ASYMMETRIC ACETYLCHOLINESTERASE IS ASSEMBLED IN THE GOLGI-APPARATUS
ASYMMETRIC ACETYLCHOLINESTERASE IS ASSEMBLED IN THE GOLGI-APPARATUS
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DOI：
10.1073/pnas.81.2.479
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发表时间：
1984-01-01
期刊：
影响因子：
--
通讯作者：
ROTUNDO, RL
中科院分区：
文献类型：
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作者：
ROTUNDO, RL
用凝集素区分不同亚细胞区室中的乙酰胆碱酯酶分子，研究了鹌鹑肌肉培养物中多种分子形式的乙酰胆碱酯酶的合成、组装和加工。特别强调了不对称AcChoEase分子的组装，因为这些似乎是脊椎动物神经肌肉接头处AcChoEase的主要（如果不是唯一的）形式。所有细胞表面和分泌的AcChoEase形式结合固定的麦胚凝集素，蓖麻毒素和伴刀豆球蛋白A，表明它们具有复杂的寡糖。在用膜可渗透的不可逆AcChoEase抑制剂处理肌细胞后，存在球状单体、二聚体和四聚体AcChoEase形式的快速再现。然而，胶原蛋白尾不对称形式直到. apprx才出现。处理后90 min。AcChoEase低聚糖与凝集素的分析表明在90分钟的时间内成熟为复杂的形式。大部分细胞内球状AcChoEase分子仅与伴刀豆球蛋白A结合，表明它们在粗面内质网中组装。相比之下，所有细胞内不对称AcChoEase结合麦胚凝集素，和一个显着的分数结合蓖麻毒素，表明这种独特的AcChoEase形式是从亚基组装，以前获得的复合糖。装配的不对称AcChoEase，因此收购的信息指定基板定位，显然发生在高尔基体。
The synthesis, assembly and processing of the multiple molecular forms of acetylcholinesterase in quail muscle cultures was studied by using lectins to distinguish enzyme molecules residing in different subcellular compartments. special emphasis was given to the assembly of asymmetric AcChoEase molecules because these appear to be the predominant, if not unique, forms of AcChoEase at the vertebrate neuromuscular junction. All cell surface and secreted AcChoEase forms bind to immobilized wheat germ agglutinin, ricin and concanavalin A, indicating that they have complex oligosacchrides. After treatment of muscle cells with a membrane-permeable irreversible AcChoEase inhibitor, there is a rapid reappearance of the globular monomeric, dimeric and tetrameric AcChoEase forms. However, the collagen-tailed asymmetric form does not appear until .apprx. 90 min after treatment. Analysis of the AcChoEase oligosaccharides with lectins indicates maturation to complex forms over a 90-min period. A large fraction of the intracellular globular AcChoEase molecules bind only to concanavalin A, indicating that they are assembled in the rough endoplasmic reticulum. In contrast, all intracellular asymmetric AcChoEase binds to wheat germ agglutinin, and a significant fraction binds to ricin, indicating that this unique AcChoEase form is assembled from subunits that have previously acquired complex sugars. The assembly of asymmetric AcChoEase, hence acquisition of information specifying basal lamina localization, apparently occurs in the Golgi apparatus.