Astaxanthin Protects Against HO- and Doxorubicin-Induced Cardiotoxicity in H9c2 Rat Myocardial Cells.

Astaxanthin (AST) is a carotenoid that has positive effects on various organs and tissues. It also exhibits a cardioprotective action. In this study, the influence of AST on the survival of H9c2 cardiomyocytes under hydrogen peroxide (HO)- and doxorubicin (DOX)-induced cardiotoxicity was investigated.

Astaxanthin Reduces HO- and Doxorubicin-Induced Cardiotoxicity in H9c2 Cardiomyocyte Cells.

Cardiovascular diseases are among the most challenging problems in clinical practice. Astaxanthin (AST) is a keto-carotenoid (xanthophyll) mainly of marine origin, which is able to penetrate the cell membrane, localize in mitochondria, and prevent mitochondrial dysfunction. In this study effect of astaxanthin on the death of H9c2 cardiomyocytes caused by the cytotoxic effect of hydrogen peroxide (HO) and doxorubicin (DOX) was examined.

Potential Targets for the Protective Effect of Astaxanthin on Ethanolinduced Damage in Rat Liver Mitochondria.

Background: Alcohol intoxication leads to multiple degenerative disorders in the structure and function of mitochondria. The mechanisms underlying these disorders, as well as ways to prevent them, are an urgent task in biomedicine. We investigate the mechanism of the positive effect of AX on rat liver mitochondria after chronic alcohol administration and suggest the targets of its effects.

[Melatonin Enhances the Effect of ABT-737 in Acute Monocytic Leukemia THP-1 Cells].

Melatonin (N-acetyl-5-methoxytryptamine, MEL) is a hormone synthesized by the pineal gland. Due to its oncostatic effect, it can be considered as an antitumor agent and used for combination therapy. ABT-737, a Bcl-2 inhibitor, promotes cell death after treatment with agents that induce pro-apoptotic signals.

Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca-Dependent Formation of Large Channels.

Monomers, dimers, and individual FF-ATP synthase subunits are, presumably, involved in the formation of the mitochondrial permeability transition pore (PTP), whose molecular structure, however, is still unknown. We hypothesized that, during the Ca-dependent assembly of a PTP complex, the F-ATP synthase (subunits) recruits mitochondrial proteins that do not interact or weakly interact with the F-ATP synthase under normal conditions. Therefore, we examined whether the PTP opening in mitochondria before the separation of supercomplexes via BN-PAGE will increase the channel stability and channel-forming capacity of isolated F-ATP synthase dimers and monomers in planar lipid membranes.