Role of Phosphorylase Kinase and Cyclic AMP-dependent Protein Kinase in the Regulation of Phosphorylase Phosphatase

1978 ◽  
Vol 6 (1) ◽  
pp. 21-25 ◽  
Author(s):  
PÁL GERGELY ◽  
GYÖRGY BOT
1975 ◽  
Vol 149 (3) ◽  
pp. 525-533 ◽  
Author(s):  
H A Cole ◽  
S V Perry

1. Troponin I isolated from fresh cardiac muscle by affinity chromatography contains about 1.9 mol of covalently bound phosphate/mol. Similar preparations of white-skeletal-muscle troponin I contain about 0.5 mol of phosphate/mol. 2. A 3':5'-cyclic AMP-dependent protein kinase and a protein phosphatase are associated with troponin isolated from cardiac muscle. 3. Bovine cardiac 3':5'-cyclic AMP-dependent protein kinase catalyses the phosphorylation of cardiac troponin I 30 times faster than white-skeletal-muscle troponin I. 4. Troponin I is the only component of cardiac troponin phosphorylated at a significant rate by the endogenous or a bovine cardiac 3':5'-cyclic AMP-dependent protein kinase. 5. Phosphorylase kinase catalyses the phosphorylation of cardiac troponin I at similar or slightly faster rates than white-skeletal-muscle troponin I. 6. Troponin C inhibits the phosphorylation of cardiac and skeletal troponin I catalysed by phosphorylase kinase and the phosphorylation of white skeletal troponin I catalysed by 3':5'-cyclic AMP-dependent protein kinase; the phosphorylation of cardiac troponin I catalysed by the latter enzyme is not inhibited.


2004 ◽  
Vol 279 (20) ◽  
pp. 21135-21143 ◽  
Author(s):  
Lidia A. Gardner ◽  
Noel M. Delos Santos ◽  
Shannon G. Matta ◽  
Michael A. Whitt ◽  
Suleiman W. Bahouth

1977 ◽  
Vol 168 (2) ◽  
pp. 307-310 ◽  
Author(s):  
P J England

When hearts from control and phosphorylase kinase-deficient (I strain) mice were perfused with 0.1 micrometer-DL-isoprenaline, there was a parallel increase in contraction, cyclic AMP concentration and troponin I phosphorylation. However, there was no increase in phosphorylase a in the I-strain hearts, whereas the control hearts showed a large increase. Assays of I-strain heart extracts showed a normal cyclic AMP-dependent protein kinase activity but no phosphorylase kinase activity. It is concluded that troponin I is phosphorylated in intact hearts by protein kinase and not phosphorylase kinase.


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