Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K
Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K
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DOI：
10.1006/bbrc.1997.6495
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发表时间：
1997-04-17
影响因子：
3.1
通讯作者：
Fry, MJ
中科院分区：
文献类型：
--
作者：
Brown, RA;Ho, LKF;Fry, MJ
磷脂酰肌醇（PI）S-激酶已被证明在信号转导，细胞转化和细胞内蛋白质运输中具有关键作用。逆转录聚合酶链反应方法，使用简并引物来自脂质激酶的共识区，被用来确定PIS-激酶在正常人乳腺。在这里，我们报告了一个新的人PI 3-激酶亚型，HsC 2-PI 3 K的cDNA克隆。该PI 3-激酶与最近描述的包含C2结构域的PI 3-激酶家族最密切相关，该PI 3-激酶家族包括果蝇PI 3K_68D/cpk和鼠cpk-m/p170。序列分析表明，HsC 2-PI 3 K是第二个不同的哺乳动物成员的C2域含有PI 3激酶家族。北方印迹分析表明HsC 2-PI 3 K在人体组织中广泛表达。荧光原位杂交已将HsC 2-PI 3 K定位于染色体1 q32。(C)北京：科学出版社.
Phosphoinositide (PI) S-kinases have been shown to have critical roles in signal transduction, cell transformation and intracellular protein trafficking. Reverse-transcription polymerase chain reaction methods, using degenerate primers derived from the lipid kinase consensus region, were utilised to identify PI S-kinases in the normal human breast. Here we report the cDNA cloning of a novel human PI 3-kinase isoform, HsC2-PI3K. This PI 3-kinase is most closely related to the recently described C2 domain-containing family of PI 3-kinases which includes Drosophila PI3K_68D/cpk and murine cpk-m/p170. Sequence analysis suggests that HsC2-PI3K is a second distinct mammalian member of the C2 domain-containing PI 3-kinase family. Northern blot analysis of human tissues indicates that HsC2-PI3K is widely expressed. Fluorescence in situ hybridisation has mapped HsC2-PI3K to chromosome 1q32. (C) 1997 Academic Press.