Induction of spermidine N1-acetyltransferase by 1 alpha,25-dihydroxyvitamin D3 as an early common event in the target tissues of vitamin D

• Published in: The Journal of biological chemistry Vol. 260; no. 4; pp. 2185 - 2190
• Main Authors: Shinki, T, Takahashi, N, Kadofuku, T, Sato, T, Suda, T
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.02.1985; American Society for Biochemistry and Molecular Biology
• Subjects: Acetyltransferases - biosynthesis; Animals; Biological and medical sciences; Calcifediol - pharmacology; Calcitriol - pharmacology; Chickens; Dose-Response Relationship, Drug; Duodenum - enzymology; Enzyme Induction - drug effects; Fundamental and applied biological sciences. Psychology; Intestine. Mesentery; Kinetics; Male; Ornithine Decarboxylase - metabolism; Putrescine - metabolism; Spermidine - metabolism; Tissue Distribution; Vertebrates: digestive system; Vitamin D Deficiency - enzymology; Polyamine; Duodenum; Digestive system; Enzyme; Gut; Biosynthesis; Metabolism; Small intestine; Cholecalciferol(dihydroxy-1,25); Vertebrata; Amine; Vitamin D; Spermidine; Spermidine N-acetyltransferase; Chicken; Aves
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)89535-7

We have reported that the duodenal ornithine decarboxylase activity and the tissue content of putrescine increase markedly after a single intravenous injection of 1 alpha,25-dihydroxyvitamin D3 (1 alpha,25(OH)2D3) into vitamin D-deficient chicks (Shinki, T., Takahashi, N., Miyaura, C., Samejima, K., Nishii, Y., and Suda, T. (1981) Biochem. J. 195, 685-690). In the present study, we examined in the same experimental system the effect of 1 alpha,25(OH)2D3 on the activity of duodenal spermidine N1-acetyltransferase, a rate-limiting enzyme catalyzing the conversion from spermidine to putrescine. The duodenal spermidine N1-acetyltransferase activity began to increase 30 min after a single intravenous injection of 625 ng of 1 alpha,25(OH)2D3 and attained a maximum in 2 h. As little as 1.25 ng of 1 alpha,25(OH)2D3 induced a small but significant increase in the spermidine N1-acetyltransferase activity, and the maximal response was obtained by 125 ng of the vitamin. The dose levels of 1 alpha,25(OH)2D3 required to induce duodenal spermidine N1-acetyltransferase activity were only one-tenth as much as those required to induce ornithine decarboxylase activity. The spermidine N1-acetyltransferase activity was induced commonly in the target tissues of vitamin D, whereas ornithine decarboxylase activity occurred only in intestine. The 1 alpha,25(OH)2D3-induced spermidine N1-acetyltransferase activity was greatly inhibited by prior administration of actinomycin D or cycloheximide. When 30,000 X g intestinal supernatants were incubated with [14C]spermidine, [14C]putrescine was formed. These results clearly indicate that the induction of spermidine N1-acetyltransferase activity is the 1 alpha,25(OH)2D3-induced earliest de novo synthesis in several proteins induced by the vitamin reported to date and that the 1 alpha,25(OH)2D3-induced duodenal synthesis of putrescine occurs by the pathways from both ornithine and spermidine.