Rapid capping in alpha-spectrin-deficient MEL cells from mice afflicted with hereditary hemolytic anemia.
Rapid capping in alpha-spectrin-deficient MEL cells from mice afflicted with hereditary hemolytic anemia.
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DOI：
10.1083/jcb.125.5.1057
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发表时间：
1994-06
期刊：
影响因子：
--
通讯作者：
Branton D
中科院分区：
文献类型：
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作者：
Dahl SC;Geib RW;Fox MT;Edidin M;Branton D
基于血影蛋白的膜骨架对于红细胞的稳定性和组织化是重要的。为了研究血影蛋白在具有复杂细胞骨架的细胞中的作用，我们从sph/sph小鼠中产生了α-血影蛋白缺陷的红白血病细胞系。通过免疫印迹和北方印迹分析确定，这些细胞含有β-血影蛋白，但缺乏α-血影蛋白。α-血影蛋白缺乏的影响在培养的细胞的不规则形状和脆弱性中是明显的。荧光凝集素或抗体对膜糖蛋白的加帽作用在SPH/SPH中比在野生型红白血病细胞中发生得更快，并且帽显得更集中。这些数据支持血影蛋白在组织膜结构和限制成熟红细胞以外的细胞中的完整膜糖蛋白的横向流动性方面起重要作用的观点。
A spectrin-based membrane skeleton is important for the stability and organization of the erythrocyte. To study the role of spectrin in cells that possess complex cytoskeletons, we have generated alpha-spectrin- deficient erythroleukemia cell lines from sph/sph mice. These cells contain beta-spectrin, but lack alpha-spectrin as determined by immunoblot and Northern blot analyses. The effects of alpha-spectrin deficiency are apparent in the cells' irregular shape and fragility in culture. Capping of membrane glycoproteins by fluorescent lectin or antibodies occurs more rapidly in sph/sph than in wild-type erythroleukemia cells, and the caps appear more concentrated. The data support the idea that spectrin plays an important role in organizing membrane structure and limiting the lateral mobility of integral membrane glycoproteins in cells other than mature erythrocytes.