Calcium ionophore A23187 induction of spermidine/spermine N1-acetyltransferase activity in bovine lymphocytes.
The divalent cation ionophore A23187 increased the activity in bovine lymphocytes of spermidine/spermine N1-acetyltransferase, a rate-limiting enzyme in polyamine biodegradation. The enzyme was induced in a dose- and time-dependent manner. Induction was suppressed by indomethacin, but not by trifluoperazine (TFP), N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7) or palmitoylcarnitine. These results suggest that the activation of phospholipase A2 involves the induction of spermidine/spermine N1-acetyltransferase. Ornithine decarboxylase, a rate-limiting enzyme in polyamine biosynthesis, was not suppressed by indomethacin but was by TFP and W-7. The molecular mechanism of the induction of spermidine/spermine N1-acetyltransferase and ornithine decarboxylase may be different.
D000123:Acetyltransferases / Q000096:biosynthesis / Q000097:blood*; D000818:Animals; D000001:Calcimycin / Q000494:pharmacology*; D002417:Cattle; D004790:Enzyme Induction / Q000187:drug effects; D007213:Indomethacin / Q000494:pharmacology; D008214:Lymphocytes / Q000201:enzymology*; D009955:Ornithine Decarboxylase / Q000097:blood; D010172:Palmitoylcarnitine / Q000494:pharmacology; D000099228:Diamine N-Acetyltransferase
D000123:Acetyltransferases; D000001:Calcimycin; D007213:Indomethacin; D009955:Ornithine Decarboxylase; D010172:Palmitoylcarnitine; D000099228:Diamine N-Acetyltransferase