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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.