来自杜氏利什曼原虫的肌醇/氢离子同向转运体的功能表达。
Functional expression of a myo-inositol/H+ symporter from Leishmania donovani.
作者信息
Drew M E, Langford C K, Klamo E M, Russell D G, Kavanaugh M P, Landfear S M
机构信息
Department of Molecular Microbiology and Immunology, Oregon Health Sciences University, Portland 97201, USA.
出版信息
Mol Cell Biol. 1995 Oct;15(10):5508-15. doi: 10.1128/MCB.15.10.5508.
Abstract
The vast majority of surface molecules in such kinetoplastid protozoa as members of the genus Leishmania contain inositol and are either glycosyl inositol phospholipids or glycoproteins that are tethered to the external surface of the plasma membrane by glycosylphosphatidylinositol anchors. We have shown that the biosynthetic precursor for these abundant glycolipids, myo-inositol, is translocated across the parasite plasma membrane by a specific transporter that is structurally related to mammalian facilitative glucose transporters. This myo-inositol transporter has been expressed and characterized in Xenopus laevis oocytes. Two-electrode voltage clamp experiments demonstrate that this protein is a sodium-independent electrogenic symporter that appears to utilize a proton gradient to concentrate myo-inositol within the cell. Immunolocalization experiments with a transporter-specific polyclonal antibody reveal the presence of this protein in the parasite plasma membrane.
摘要
在诸如利什曼原虫属成员这类动基体原生动物中，绝大多数表面分子都含有肌醇，并且要么是糖基肌醇磷脂，要么是通过糖基磷脂酰肌醇锚定连接到质膜外表面的糖蛋白。我们已经表明，这些丰富糖脂的生物合成前体——肌醇，是通过一种与哺乳动物易化葡萄糖转运体结构相关的特定转运体跨寄生虫质膜转运的。这种肌醇转运体已在非洲爪蟾卵母细胞中表达并进行了特性鉴定。双电极电压钳实验表明，该蛋白是一种不依赖钠的生电同向转运体，似乎利用质子梯度将肌醇浓缩在细胞内。用转运体特异性多克隆抗体进行的免疫定位实验揭示了该蛋白在寄生虫质膜中的存在。
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