SEQUENCE AND STRUCTURE OF A HUMAN GLUCOSE TRANSPORTER
SEQUENCE AND STRUCTURE OF A HUMAN GLUCOSE TRANSPORTER
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DOI：
10.1126/science.3839598
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发表时间：
1985-01-01
期刊：
影响因子：
56.9
通讯作者：
LODISH, HF
中科院分区：
文献类型：
--
作者：
MUECKLER, M;CARUSO, C;LODISH, HF
人 HepG2 肝癌细胞的葡萄糖转运蛋白的氨基酸序列是通过对互补 DNA 克隆的分析推导出来的。通过快原子轰击图谱和气相 Edman 降解对纯化的人红细胞葡萄糖转运蛋白进行结构分析，证实了克隆的身份，并证明 HepG2 和红细胞转运蛋白高度同源，可能是相同的。该蛋白质缺乏可切割的氨基末端信号序列。一级结构分析表明存在 12 个跨膜结构域。其中一些可以形成两亲性α。螺旋并含有丰富的羟基和酰胺侧链，可以参与葡萄糖结合或排列糖移动通过的跨膜孔。预计蛋白质中心的氨基末端、羧基末端和高度亲水的结构域都位于细胞质面上。在 K562 白血病细胞、HT29 结肠腺癌细胞和人肾组织中检测到与 HepG2 葡萄糖转运蛋白信使 RNA 同源的信使 RNA 种类。
The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic .alpha. helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.