Effect of calcium-activated, phospholipid, diacylglycerol-dependent protein kinase from rat basophilic leukemia cell (RBL-1 cell) on protein phosphorylation in rat mast cell granule membrane

1987 ◽  
Vol 10 (4) ◽  
pp. 376-383 ◽  
Author(s):  
Motohiro Kurosawa
Keyword(s):  
Mast Cell ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Leukemia Cell ◽  
Dependent Protein Kinase ◽  
Mast Cell Granule ◽  
Granule Membrane ◽  
Dependent Protein ◽  
Basophilic Leukemia Cell ◽  
Basophilic Leukemia

scholarly journals Ca2+/Calmodulin-dependent Protein Kinase II Regulates Tiam1 by Reversible Protein Phosphorylation

1999 ◽  
Vol 274 (18) ◽  
pp. 12753-12758 ◽  
Author(s):  
Ian N. Fleming ◽  
Cassondra M. Elliott ◽  
F. Gregory Buchanan ◽  
C. Peter Downes ◽  
John H. Exton
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Reversible Protein Phosphorylation

cAMP-dependent protein kinase mediates hydrosmotic effect of vasopressin in collecting duct

1992 ◽  
Vol 263 (1) ◽  
pp. C147-C153 ◽  
Author(s):  
H. M. Snyder ◽  
T. D. Noland ◽  
M. D. Breyer
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Water Permeability ◽  
Collecting Duct ◽  
Regulatory Subunit ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Pka Regulatory Subunit

The role of adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase A (PKA) in mediating the hydrosmotic effect of vasopressin in in vitro microperfused rabbit cortical collecting ducts (CCDs) was examined. We measured PKA substrate phosphorylation and water permeability [hydraulic conductivity (Lp) = 10(-7) cm.atm-1.s-1], stimulated by substituted cAMP analogues selective for a unique cAMP binding site (site A or B) on PKA regulatory subunit (R). Synergy between site A- and site B-selective analogues suggests involvement of PKA, because both sites must be occupied for R to dissociate from the catalytic subunit (C), allowing phosphorylation to proceed. As single agents, the site B-selective analogues 8-(4-chlorophenylthio)-cAMP (8-CPT) and 8-thiomethyl-cAMP (8-SCH3) were at least two orders of magnitude more potent than the site A-selective analogues N6-monobutyryl-cAMP (N6-mono) or N6-benzoyl-cAMP (N6-benz). Combinations of subthreshold concentrations of two site A analogues (N6-mono+N6-benz) or two site B-selective analogues (8-CPT + 8-SCH3) failed to significantly increase protein phosphorylation or water permeability. In contrast, combination of a site A plus site B analogue synergistically stimulated both protein phosphorylation and Lp. Rp-cAMPS, an inhibitor of cAMP binding to PKA, reduced both vasopressin (41% inhibition)- and cAMP (56% inhibition)-stimulated water permeability. H-89 (50 microM), an inhibitor of PKA kinase activity, also blocked cAMP-stimulated water permeability (90% inhibition). These findings suggest that vasopressin-induced water permeability in the rabbit CCD is mediated by PKA.

scholarly journals Hormone-induced protein phosphorylation. III. regulation of the phosphorylation of the secretagogue-responsive 29,000-dalton protein by both Ca2+ and cAMP in vitro.

1982 ◽  
Vol 95 (3) ◽  
pp. 918-923 ◽  
Author(s):  
S D Freedman ◽  
J D Jamieson
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Exocrine Pancreas ◽  
Second Messengers ◽  
Subcellular Fractions ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Intact Cells ◽  
Dependent Protein

In the preceding papers, we demonstrated that the endogenous phosphorylation of a 29,000-dalton protein is stimulated in response to secretagogue application to intact cells from the rat exocrine pancreas and parotid and dephosphorylated upon termination of secretagogue action. One- and two-dimensional gel analysis of 32Pi-labeled pancreatic and parotid lobules as well as their respective subcellular fractions revealed that the same protein was covalently modified in both tissues and was localized to the ribosomal fraction. To identify the intracellular second messengers which may mediate or modulate the phosphorylation of the 29,000-dalton protein in intact cells, the effects of Ca2+, cAMP, and cGMP on the endogenous phosphorylation of this protein were assessed in subcellular fractions from the rat pancreas and parotid. Our results demonstrate that the phosphorylation of the 29,000-dalton polypeptide may be regulated by both Ca2+ and cAMP in the pancreas and in the parotid. No cGMP-dependent protein phosphorylation was found in either tissue. As in the in situ phosphorylation studies, the Ca2+- and cAMP-dependent phosphorylation of this same protein was localized to the ribosomal fraction. The cAMP-dependent protein kinase activity was found primarily in the postmicrosomal supernatant in contrast to the Ca2+-dependent protein kinase that appeared to be tightly associated with the substrate in addition to being present in the postmicrosomal supernatant. The data suggest that, in cells from the exocrine pancreas and parotid, secretagogues may regulate the phosphorylation of the 29,000-dalton protein through Ca2+ and/or cAMP.

Calcium-dependent Protein Kinase Reactions Associated with Parotid Gland Secretory Granule Membranes

1987 ◽  
Vol 66 (2) ◽  
pp. 557-563 ◽  
Author(s):  
F. Dowd ◽  
E.L. Watson ◽  
Y.-S. Lau ◽  
J. Justin ◽  
J. Pasieniuk ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Secretory Granule ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Granule Membrane ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinase

Rat parotid secretory granule membranes were examined for the presence of calcium-dependent protein kinase activities and kinase substrates. Protein kinase C (C-kinase), which is stimulated by certain phospholipids, was present in the membranes, as indicated by its ability to catalyze the phosphorylation of histone. Two substrates for protein kinase C were seen in the granule membranes. The cytosolic fraction from the cell contained kinase activity, which was stimulated by phosphatidylserine and which caused the phosphorylation of two granule membrane polypeptides. In addition, when both granule membranes and cytosol were incubated together, phosphorylation of the cytosolic substrates was inhibited, indicating that the granule membrane substrates were phosphorylated preferentially. The results indicate that the granule membranes may react with cytosolic protein kinase C activity in a way which would direct an intracellular calcium and diacylglycerol signal toward the granule membrane. Since these signals occur during stimulation by various agonists, the mechanism may contribute to secretion.

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