Protein Kinase C Phosphorylation of Cardiac Troponin I and Troponin T Inhibits Ca2+-Stimulated MgATPase Activity in Reconstituted Actomyosin and Isolated Myofibrils, and Decreases Actin-Myosin Interactions

1993 ◽  
Vol 25 (1) ◽  
pp. 53-65 ◽  
Author(s):  
Thomas A. Noland ◽  
J.F. Kuo
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Troponin T ◽  
Cardiac Troponin I ◽  
Kinase C ◽  
Mgatpase Activity

scholarly journals Phosphorylation Specificities of Protein Kinase C Isozymes for Bovine Cardiac Troponin I and Troponin T and Sites within These Proteins and Regulation of Myofilament Properties

1996 ◽  
Vol 271 (38) ◽  
pp. 23277-23283 ◽  
Author(s):  
Nathan M. Jideama ◽  
Thomas A. Noland ◽  
Robert L. Raynor ◽  
Gerard C. Blobe ◽  
Doriano Fabbro ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Troponin T ◽  
Cardiac Troponin I ◽  
Kinase C

scholarly journals Protein kinase C phosphorylation of cardiac troponin T decreases Ca2+-dependent actomyosin MgATPase activity and troponin T binding to tropomyosin-F-actin complex

1992 ◽  
Vol 288 (1) ◽  
pp. 123-129 ◽  
Author(s):  
T A Noland ◽  
J F Kuo
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Troponin ◽  
Thin Filament ◽  
Phorbol Esters ◽  
Troponin T ◽  
Cardiac Troponin T ◽  
Kinase C ◽  
Inotropic Responses ◽  
Mgatpase Activity

Effects of phosphorylation of bovine cardiac troponin T (TnT) by protein kinase C on the Ca(2+)-stimulated MgATPase activity of reconstituted actomyosin complex and the binding of TnT to tropomyosin(Tm)-F-actin were investigated. The Ca(2+)-stimulated MgATPase of actomyosin containing phosphorylated TnT (1.8 mol of P/mol), compared with that containing unphosphorylated TnT, was decreased by up to 48%. Phosphorylation of TnT also decreased (up to 48%) its maximum binding to Tm-F-actin, which was accompanied by a decrease (up to 3.5-fold) in its apparent binding affinity. The findings indicate that the effects of phosphorylated TnT in decreasing actomyosin MgATPase might be secondary to its decreased interactions with the other components of the thin filament, representing a new mechanism underlying the negative inotropic responses of various cardiac preparations to protein kinase C-activating phorbol esters.

scholarly journals Phosphorylation of Cardiac Troponin I at Protein Kinase C Site Threonine 144 Depresses Cooperative Activation of Thin Filaments

2010 ◽  
Vol 285 (16) ◽  
pp. 11810-11817 ◽  
Author(s):  
Qun-Wei Lu ◽  
Aaron C. Hinken ◽  
Stacey E. Patrick ◽  
R. John Solaro ◽  
Tomoyoshi Kobayashi
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Thin Filaments ◽  
Kinase C ◽  
Cooperative Activation

scholarly journals Tyrosine Phosphorylation Modifies Protein Kinase C δ-dependent Phosphorylation of Cardiac Troponin I

2008 ◽  
Vol 283 (33) ◽  
pp. 22680-22689 ◽  
Author(s):  
Marius P. Sumandea ◽  
Vitalyi O. Rybin ◽  
Aaron C. Hinken ◽  
Chaojian Wang ◽  
Tomoyoshi Kobayashi ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Kinase C
Sign in / Sign up

Export Citation Format

Share Document