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.