Effect of palmitoylcarnitine on the cellular differentiation, proliferation and protein kinase C activity in neuroblastoma nb-2a
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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.
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K.A. Nalecz, Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, 3 Pasteur St., 02-093 Warsaw, Poland, Email: firstname.lastname@example.org