Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell.
Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell.
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红细胞膜细胞骨架蛋白 4.1 的膜附着位点。
DOI：
10.1182/blood.v82.11.3482.bloodjournal82113482
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发表时间：
1993
期刊：
影响因子：
20.3
通讯作者：
W. Gratzer
中科院分区：
文献类型：
--
作者：
J. Pinder;A. Chung;M. Reid;W. Gratzer
研究了人红细胞膜骨架蛋白4.1的膜结合位点。用一系列蛋白酶对膜进行彻底的蛋白水解导致仅消除了约60%的所有结合位点。主要的整合膜蛋白，带3，以及血型糖蛋白A，被完全消化的蛋白水解的水平，基本上没有影响的4.1结合位点的数量。蛋白水解导致血型糖蛋白C的多肽链（连同同一基因的次要产物血型糖蛋白D）断裂，但留下C-末端区域的片段仍然附着在膜上。我们已经在Leach表型的细胞中发现了一种低分子量蛋白，其具有与该蛋白水解片段共同的表位（被针对血型糖蛋白C的胞质结构域的抗体识别），Leach表型的细胞的特征在于缺乏血型糖蛋白C的细胞外表位。当在低离子强度下提取这些膜以解离膜细胞骨架时，大约一半的4.1含量被释放，而正常膜中只有大约25%。Leach表型的不同变体的细胞，其完全缺乏血型糖蛋白C，在这些情况下失去了接近70%的4.1。与膜细胞骨架相互作用的Rh（D）跨膜蛋白也对细胞质膜表面的蛋白水解具有抗性，但是没有该蛋白的Rhnull细胞没有显示出4.1的保留降低。结果表明，血型糖蛋白C（与D）可能含有两种类型的结合位点的4.1，这将是足够的数量占所有的强结合的4.1正常膜;调制的结合在一个网站由另一种蛋白质或脂质不排除。在表达截短血型糖蛋白C的突变体中，与提前终止密码子重叠的翻译重新起始的可能位点可以被识别。
The identity of the membrane binding sites for the membrane cytoskeletal protein 4.1 of the human red blood cell has been investigated. Exhaustive proteolysis of the membrane with a range of proteases led to the elimination of only some 60% of all binding sites. The predominant integral membrane protein, band 3, as well as glycophorin A, was totally digested at levels of proteolysis that were essentially without effect on the number of 4.1 binding sites. Proteolysis caused scission of the polypeptide chain of glycophorin C (together with the minor product, glycophorin D, of the same gene), but left a fragment from the region of the C-terminus still attached to the membrane. We have found a low-molecular weight protein, possessing an epitope (recognized by an antibody directed against the cytoplasmic domain of glycophorin C) in common with this proteolytic fragment, in cells of a Leach phenotype, which are characterized by lack of extracellular epitopes of glycophorin C. When these membranes were extracted at low ionic strength to dissociate the membrane cytoskeleton, approximately half the content of 4.1 was liberated, compared with only some 25% from normal membranes. Cells of a different variant of the Leach phenotype, which are totally devoid of glycophorin C, lost close to 70% of their 4.1 under these circumstances. The Rh(D) transmembrane protein, which interacts with the membrane cytoskeleton, is also resistant to proteolysis of the cytoplasmic membrane surface, but Rhnull cells, devoid of this protein, showed no decreased retention of 4.1. The results suggest that glycophorin C (with D) may contain two types of binding site for 4.1, which would be sufficient in number to account for all the strong binding of 4.1 on normal membranes; modulation of binding at one of the sites by another protein or by lipid is not excluded. A possible site for reinitiation of translation overlapping the premature stop codon in the mutant expressing the truncated glycophorin C can be discerned.
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Leach 表型中与糖蛋白 C 和 D 缺乏相关的椭圆形红细胞增多症的分子基础。
影响因子：
20.3
作者：
Telen,MJ;LeVanKim,C;Chung,A;Cartron,JP;Colin,Y
通讯作者：
Colin,Y
红细胞糖蛋白。
影响因子：
20.3
作者：
Chasis,JA;Mohandas,N
通讯作者：
Mohandas,N
蛋白质 4.1：其与人红细胞膜的关联。
DOI：
10.1073/pnas.81.14.4404
发表时间：
1984
影响因子：
11.1
作者：
Shiffer,KA;Goodman,SR
通讯作者：
Goodman,SR
人红细胞膜的血型糖蛋白C含量受蛋白质4.1调节。
影响因子：
20.3
作者：
Reid,ME;Takakuwa,Y;Conboy,J;Tchernia,G;Mohandas,N
通讯作者：
Mohandas,N
红细胞蛋白 4.1 与磷脂的相互作用。
DOI：
10.1016/0005-2736(88)90249-0
发表时间：
1988
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Shiffer,KA;Goerke,J;Düzgüneş,N;Fedor,J;Shohet,SB
通讯作者：
Shohet,SB