Rhodamine 123 staining, light and electron microscopy were used to evaluate the ultrastructural and functional state of cultured cerebellar granule cells after short treatment with the solution where NaCl was substituted by sucrose (sucrose balance salt medium, SBSM). Cell exposure to SBSM for 20 min resulted in the fact that mitochondria in the neurons lost their ability to sequester rhodamine 123. This effect could be prevented by : (i) non-competitive N-methyl-D-aspartate (NMDA) receptor channel blocker, 1035 M MK-801; (ii) a competitive specific antagonist of NMDA glutamate receptors,33 M cobalt chloride; (iv) removal of Ca 2+ from the medium. Low Na + in the Ca 2+ -containing medium caused considerable mitochondrial swelling in granule cells. However, the same treatment in the absence of calcium ions in the medium abolished the deleterious effect of SBSM on the neuronal mitochondrial structure and functions. It is suggected that (i) the exposure of cultured cerebellar granule cells to SBSM leads to a release of endogenous glutamate from cells; (ii) Ca 2+ ions potentially deenergizing neuronal mitochondria enter the neuron preferentially through the NMDA channels rather than through the Na + /Ca 2+ exchanger; (iii) mitochondrial swelling in granule cells is highly Ca 2+ -dependent; (iv) cellular overload with sodium ions can activate mitochondrial Na + /Ca 2+ exchanger and thus prevent permeability transition pore opening in mitochondria.z 1998 Federation of European Biochemical Societies.
Isolated rat liver mitochondria undergo permeability transition after supplementation with a suspension of tobacco mosaic virus. Four mitochondrial parameters proved the opening of the permeability transition pore in the inner mitochondrial membrane : increased oxygen consumption, collapse of the membrane potential, release of calcium ions from mitochondria, and high amplitude mitochondrial swelling. All virus-induced changes in mitochondria were prevented by cyclosporin A. These effects were not observed if the virus was treated with EGTA or disrupted by heating. Protein component of the virus particle in the form of 20S aggregate A-protein, or helical polymer, as well as supernatant of the heat-disrupted virus sample, had no effect on mitochondrial functioning. Electron microscopy revealed the direct interaction of the virus particles with isolated mitochondria. The possible role of the mitochondrial permeability transition pore in virus-induced apoptosis is discussed.z 2000 Federation of European Biochemical Societies.
Bei der Phosphorylierung von Nucleosiden ist es schwer, das Phosphorylierungsprodukt mit guter Ausbeute von den Ausgangs‐ und Nebenprodukten zu trennen.
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