Effects of an Endogenous Cyclic AMP-Dependent Protein Kinase Catalytic Subunit on Ca-Uptake by Plasma Membrane Vesicles from Rat Mesenteric Artery

1984 ◽  
Vol 21 (6) ◽  
pp. 257-266 ◽  
Author(s):  
D.M. Kattenburg ◽  
E.E. Daniel
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Mesenteric Artery ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Dependent Protein Kinase ◽  
Rat Mesenteric Artery ◽  
Ca Uptake ◽  
Dependent Protein

scholarly journals Release of Ca2+ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cyclic AMP-dependent protein kinase

1989 ◽  
Vol 257 (3) ◽  
pp. 715-721 ◽  
Author(s):  
F O'Rourke ◽  
G B Zavoico ◽  
M B Feinstein
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Membrane Protein ◽  
Protein Phosphorylation ◽  
Kinase Inhibitor ◽  
Membrane Vesicles ◽  
Platelet Membrane ◽  
Dependent Protein Kinase ◽  
Inositol 1,4,5 Trisphosphate ◽  
Dependent Protein

In contrast with previous reports, it was found that membrane-protein phosphorylation by the catalytic subunit (CS) of cyclic AMP-dependent protein kinase had no effect on Ca2+ uptake into platelet membrane vesicles or on subsequent Ca2+ release by inositol 1,4,5-trisphosphate (IP3). Furthermore, IP-20, a highly potent synthetic peptide inhibitor of CS, which totally abolished membrane protein phosphorylation by endogenous or exogenous CS, also had no effect on either Ca2+ uptake or release by IP3. Commercial preparations of protein kinase inhibitor protein (PKI) usually had no effect, but one preparation partially inhibited Ca2+ uptake, which is attributable to the gross impurity of the commercial PKI preparation. IP3-induced release of Ca2+ was also unaffected by the absence of ATP from the medium, supporting the conclusion that Ca2+ release by IP3 does not require the phosphorylation of membrane protein.

scholarly journals Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane

FEBS Letters ◽  
1983 ◽  
Vol 152 (2) ◽  
pp. 195-198 ◽  
Author(s):  
B. Sarkadi ◽  
Ágnes Enyedi ◽  
Anna Faragó ◽  
G. Mészáros ◽  
T. Kremmer ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Dependent Protein Kinase ◽  
Dependent Protein

Stimulation of an individual cell with peptide hormone in a prescribed region of its plasma membrane results in a compartmentalized cyclic AMP-dependent protein kinase response

1991 ◽  
Vol 6 (3) ◽  
pp. 269-279 ◽  
Author(s):  
E. J. Podesta ◽  
A. R. Solano ◽  
J. R. Lemos
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Hormone Receptors ◽  
Individual Cell ◽  
Peptide Hormone ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
General Response ◽  
Peptide Hormone Receptors

ABSTRACT This work describes the stimulation by a peptide hormone of an individual cell in a prescribed region of its plasma membrane. When Leydig cells were stimulated via a section of membrane tightly sealed to an electrode containing LH, a very localized area exhibited the morphological change known as 'rounding up', which is a cyclic AMP-dependent protein kinase-mediated response. This localized stimulation did not produce a wider response through intracellular, intermembranous or extra-cellular signals. Each individual cell responded to peptide stimulation gradually, with an increase over time and with dose. In contrast, when the stimulation was accomplished using a non-hydrolysable cyclic AMP analogue in the patch electrode, a general response throughout an individual cell was produced. Locally stimulated peptide hormone receptors, adenylate cyclases and cyclic AMP-dependent protein kinases appear to be closely associated so that second messenger production and the effects it mediates are compartmentalized.

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