scholarly journals Protein Kinase D Is a Novel Mediator of Cardiac Troponin I Phosphorylation and Regulates Myofilament Function

2004 ◽  
Vol 95 (11) ◽  
pp. 1091-1099 ◽  
Author(s):  
Robert S. Haworth ◽  
Friederike Cuello ◽  
Todd J. Herron ◽  
Gereon Franzen ◽  
Jonathan C. Kentish ◽  
...  
2007 ◽  
Vol 100 (6) ◽  
pp. 864-873 ◽  
Author(s):  
Friederike Cuello ◽  
Sonya C. Bardswell ◽  
Robert S. Haworth ◽  
Xiaoke Yin ◽  
Susanne Lutz ◽  
...  

2013 ◽  
Vol 104 (2) ◽  
pp. 155a ◽  
Author(s):  
Paul J.M. Wijnker ◽  
D. Brian Foster ◽  
Anne M. Murphy ◽  
Ger J.M. Stienen ◽  
Jolanda van der Velden

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.


2010 ◽  
Vol 98 (3) ◽  
pp. 358a
Author(s):  
Viola Kooij ◽  
Sander R. Piersma ◽  
Kay W. Tang ◽  
Conny R. Jiménez ◽  
Pingbo Zang ◽  
...  

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