Differential regulation of basic protein phosphorylation by calcium phospholipid and cyclic-AMP-dependent protein kinases

1989 ◽  
Vol 40 (3) ◽  
pp. 261-269 ◽  
Author(s):  
Glyn Dawson ◽  
Patrick McAtee
Keyword(s):  
Cyclic Amp ◽  
Protein Phosphorylation ◽  
Protein Kinases ◽  
Basic Protein ◽  
Differential Regulation ◽  
Dependent Protein

Possible Roles for Protein Phosphorylation in Platelet Responses

1979 ◽  
Author(s):  
R.J. Haslam ◽  
J.E.B. Fox ◽  
S.E. Salama ◽  
J.A. Lynham
Keyword(s):  
Cyclic Amp ◽  
Protein Phosphorylation ◽  
Protein Kinases ◽  
Platelet Function ◽  
Subcellular Fractionation ◽  
Human Platelets ◽  
Type I ◽  
Sds Page ◽  
Dependent Protein ◽  
32P Incorporation

The relationships between the phosphorylation of specific platelet polypeptides and platelet function were studied using washed human platelets labelled by preincubation with [32p] Pi. Platelet polypeptides were separated by SDS-PAGE and 32P incorporation into them determined by autoradiography. Whereas induction of platelet aggregation alone did not affect protein phosphorylation, induction of the release reaction increased 3P incorporation into several polypeptides (P75,P47,P40,P27,P20,P19), including the P-light chain of platelet myosin (P20). These changes were inhibited by drugs that blocked Ca2 movements and may be due to activation of Ca2+-dependent protein kinases. Compounds that inhibited platelet function by increasing cyclic AMP (e.g. PCE1) also suppressed these reactions but, in addition, increased phosphorylation of other polypeptides (P50,P49,P36,P24,P22). Type I and Type II cyclic AMP-dependent protein kinases were present in platelets and may mediate Che latter effects of cyclic AMP. Subcellular fractionation of 32p-labelled platelets that had been exposed to PCE1 showed that P24 was present in membranes that could take up Ca2+ by an ATP-dependent mechanism. Membranes from PCE1-treated platelets took up Ca2+ more rapidly than control membranes. Thus, the cyclic AMP-dependent phosphorylation of P24 may stimulate the removal of Ca2+ from platelet cytosol and suppress Ca2+-dependent phosphorylation reactions necessary for release of granule constituents.

scholarly journals Calcium- and cyclic AMP-regulated protein kinases of bovine central-nervous-system myelin

1984 ◽  
Vol 218 (3) ◽  
pp. 923-932 ◽  
Author(s):  
N C Wu ◽  
F Ahmad
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Cyclic Amp ◽  
Substrate Specificity ◽  
Protein Kinases ◽  
Basic Protein ◽  
Phospholipases A2 ◽  
Dependent Protein ◽  
Myelin Fraction ◽  
Triton X

Bovine central-nervous-system myelin was found to contain both Ca2+-activated and cyclic AMP-dependent protein kinases. Each enzyme possesses unique solubility and substrate-specificity characteristics. The Ca2+-activated enzyme, like its substrate (basic protein), is probably deeply embedded in the neural membrane, whereas the cyclic AMP-dependent kinase appears to be much less tightly associated with myelin. Treatment of insoluble myelin fraction housing the Ca2+-activated kinase with phospholipase A2 and phospholipases A2 + C causes a decrease in its ability to become activated by Ca2+. This can be countered by phosphatidylserine and phosphatidylethanolamine. Whereas the activity of the Ca2+-activated membrane-associated kinase is inhibited by chlorpromazine, dibucaine, melittin and Triton X-100, it is activated by certain phorbol diesters (4 beta-phorbol 12-myristate 13-acetate, 4 beta-phorbol 12,13-didecanoate, 4 beta-phorbol 12,13-dibenzoate and 4 beta-phorbol 12,13-diacetate), which appear to exert this effect by lowering the concentration of Ca2+ normally required for the activation of this enzyme. Together these results suggest that the activation of the membrane-associated kinase by Ca2+ most probably requires certain lipids, perhaps those already present in the membrane.

scholarly journals Ca2+-induced insulin secretion from electrically permeabilized islets. Loss of the Ca2+-induced secretory response is accompanied by loss of Ca2+-induced protein phosphorylation

1992 ◽  
Vol 285 (3) ◽  
pp. 973-978 ◽  
Author(s):  
P M Jones ◽  
S J Persaud ◽  
S L Howell
Keyword(s):  
Protein Kinase C ◽  
Insulin Secretion ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Phosphorylation ◽  
Prolonged Exposure ◽  
Kinase C ◽  
Dependent Protein ◽  
32P Incorporation ◽  
Rat Islets Of Langerhans

Increasing the cytosolic Ca2+ concentration of electrically permeabilized rat islets of Langerhans caused rapid increases in insulin secretion and in 32P incorporation into islet proteins. However, the secretory responsiveness of permeabilized islets was relatively transient, with insulin secretion approaching basal levels within 20-30 min despite the continued presence of stimulatory concentrations of Ca2+. The loss of Ca2(+)-induced insulin secretion was accompanied by a marked reduction in Ca2(+)-dependent protein phosphorylation, but not in cyclic AMP-dependent protein phosphorylation. Similarly, permeabilized islets which were no longer responsive to Ca2+ were able to mount appropriate secretory responses to cyclic AMP and to a protein kinase C-activating phorbol ester. These results suggest that prolonged exposure to elevated cytosolic Ca2+ concentrations results in a specific desensitization of the secretory mechanism to Ca2+, perhaps as a result of a decrease in Ca2(+)-dependent kinase activity. Furthermore, these studies suggest that secretory responses of B-cells to cyclic AMP and activators of protein kinase C are not dependent upon the responsiveness of the cells to changes in cytosolic Ca2+.

scholarly journals Deficiency of cyclic AMP-dependent protein kinases in human psoriasis.

1986 ◽  
Vol 83 (14) ◽  
pp. 5272-5276 ◽  
Author(s):  
D. E. Brion ◽  
F. Raynaud ◽  
A. Plet ◽  
P. Laurent ◽  
B. Leduc ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Protein Kinases ◽  
Dependent Protein

Involvement of cyclic AMP-dependent protein kinases in the signal transduction pathway for interleukin-1

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827
Author(s):  
M Chedid ◽  
S B Mizel
Keyword(s):  
Signal Transduction ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Cell Types ◽  
Specific Protein ◽  
Transduction Pathway ◽  
Dependent Protein

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.

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