NON-ERYTHROCYTE SPECTRINS - ACTIN-MEMBRANE ATTACHMENT PROTEINS OCCURRING IN MANY CELL-TYPES

NON-ERYTHROCYTE SPECTRINS - ACTIN-MEMBRANE ATTACHMENT PROTEINS OCCURRING IN MANY CELL-TYPES
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DOI:
10.1083/jcb.95.2.478
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发表时间:
1982-01-01
影响因子:
7.8
通讯作者:
MANGEAT, P
MANGEAT, P
中科院分区:
生物学1区
文献类型:
--
作者:
BURRIDGE, K;KELLY, T;MANGEAT, P

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对牛、猪脑胞膜蛋白的性质进行了分析,并与红细胞血影蛋白的性质进行了比较。这两种蛋白质组成的高分子量的多肽对SDS [十二烷基硫酸钠]聚丙烯酰胺凝胶和溶液中表现为非常大的不对称分子。这两种蛋白质在20 mM KCl的存在下显示出沉降系数的特征性增加。针对脑蛋白的抗体与红细胞血影蛋白交叉反应,并与其他细胞类型和质膜制备物的SDS聚丙烯酰胺凝胶中的类似高MW双联体多肽交叉反应。两种蛋白质都结合肌动蛋白。脑蛋白和红细胞血影蛋白显示出与红细胞膜的特异性和竞争性结合,并且这种结合被针对红细胞锚蛋白的抗体抑制。这些特性中的几个将这些蛋白质与包括细丝蛋白和巨噬细胞肌动蛋白结合蛋白的高分子量肌动蛋白结合蛋白类区分开。与红细胞血影蛋白一起,脑蛋白和其他细胞类型中的等效免疫相关蛋白属于一类蛋白质,其共同功能是将肌动蛋白附着到质膜上。基于结构和功能的相似性,血影蛋白的名称似乎适合这整个类别的蛋白质。
The properties of [beef and pig] brain fodrin were analyzed and compared with those of erythrocyte spectrin. Both proteins consist of high MW polypeptide doublets on SDS [sodium dodecyl sulfate] polyacrylamide gels and in solution behave as very large asymmetric molecules. Both proteins show a characteristic increase in sedimentation coefficient in the presence of 20 mM KCl. Antibodies against the brain protein cross-react with erythrocyte spectrin and cross-react with similar high MW doublet polypeptides in SDS polyacrylamide gels of other cell types and plasma membrane preparations. Both proteins bind actin. The brain protein and erythrocyte spectrin show specific and competitive binding to erythrocyte membranes and this binding is inhibited by antibodies against erythrocyte ankyrin. Several of these properties distinguish these proteins from the class of high MW actin-binding proteins that includes filamin and macrophage actin-binding protein. Together with erythrocyte spectrin, the brain protein and equivalent, immunologically related proteins in other cell types belong to a single class of proteins with the common function of attachment of actin to plasma membranes. Based on the structural and functional similarities, the name spectrin would seem appropriate for this whole class of proteins.