The hybrid rat cytochrome P450 containing the first 5 exons of the CYP11B1 and last 4 exons from the CYP11B2 enzyme retains 11 beta-hydroxylase activity, but the alternative hybrid is inactive.
The hybrid rat cytochrome P450 containing the first 5 exons of the CYP11B1 and last 4 exons from the CYP11B2 enzyme retains 11 beta-hydroxylase activity, but the alternative hybrid is inactive.
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含有 CYP11B1 前 5 个外显子和 CYP11B2 酶后 4 个外显子的杂交大鼠细胞色素 P450 保留了 11 β-羟化酶活性，但替代杂交体没有活性。
DOI：
10.1006/bbrc.1994.1204
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发表时间：
1994
影响因子：
3.1
通讯作者：
Foecking,MF
中科院分区：
文献类型：
--
作者：
Zhou,MY;Gomez-Sanchez,CE;Xue,D;Foecking,MF
人、小鼠和大鼠肾上腺皮质有2种不同的细胞色素P-450 11β-羟化酶。经典的大鼠11β-羟化酶或CYP11B1酶将脱氧皮质酮羟化为皮质酮和18-羟脱氧皮质酮，并分布于整个肾上腺。第二醛固酮合成酶或CYP11B2酶位于肾小球带，将去氧皮质酮转化为皮质酮、18-羟皮质酮和醛固酮。大鼠CYP11B1和CYP11B2基因的编码核苷酸序列和推导出的氨基酸序列同源性分别为88%和83%。我们通过交换大鼠CYP11B1和CYP11B2在5/6外显子交界处的两个片段，构建了两种不同的杂交cdna，并在COS 7细胞中表达。杂交CYPH11B1构建体在表达时包含CYP11B1的前5个外显子，保留11β-羟化酶活性，但不能将皮质酮加工成18-羟基皮质酮或醛固酮。含有CYP11B2酶前5个外显子的杂交CYPH11B2构建体在表达时是无活性的。
Human, mouse and rats have 2 different cytochrome P-450 11β-hydroxylases in the adrenal cortex. The classical rat 11β-hydroxylase or CYP11B1 enzyme hydroxylates deoxycorticosterone to corticosterone and 18-hydroxydeoxycorticosterone and is located throughout the adrenal. The second aldosterone synthase or CYP11B2 enzyme is located in the zona glomerulosa and converts deoxycorticosterone to corticosterone, 18-hydroxycorticosterone and aldosterone. In rat the coding nucleotide sequence and the deduced amino acid sequences of the CYP11B1 and CYP11B2 genes are homologous by 88% and 83%,respectively. We have constructed two different hybrid cDNAs by exchanging two fragments of the rat CYP11B1 and CYP11B2 at the junction of the 5/6 exon and expressed them in COS 7 cells. The hybrid CYPH11B1 construct containing the first 5 exons of the CYP11B1 when expressed, retains 11β-hydroxylase activity, but cannot process corticosterone to 18-hydroxycorticosterone or aldosterone. The hybrid CYPH11B2 construct containing the first 5 exons of the CYP11B2 enzyme when expressed is inactive.