Santos ◽  
Shannon G. Matta ◽  
Michael A. Whitt ◽  
Suleiman W. Bahouth
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Adrenergic Receptor ◽  
Dependent Protein Kinase ◽  
Dependent Protein
Sign in / Sign up

Export Citation Format

Share Document