Modulation by palmitoyl-carnitine of calcium activated, phospholipid-dependent protein kinase activity and inhibition of melanoma cell growth.
Phospholipid-sensitive, Ca++-dependent protein kinase activity was investigated in the cytosol of melanoma cells. A protein kinase system was partially purified, and enzyme activity was found to be modulated by palmitoyl-carnitine. In order to link the actions of palmitoyl-carnitine on phospholipid-sensitive protein kinase activity and the already reported role of protein kinase C in cell division, we studied the action of palmitoyl-carnitine on melanoma cell growth by measuring colony forming ability in a soft agar culture system. Palmitoyl-carnitine was found to inhibit cell growth in a dose-dependent manner. These findings suggest that palmitoyl-carnitine (or long-chain acylcarnitine), a naturally occurring metabolite, may play a key role in the onset of cell division. We suggest that the action of palmitoyl-carnitine on phospholipid-dependent protein kinase activity is in part related to the molecular events linking protein kinase C activity and the ionic events in the initiation of cell growth.
Vescovi
G
G
Laboratoire de Biochimie, Faculté de Médecine, Université de Nancy, France.
Weber
B
B
Matrat
M
M
Ramacci
C
C
Nabet
P
P
Kremer
B
B
D000328:Adult; D002331:Carnitine / Q000031:analogs & derivatives*; D002470:Cell Survival / Q000187:drug effects; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D008297:Male; D008545:Melanoma / Q000201:enzymology* / Q000473:pathology; D010172:Palmitoylcarnitine / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D014410:Tumor Stem Cell Assay
D010172:Palmitoylcarnitine; D011493:Protein Kinase C; D002331:Carnitine