Structural and functional changes in myocardial thin filaments in experimental hypothyrosis.

Fluorescence resonance energy transfer study revealed decreased intermonomer mobility of Ca-actin and Mg-actin filaments of myocardial myofibrils in myocardial dystrophy caused by diffuse endocrine disorders, e. g. hypothyrosis.

Effectiveness of combined treatment with superoxide dismutase and Reamberin during skin ischemia.

Experimental skin ischemia in rats was induced by suturing a skin fold on the back with a silk thread. Combined pretreatment with superoxide dismutase (intraperitoneally) and Reamberin (intravenously) in doses of 0.01 and 6.

Antinecrotic and antioxidant effects of superoxide dismutase during skin ischemia.

Antinecrotic activity of SOD was studied in rats with experimental skin ischemia. Treatment with SOD increased activity of endogenous SOD in skin homogenates (by 70 and 26% compared to the ischemic and intact skin, respectively). However, the rate of superoxide anion generation remained unchanged after SOD treatment.

Submolecular mechanisms underlying in vitro and in vivo effect of cardiac glycosides on contractile activity of myocardial myofibrils during heart failure.

The development of severe heart failure associated with toxicoallergic myocarditis is accompanied by profound structural and conformational changes in the outer domain of actin (major protein in a thin filament of cardiomyocyte sarcomere). These changes were revealed in subdomains 1 (Cys374 and Cys10) and 2 (Lys61 and Tyr69). Structural and conformational changes in the monomer and protomer of the actin thread during heart failure were energetically forbidden.

Structural and conformational changes in myocardial and erythrocyte actin during cardiac ischemia.

Structural and conformational changes in myocardial and erythrocyte actin during cardiac ischemia were studied by the method of fluorescence resonance energy transfer with highly selective fluorescent probes. In contrast to 15-min coronary artery occlusion, 120-min ischemia was accompanied by irreversible structural and conformational changes in the small domain of erythrocyte actin. Posttranslational changes during myocardial ischemia concerned the N- and C-terminal regions of actin and went beyond the allowed conformational fluctuations in the actin molecule without breaking the energy barrier.