Details

Autor(en) / Beteiligte

• DECKER, Robert S
• DECKER, Marlene L
• KULIKOVSKAYA, Irina
• NAKAMURA, Sakie
• LEE, Daniel C
• HARRIS, Kathleen
• KLOCKE, Francis J
• WINEGRAD, Saul

Titel

Myosin-binding protein C phosphorylation, myofibril structure, and contractile function during low-flow ischemia

Ist Teil von

• Circulation (New York, N.Y.), 2005-02, Vol.111 (7), p.906-912

Ort / Verlag

Hagerstown, MD: Lippincott Williams & Wilkins

Erscheinungsjahr

2005

Quelle

MEDLINE

Beschreibungen/Notizen

• Contractile dysfunction develops in the chronically instrumented canine myocardium after bouts of low-flow ischemia and persists after reperfusion. The objective of this study is to identify whether changes in the phosphorylation state of myosin-binding protein C (MyBP-C) are a potential cause of dysfunction. During low-flow ischemia, MyBP-C is dephosphorylated, and the number of actomyosin cross-bridges in the central core of the sarcomere decreases as thick filaments dissemble from the periphery of the myofibril. During reperfusion, MyBP-C remains dephosphorylated, and its degradation is accelerated. Dephosphorylation of MyBP-C may initiate changes in myofibril thick filament structure that decrease the interaction of myosin heads with actin thin filaments. Limiting the formation of actomyosin cross-bridges may contribute to the contractile dysfunction that is apparent after low-flow ischemia. Breakdown of MyBP-C during reperfusion may prolong myocardial stunning.