SPPL3-dependent downregulation of the synthesis of (neo)lacto-series glycosphingolipid is required for the staining of cell surface CD59
SPPL3-dependent downregulation of the synthesis of (neo)lacto-series glycosphingolipid is required for the staining of cell surface CD59
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DOI：
10.1016/j.bbrc.2021.06.093
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发表时间：
2021-07-23
影响因子：
3.1
通讯作者：
Goto, Satoshi
中科院分区：
文献类型：
--
作者：
Kawaguchi, Kohei;Yamamoto-Hino, Miki;Goto, Satoshi
CD59是一种小糖蛋白，经糖磷脂酰肌醇（GPI）锚点修饰，可防止膜攻击复合物的形成，从而保护宿主细胞免受裂解。先前的研究发现细胞表面CD59染色需要膜内蛋白酶信号肽肽酶样3 （SPPL3）。然而，SPPL3对CD59染色的影响尚不清楚。这项研究表明，SPPL3对于CD59的表面标记是必需的，而不是主要的gpi锚定蛋白的表面标记。表面CD59染色需要SPPL3的膜内蛋白酶活性和SPPL3介导的（neo）乳系列鞘糖脂（nsGSLs）的抑制，但不需要n -聚糖合成途径。nsGSLs的丰度可能通过改变细胞表面CD59的丰度或可及性来影响补体依赖性细胞毒性。(c) 2021爱思唯尔公司版权所有。
CD59 is a small glycoprotein modified with a glycophosphatidylinositol (GPI) anchor that prevents the formation of the membrane attack complex, thereby protecting host cells from lysis. A previous study identified that cell surface CD59 staining required the intramembrane protease signal peptide peptidase like 3 (SPPL3). However, the effect of SPPL3 on the staining of CD59 remains unknown. This study shows that SPPL3 is essential for the surface labeling of CD59 but not of major GPI-anchored proteins. Surface CD59 staining requires the intramembrane protease activity of SPPL3 and SPPL3-mediated suppression of the (neo)lacto-series glycosphingolipids (nsGSLs)dbut not N-glycandsynthesis pathway. The abundance of nsGSLs may affect complement-dependent cytotoxicity by altering the abundance or accessibility of cell surface CD59. (c) 2021 Elsevier Inc. All rights reserved.