Vidugiriene J, Menon A K
Laboratory of Molecular Parasitology, Rockefeller University, New York 10021-6399.
J Cell Biol. 1993 Jun;121(5):987-96. doi: 10.1083/jcb.121.5.987.
Glycosylated phosphoinositides serve as membrane anchors for numerous eukaryotic cell surface glycoproteins. Recent biochemical and genetic studies indicate that the glycolipids are assembled by sequential addition of components (monosaccharides and phosphoethanolamine) to phosphatidylinositol. The biosynthetic steps are presumed to occur in the ER, but formal proof of this is lacking. We describe experiments designed to establish the subcellular location of the initial steps in glycosyl-phosphatidylinositol (GPI) anchor biosynthesis and to define the transmembrane distribution of early biosynthetic lipid intermediates. The experiments were performed with the thymoma cell line BW5147.3. A subcellular fractionation protocol was used to show that early biosynthetic steps in GPI assembly, i.e., synthesis and deacetylation of N-acetylglucosaminyl phosphatidylinositol, occur in the ER. GPI biosynthetic intermediates were synthesized by incubating the microsomes with UDP-[3H]GlcNAc, and the transmembrane distribution of the labeled lipids was probed with phosphatidylinositol-specific phospholipase C (PI-PLC). Treatment of the radiolabeled microsomes with PI-PLC showed that > 70% of the N-acetylglucosaminyl phosphatidylinositol and glucosaminyl phosphatidylinositol could be hydrolyzed, indicating that the two lipids were primarily distributed in the cytoplasmic (outer) leaflet of the microsomes. Similar cleavage results were obtained using Streptolysin O-permeabilized thymoma cells. When permeabilized cells were incubated with UDP-[3H]GlcNAc and treated with PI-PLC, approximately 85% of the radiolabeled N-acetylglucosaminyl phosphatidylinositol and glucosaminyl phosphatidylinositol could be cleaved, indicating that they were accessible to the enzyme. The cumulative data indicate that early GPI intermediates are primarily located in the cytoplasmic leaflet of the ER, and are probably synthesized from PI located in the cytoplasmic leaflet and UDP-GlcNAc synthesized in the cytosol.
糖基化磷脂酰肌醇作为众多真核细胞表面糖蛋白的膜锚定物。最近的生化和遗传学研究表明,糖脂是通过将成分(单糖和磷酸乙醇胺)顺序添加到磷脂酰肌醇上而组装而成的。生物合成步骤推测发生在内质网中,但缺乏对此的正式证据。我们描述了旨在确定糖基磷脂酰肌醇(GPI)锚定生物合成初始步骤的亚细胞定位并定义早期生物合成脂质中间体跨膜分布的实验。实验是用胸腺瘤细胞系BW5147.3进行的。采用亚细胞分级分离方案表明,GPI组装的早期生物合成步骤,即N-乙酰葡糖胺基磷脂酰肌醇的合成和脱乙酰化,发生在内质网中。通过将微粒体与UDP-[3H]GlcNAc孵育来合成GPI生物合成中间体,并用磷脂酰肌醇特异性磷脂酶C(PI-PLC)探测标记脂质的跨膜分布。用PI-PLC处理放射性标记的微粒体表明,>70%的N-乙酰葡糖胺基磷脂酰肌醇和葡糖胺基磷脂酰肌醇可以被水解,这表明这两种脂质主要分布在微粒体的细胞质(外)小叶中。使用链球菌溶血素O通透的胸腺瘤细胞也获得了类似的切割结果。当通透细胞与UDP-[3H]GlcNAc孵育并用PI-PLC处理时,约85%的放射性标记的N-乙酰葡糖胺基磷脂酰肌醇和葡糖胺基磷脂酰肌醇可以被切割,这表明它们可被该酶作用。累积数据表明,早期GPI中间体主要位于内质网的细胞质小叶中,可能由位于细胞质小叶中的PI和在细胞质中合成的UDP-GlcNAc合成。