Spermidine N1-acetyltransferase has a larger role than ornithine decarboxylase in 1 alpha,25-dihydroxyvitamin D3-induced putrescine synthesis.
Spermidine N1-acetyltransferase has a larger role than ornithine decarboxylase in 1 alpha,25-dihydroxyvitamin D3-induced putrescine synthesis.
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亚精胺 N1-乙酰转移酶在 1α,25-二羟基维生素 D3 诱导的腐胺合成中比鸟氨酸脱羧酶具有更大的作用。
DOI：
10.1016/s0021-9258(18)67302-8
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
T. Suda
中科院分区：
文献类型：
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作者：
T. Shinki;T. Kadofuku;Tsuneo Sato;T. Suda
我们已经报道，将1 α，25-二羟基维生素D3（1 α，25（OH）2D 3）（维生素D3的活性形式）单次注射到维生素D缺乏的雏鸡中，通过两种途径（一种来自鸟氨酸，一种来自亚精胺）产生十二指肠腐胺形成的显著增加（Shinki，T.，Takahashi，N.，Kadofuku，T.，佐藤，T.，和苏达，T.（1985）J.Biol.Chem.260，2185-2190）。本工作比较了鸟氨酸脱羧酶催化[~ 3 H]鸟氨酸转化为[~ 3 H]腐胺与亚精胺N1-乙酰转移酶和多胺氧化酶催化[~（14）C]亚精胺转化为[~（14）C]腐胺的反应。使用原位十二指肠袢法在存在或不存在α-二氟甲基鸟氨酸，我们评估了这两个途径的相对贡献，在1 α，25（OH）2D 3-诱导的十二指肠合成腐胺。α-二氟甲基鸟氨酸的预先给药既不抑制1 α，25（OH）2D 3诱导的十二指肠亚精胺N1-乙酰转移酶活性的增加，也不抑制维生素诱导的十二指肠腐胺含量的增加，尽管它完全抑制了1 α，25（OH）2D 3诱导的十二指肠鸟氨酸脱羧酶活性。注射1 α，25（OH）2D 3后，亚精胺的十二指肠含量呈时间依赖性下降。增加十二指肠腐胺的1 α，25（OH）2D 3符合定量的腐胺合成亚精胺，但不是从鸟氨酸注射后的维生素。这些意想不到的结果清楚地表明，亚精胺N1-乙酰转移酶在1 α，25（OH）2D 3诱导的十二指肠腐胺合成增加中具有比鸟氨酸脱羧酶更大的作用。本文报道的多胺代谢可能与肠上皮细胞的特征有关，如短寿命（90-108 h）和典型的从隐窝到绒毛区的分化梯度。
We have reported that a single injection of 1 alpha,25-dihydroxyvitamin D3 (1 alpha,25(OH)2D3), the active form of vitamin D3, into vitamin D-deficient chicks produces a marked increase in the formation of duodenal putrescine by two pathways, one from ornithine and one from spermidine (Shinki, T., Takahashi, N., Kadofuku, T., Sato, T., and Suda, T. (1985) J. Biol. Chem. 260, 2185-2190). In this work, the conversion of [3H]ornithine into [3H]putrescine catalyzed by ornithine decarboxylase was compared with the conversion of [14C]spermidine into [14C]putrescine catalyzed by spermidine N1-acetyltransferase and polyamine oxidase. Using the in situ duodenal loop method in the presence or absence of alpha-difluoromethylornithine, we evaluated the relative contributions of these two pathways in the 1 alpha,25(OH)2D3-induced duodenal synthesis of putrescine. Prior administration of alpha-difluoromethylornithine inhibited neither the 1 alpha,25(OH)2D3-induced increase in duodenal spermidine N1-acetyltransferase activity nor the vitamin-induced enhancement of the duodenal putrescine content, although it completely suppressed the duodenal ornithine decarboxylase activity induced by 1 alpha,25(OH)2D3. The duodenal content of spermidine decreased time-dependently after injection of 1 alpha,25(OH)2D3. The increase of duodenal putrescine by 1 alpha,25(OH)2D3 coincided quantitatively with the amount of putrescine synthesized from spermidine but not from ornithine after injection of the vitamin. These unexpected results clearly indicate that spermidine N1-acetyltransferase has a larger role than ornithine decarboxylase in the increase of duodenal putrescine synthesis induced by 1 alpha,25(OH)2D3. The polyamine metabolism reported here may be related to the characteristics of intestinal epithelial cells such as the short lifetime (90-108 h) and typical gradient of differentiation from the crypt to villus regions.