[HTML][HTML] Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity
EM Burkart, MP Sumandea, T Kobayashi, M Nili… - Journal of Biological …, 2003 - ASBMB
There is evidence that multi-site phosphorylation of cardiac troponin I (cTnI) by protein
kinase C is important in both long-and short-term regulation of cardiac function. To
determine the specific functional effects of these phosphorylation sites (Ser-43, Ser-45, and
Thr-144), we measured tension and sliding speed of thin filaments in reconstituted
preparations in which endogenous cTnI was replaced with cTnI phosphorylated by protein
kinase C-ε or mutated to cTnI-S43E/S45E/T144E, cTnI-S43E/S45E, or cTnI-T144E. We used …
kinase C is important in both long-and short-term regulation of cardiac function. To
determine the specific functional effects of these phosphorylation sites (Ser-43, Ser-45, and
Thr-144), we measured tension and sliding speed of thin filaments in reconstituted
preparations in which endogenous cTnI was replaced with cTnI phosphorylated by protein
kinase C-ε or mutated to cTnI-S43E/S45E/T144E, cTnI-S43E/S45E, or cTnI-T144E. We used …