Staurosporine-inhibitable protein kinase activity associated with secretory granule membranes isolated from rat submandibular gland cells

2003 ◽  
Vol 48 (8) ◽  
pp. 553-558 ◽  
Author(s):  
Su Ryeon Seo ◽  
Yeun Ju Kim ◽  
Seok Jun Moon ◽  
Hiroshi Sugiya ◽  
Dong Min Shin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Submandibular Gland ◽  
Secretory Granule ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Gland Cells ◽  
Rat Submandibular Gland

Characterization and partial purification of rat submandibular gland protein kinase C

1988 ◽  
Vol 66 (7) ◽  
pp. 683-690
Author(s):  
D. J. Pon ◽  
S. P. Lintlop ◽  
A. K. Sen
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Submandibular Gland ◽  
Kinase Activity ◽  
Partial Purification ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Kinase C ◽  
Membrane Bound ◽  
Rat Submandibular Gland

Membrane-bound protein kinase C of rat submandibular gland was characterized and the cytosolic kinase C of the tissue was partially purified. The membrane-bound kinase could be activated by Triton X-100 but not EGTA in the presence of both Ca2+ and phosphatidylserine (PS). The Km values for Ca2+ and PS were 150 μM and 5 μg, respectively. Addition of 10−6 M diacylglycerol resulted in an increased affinity of the kinase for Ca2+ (Km = 10 μM). Phorbol 12,13-dibutyrate activated the kinase in the absence of exogenous Ca2+ and PS, suggesting that adequate amounts of each activator are present in the membrane itself. Polymyxin B inhibited the stimulated kinase C activity in a concentration-dependent manner. This inhibition could be overcome by addition of PS. The cytosolic kinase was partially purified 133-fold by chromatography on columns of DEAE-Sephacel and S-300 Sephacryl. The total kinase activity increased with respect to the kinase activity measured in the starting material with column chromatography, suggesting that an inhibitor is present in the cytosolic fraction of the tissue.

Effect of Thrombin on Phosphorylation of Platelet Membrane Proteins

1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Qualitative Change ◽  
Protein Kinase Activity ◽  
Protein Substrates ◽  
Phosphoprotein Phosphatase ◽  
Progressive Loss ◽  
Platelet Membranes ◽  
Endogenous Protein ◽  
Considerable Loss

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.

scholarly journals Evidence for Ecto-Protein Kinase Activity That Phosphorylates Kemptide in a Cyclic AMP-dependent Mode

1989 ◽  
Vol 264 (24) ◽  
pp. 14549-14555 ◽  
Author(s):  
D Kübler ◽  
W Pyerin ◽  
O Bill ◽  
A Hotz ◽  
J Sonka ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Protein Kinase Activity
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