Membrane skeleton protein 4.1 in developing Xenopus: expression in postmitotic cells of the retina.
Membrane skeleton protein 4.1 in developing Xenopus: expression in postmitotic cells of the retina.
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DOI：
10.1016/0012-1606(90)90297-v
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发表时间：
1990-06
影响因子：
2.7
通讯作者：
Maribeth Spencer;D. H. Giebelhaus;Gregory M. Kelly;James N. Bicknell;Stephanie K. Florio;A. Milam;R. T. Moon
中科院分区：
文献类型：
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作者：
Maribeth Spencer;D. H. Giebelhaus;Gregory M. Kelly;James N. Bicknell;Stephanie K. Florio;A. Milam;R. T. Moon
膜骨架蛋白4.1在调节红系和非红系细胞中血影蛋白、肌动蛋白和整合膜蛋白的相互作用中起关键作用。我们研究了它的结构及其在非洲爪蟾胚胎发育过程中的表达。分析了X的2758个核苷酸的完整序列，并预测了801个氨基酸（85.5 kDa）的翻译。LAEVISOOCYTE蛋白4.1揭示，在重叠区域内，卵母细胞蛋白4.1为74% S1核酸酶保护分析表明，在人红细胞和淋巴样蛋白4.1中存在单一种类的蛋白4.1转录物，胚胎抗X产生的抗体。laevisprotein 4.1融合蛋白在X的Western印迹上识别180和115 kDa的两条带。利用免疫细胞化学技术，对发育中的视网膜进行了标记。laevisprotein 4.1产生一种合成的mRNA，当在体外培养时，产生一种多肽，该多肽在SDS-聚丙烯酰胺凝胶上与115-kDa形式的胚胎和视网膜共迁移。蛋白质4.1仅在视网膜神经元终末有丝分裂后的光感受器中发现。当视网膜突触发生完成时，蛋白4.1也在内层视网膜中表达。在成年两栖动物视网膜中，在光感受器、双极细胞和神经节细胞轴突中检测到蛋白4.1。由于这些细胞类型先前已显示表达血影蛋白、肌动蛋白和锚蛋白，因此红细胞和视网膜细胞的膜骨架可能具有功能相似性。
Membrane skeleton protein 4.1 plays a key role in modulating the interactions of spectrin, actin, and integral membrane proteins in erythroid and nonerythroid cells. We have investigated its structure and expression during embryonic development ofXenopus laevis. An analysis of the complete 2758-nucleotide sequence and predicted translation of 801 amino acids (85.5 kDa) ofX. laevisoocyte protein 4.1 reveals that, within overlapping regions, oocyte protein 4.1 is 74% identical to a composite amino acid sequence of human erythroid and lymphoid protein 4.1 and has an identity similar to that of amino acid motifs variably expressed in either human erythroid or lymphoid protein 4.1 S1 nuclease protection analysis demonstrates the presence of a single species of protein 4.1 transcript in embryos. Antibodies produced againstX. laevisprotein 4.1 fusion protein recognize two bands of 180 and 115 kDa on Western blots ofX. laevisembryos and retina and, using immunocytochemical techniques, label the developing retina most intensely.In vitrotranscription of a cDNA constrnet fully encodingX. laevisprotein 4.1 yields a synthetic mRNA which, when translatedin vitro, produces a polypeptide that comigrates on SDS-polyacrylamide gels with the 115-kDa form of embryos and retina. Protein 4.1 is found exclusively in photoreceptors following the terminal mitoses of retinal neurons. When retinal synaptogenesis is complete, protein 4.1 is also expressed in the inner retina. In adult amphibian retinas, protein 4.1 is detected in photoreceptors, bipolar cells, and ganglion cell axons. As these cell types have previously been shown to express spectrin, actin, and ankyrin, it is likely that the membrane skeleton of erythrocytes and retinal cells share functional similarities.