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Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype

机译:补体系统的膜辅因子蛋白:丝氨酸/苏氨酸/脯氨酸丰富的外显子和胞质尾部的可变剪接产生与蛋白表型相关的多种同工型

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摘要

Membrane cofactor protein (MCP) is a complement regulatory protein that is expressed on human cells and cell lines as two relatively broad species with Mr of 58,000-68,000 and 48,000-56,000. The structure of a previously reported cDNA clone indicated that MCP was a type 1 membrane glycoprotein and a member of the regulators of complement activation gene/protein cluster. However, it did not provide an explanation for the unusual phenotypic pattern of MCP. Therefore, in parallel with an analysis of the gene, additional cDNAs were cloned and characterized. Six different MCP cDNA classes were identified. All encode the same 5' untranslated signal peptide, four SCRs, transmembrane domain, and basic amino acid anchor. However, they differ in the length and composition of an extracellular serine/threonine/proline (STP)-rich area, a site of heavy O-glycosylation, and cytoplasmic tail. Analysis of the MCP gene demonstrated that the variation in cDNA structure was a result of alternative splicing. Peripheral blood cells and cell lines predominantly expressed four of the six isoforms. These varied by the presence or absence of an STP-rich segment of 15 amino acids (STPB) and by the use of one of two cytoplasmic domains. Analysis by polymerase chain reaction, Northern blots, and transfection indicated that the predominance of MCP cDNA isoforms with STPB correlated with the high molecular weight protein phenotype, while the predominance of isoforms without STPB correlated with the lower molecular weight phenotype. The expression in a single cell of four distinct protein species with variable STP-rich regions and cytoplasmic tails represents an interesting example of the use of alternative splicing to provide variability in a mammalian protein.
机译:膜辅因子蛋白(MCP)是一种补体调节蛋白,在人类细胞和细胞系中表达为两种相对较宽的物种,Mr分别为58,000-68,000和48,000-56,000。先前报道的cDNA克隆的结构表明,MCP是1型膜糖蛋白,是补体激活基因/蛋白簇调节剂的成员。但是,它没有提供MCP异常表型的解释。因此,与基因分析同时,克隆和鉴定了其他cDNA。确定了六种不同的MCP cDNA类。全部编码相同的5'非翻译信号肽,四个SCR,跨膜结构域和碱性氨基酸锚。但是,它们在富含细胞外丝氨酸/苏氨酸/脯氨酸(STP)的区域,重度O-糖基化位点和细胞质尾巴的长度和组成方面有所不同。对MCP基因的分析表明,cDNA结构的变异是选择性剪接的结果。外周血细胞和细胞系主要表达六个同工型中的四个。这些因存在或不存在富含15个氨基酸的STP片段(STPB)和使用两个胞质域之一而变化。通过聚合酶链反应,Northern印迹和转染的分析表明,带有STPB的MCP cDNA亚型的优势与高分子量蛋白表型相关,而没有STPB的同种型的优势与较低的分子量表型相关。具有可变STP富集区和胞质尾巴的四个不同蛋白质种类在单个细胞中的表达代表了使用替代剪接提供哺乳动物蛋白质变异性的一个有趣例子。

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