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人纤连蛋白以前原多肽形式合成。

Human fibronectin is synthesized as a pre-propolypeptide.

作者信息

Gutman A, Yamada K M, Kornblihtt A

出版信息

FEBS Lett. 1986 Oct 20;207(1):145-8. doi: 10.1016/0014-5793(86)80029-1.

Abstract

Fibronectins (FNs) are extracellular glycoproteins consisting of dimers or multimers of similar but not identical subunits. The subunit differences result from variations in internal primary sequence due to alternative splicing in at least 2 regions of the pre-mRNA. The complete amino acid sequence of mature human cellular FN has been reported recently from cDNA cloning and sequencing. The same approach has now enabled us to deduce, for the first time, that FN has a 26 amino acid signal peptide and that it undergoes proteolytic processing at its N-terminus to eliminate a 5 amino acid pro-sequence (Ser-Lys-Ser-Lys-Arg). The signal sequence matches the consensus format, while this pro-sequence is a distinctive, very hydrophilic and basic peptide.

摘要

纤连蛋白(FNs)是细胞外糖蛋白,由相似但不完全相同的亚基的二聚体或多聚体组成。亚基差异源于前体mRNA至少2个区域的可变剪接导致的内部一级序列变化。最近通过cDNA克隆和测序报道了成熟人细胞FN的完整氨基酸序列。现在,同样的方法首次使我们能够推断出FN有一个26个氨基酸的信号肽,并且它在其N端进行蛋白水解加工以去除一个5个氨基酸的前序列(丝氨酸-赖氨酸-丝氨酸-赖氨酸-精氨酸)。该信号序列符合共有格式,而这个前序列是一种独特的、非常亲水且呈碱性的肽。

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