Glycoconnectin (PAS 2), a membrane attachment site for the human erythrocyte cytoskeleton.
Glycoconnectin (PAS 2), a membrane attachment site for the human erythrocyte cytoskeleton.
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糖连接蛋白 (PAS 2)，人红细胞细胞骨架的膜附着位点。
DOI：
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发表时间：
1981
期刊：
影响因子：
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通讯作者：
M. Morrison
中科院分区：
文献类型：
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作者：
Mueller Tj;M. Morrison
唾液糖蛋白PAS2存在于Triton X-100提取分离的人红细胞基质所产生的细胞骨架中。然而，在提取Triton之前，通过0.1N NaOH洗脱去除外周细胞骨架蛋白，使PAS 2 Triton可溶。这提示PAS-2与红细胞膜内表面的细胞骨架元素有关。出于这个原因，我们建议将PAS 2命名为糖连接素，因为它是一种连接细胞骨架核心和膜双层的糖蛋白。细胞骨架蛋白带4.1a，b似乎也直接与膜相互作用，因为所有其他外周膜蛋白都可以用pH为11.5的NaOH洗脱，而不会从膜上释放带4.1a，b。从膜上去除血影蛋白和肌动蛋白会导致Triton X-100增溶糖连接蛋白和4.1a，b条带。如果供体的细胞膜上没有4.1a，b带，则细胞骨架中不存在糖连接素。这些数据表明，糖连接素可能直接与4.1a，b带相互作用。
The sialoglycoprotein PAS 2 is present in cytoskeletons generated by Triton X-100 extraction of isolated human erythrocyte stroma. However, removal of the peripheral cytoskeletal proteins by elution with 0.1N NaOH prior to Triton extraction renders PAS 2 Triton-soluble. This suggests association of PAS 2 with the cytoskeletal elements lining the inner surface of the erythrocyte membrane. For this reason, we are proposing the name glycoconnectin for PAS 2, since it is a glycoprotein which connects the core of the cytoskeleton to the membrane bilayer. The cytoskeletal proteins bands 4.1a,b also appear to interact directly with the membrane, since all of the other peripheral membrane proteins can be eluted with NaOH, pH 11.5, without releasing bands 4.1a,b from the membrane. Removal of spectrin and actin from the membrane results in the solubilization of both glycoconnectin and bands 4.1a,b by Triton X-100. Glycoconnectin is not present in the cytoskeletons derived from a donor whose membranes are devoid of bands 4.1a,b. These data suggest that glycoconnectin may interact directly with bands 4.1a,b.