Kopustinskas A, Adaskevicius R, Krusinskas A, Kopustinskiene DM, Liobikas J, Toleikis A
Abstract:
We have developed an easy-to-use computer-based system for recording, displaying, storing and analyzing signals generated by Clark-type oxygen electrodes. A user-friendly interface of Windows-based program BioMed significantly increases the productivity of investigations. It allows to process, control, present and archive the experimental data in real time.
Liobikas J, Baniulis D, Stanys V, Toleikis A, Eriksson O.
Abstract:
We have searched through plant databases for nucleotide and protein sequences sharing a significant similarity to bacterial serine β-lactamases and metazoan LACTB. The search resulted in the identification of novel serine β-lactamase homologues in both Gymno- and Angiosperms.
The effect of exogenous cytochrome c on respiration rate of the rat and human heart mitochondria was assessed in situ, using permeabilized fibers. It was (i) much more pronounced in State 2 and 4 than in State 3 with all the respiratory substrates (pyruvate+malate, succinate, palmitoyl-CoA+carnitine and octanoyl-L-carnitine), (ii) different with different substrates, (iii) much higher after ischemia in both metabolic states, particularly in the case of succinate oxidation compared to pyruvate+malate, (iv) the highest in State 4 with succinate as a substrate.
Johans M, Milanesi E, Franck M, Johans C, Liobikas J, Panagiotaki M, Greci L, Principato G, Kinnunen PKJ, Bernardi P, Constantini P, Eriksson O
Abstract:
Methylglyoxal and synthetic glyoxal derivatives react covalently with arginine residue(s) on the mitochondrial permeability transition pore (PTP). In this study, we have investigated how the binding of a panel of synthetic phenylglyoxal derivatives influences the opening and closing of the PTP. Using both isolated mitochondria and mammalian cells, we demonstrate that the resulting arginine-phenylglyoxal adduct can lead to either suppression or induction of permeability transition, depending on the net charge and hydrogen bonding capacity of the adduct.
