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Effect of palmitoylcarnitine on the cellular differentiation, proliferation and protein kinase C activity in neuroblastoma nb-2a

100%
Nalecz K. A., Mroczkowska J. E., Berent U., Nalecz M. J.
Acta Neurobiologiae Experimentalis
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1997
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vol. 57
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issue 4
263-274
EN
Palmitoylcarnitine is synthesized through the action of palmitoylcarnitine transferase I - an enzyme specifically inhibited by etomoxir. An increase of the intracellular content of palmitoylcarnitine in neuroblastoma NB-2a cells after administration of carnitine was correlated with an inhibition of cell proliferation and a concomitant promotion of differentiation processes. The activity of protein kinase C was measured in vivo, with cells permeabilized through the use of streptolysin O and a peptide substrate. Palmitoylcarnitine inhibited the phorbol ester stimulated reaction of the peptide phosphorylation in a concentration dependent way. The degree of protein kinase C inhibition was correlated with intracellular increase of the palmitoylcarnitine content, pointing to this compound as a natural modulator of protein kinase C activity.
2
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Mechanism of carnitine transport catalyzed by carnitine carrier from rat brain mitochondria

100%
Kaminska J., Nalecz K. A., Nalecz M. J.
Acta Neurobiologiae Experimentalis
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1995
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vol. 55
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issue 1
1-9
EN
The tramnsport mechanism of reconstituted carnitine carrier purified from rat brain mitochondria was studied kinectically.Short and medium chain acyl carnitine derivatives had much higher affinity to the carnitine carrier in comparison with long chain acyl carnitine derivatives, therefore both homologous (carnitine/carnitine) and heterologous (carnitine/acetylcarnitine) antiports were analysed. A complete set of half-saturation constans was established for various subsrtrate concentrations on both the external and internal side of the membrane.Bisubstrate initial velocity analyses of the exchange reaction in a kinetic pattern which is consistent with a sequential antiport mechanism.This type of mechanism implies formation of a ternary complex of the carrier with one internal and one external substrate molecule before the transport reaction occurs.
3
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Isulfhydryl reagents with K+ transport in adrenal chromaffin granules

76%
Szewczyk A., Lobanov N. A., Nowotny M., Nalecz M. J., Berent U., Mroczkowska J. E., Nalecz K. A.
Acta Neurobiologiae Experimentalis
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1997
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vol. 57
|
issue 4
329-332
EN
In the present study the functional role of SH groups in the Ca2+ -independent K+ selective channel activity in the membrane of bovine adrenal gland chromaffin granules has been studied. Ionic channel activity has been estimated using 86Rb+, a K+ analogue, flux measurements. The inhibition of chromaffin granules K+ channel by SH modifying agents, such as N ethylmaleimide, mersalyl and phenylarsenoxide, is described.
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