Structural characterization of the circulating soluble FGF receptors reveals multiple isoforms generated by secretion and ectodomain shedding
Structural characterization of the circulating soluble FGF receptors reveals multiple isoforms generated by secretion and ectodomain shedding
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DOI：
10.1016/s0014-5793(00)02409-1
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发表时间：
2001-02-02
期刊：
影响因子：
3.5
通讯作者：
Hanneken, A
中科院分区：
文献类型：
--
作者：
Hanneken, A
可溶性成纤维细胞生长因子受体（FGFR）已被确定在多种生物液体，包括血液。研究这些蛋白质的生物学特性的努力受到第三免疫球蛋白（IG）样结构域的第二半内受体的不完全化学表征的阻碍，其中选择性剪接导致具有不同配体结合特性的受体变体。使用质谱技术，我们已经将可溶性FGFR映射到分泌型受体FGFR1（IIIa）、FGFR1的两个和三个Ig样结构域同种型（IIIc）以及来自FGFR1的两个和三个Ig样结构域同种型（IIIb）的羧基末端切割肽。分泌的FGFR通过可变剪接转录物的翻译产生，并且切割的受体通过跨膜受体的胞外域脱落释放，（C）2001 Federation of European Biochemical Societies，由Elsevier Science B.V.出版，保留所有权利。
Soluble fibroblast growth factor receptors (FGFRs) have been identified in multiple biological fluids, including blood. Efforts to examine the biological properties of these proteins have been hampered by the incomplete chemical characterization of the receptors within the second half of the third immunoglobulin (Ig)-like domain, where alternative splicing leads to receptor variants with different ligand binding properties. Using mass spectrometry techniques, we have mapped the soluble FGFRs to the secreted receptor, FGFR1(IIIa), the two and three Ig-like domain isoforms of FGFR1(IIIc) and a carboxyl-terminal cleavage peptide from the two and three Ig-like domain isoforms of FGFR1(IIIb). The secreted FGFR is produced by the translation of an alternatively spliced transcript and the cleaved receptors are released by ectodomain shedding of the transmembrane receptors, (C) 2001 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.