Palmitoylcarnitine regulates estrification of lipids and promotes palmitoylation of GAP-43 |
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Authors: | Nałecz Katarzyna A Szczepankowska Dorota Czeredys Magdalena Kulikova Natalia Grześkiewicz Stanisław |
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Affiliation: | Nencki Institute of Experimental Biology, Pasteur Street 3, 02-093 Warszawa, Poland. k.nalecz@nencki.gov.pl |
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Abstract: | Palmitoylcarnitine was previously shown to promote differentiation of neuroblastoma NB-2a cells. It was also observed to increase palmitoylation of several proteins and to diminish incorporation of palmitic acid to phospholipids, as well as to affect growth associated protein GAP-43 by decreasing its phosphorylation and interaction with protein kinase C. The present study was focused on influence of palmitoylcarnitine on palmitoylation of GAP-43 and lipid metabolism. Althought palmitoylcarnitine did not significantly affect the total phospholipids and fatty acid content, it increased incorporation of palmitate moiety to triacylglicerides and cholesterol esters, with a decrease of free cholesterol content. The presence of palmitoylcarnitine significantly increased the amount of covalently bound palmitate to GAP-43, which can regulate the signal transduction pathways. |
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Keywords: | BSA, bovine serum albumin BSTFA, N,O-bis-(trimethylsilil)-trifluoroacetamide CPT1, carnitine palmitoyltransferase I FID, flame ionization detection PBS, phosphate buffered saline PKC, protein kinase C PVDF, polivinylidene difluoride SDS, sodium dodecyl sulfate TMCS, trimethylchlorosilane |
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