scholarly journals Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases

2015 ◽  
Vol 6 ◽  
Author(s):  
Silvio Weber ◽  
Stefanie Meyer-Roxlau ◽  
Michael Wagner ◽  
Dobromir Dobrev ◽  
Ali El-Armouche
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Phosphatases ◽  
Multiple Roles ◽  
Protein Kinase Activity

scholarly journals Protein Phosphatases Regulate DNA-dependent Protein Kinase Activity

2001 ◽  
Vol 276 (22) ◽  
pp. 18992-18998 ◽  
Author(s):  
Pauline Douglas ◽  
Greg B. G. Moorhead ◽  
Ruiqiong Ye ◽  
Susan P. Lees-Miller
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Phosphatases ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Dependent Protein

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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