Heme-induced contractile dysfunction in Human cardiomyocytes caused by oxidant damage to thick filament proteins
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文摘

Binding of heme to MLC-1 initiate.

Five fold increase in Ca2+-independent passive force and decrease in Ca2+-regulated maximal activity by 90% permeabilized in human cardiomyocytes.

Heme-mediated SH oxidation of titin, α-actinin, filamin C, myosin heavy chain, and cardiac myosin binding protein C contributing to deterioration of cardiac force generation.

Heme-evoked stable sulfenic acid formation in myosin heavy chain, cardiac myosin binding protein C, and α-actinin, which was not reversed by DTT, probably contributing to the physiological effects.

Binding of heme to hemopexin or alpha-1-microglobulin prevented its effects on cardiomyocyte contractility.

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