PURIFICATION AND COMPLEMENTARY-DNA CLONING OF A RECEPTOR FOR BASIC FIBROBLAST GROWTH-FACTOR
PURIFICATION AND COMPLEMENTARY-DNA CLONING OF A RECEPTOR FOR BASIC FIBROBLAST GROWTH-FACTOR
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DOI：
10.1126/science.2544996
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发表时间：
1989-07-07
期刊：
影响因子：
56.9
通讯作者：
WILLIAMS, LT
中科院分区：
文献类型：
--
作者：
LEE, PL;JOHNSON, DE;WILLIAMS, LT
碱性成纤维细胞生长因子（bFGF）参与许多过程，包括早期发育事件、血管生成、伤口愈合和维持神经元细胞活力。基于其特异性结合bFGF的能力，分离出130千道尔顿的蛋白质。用对应于纯化蛋白的胰蛋白酶肽片段的确定氨基酸序列的寡核苷酸探针分离互补DNA克隆。由该互补DNA编码的推定bFGF受体是一种跨膜蛋白，其含有三个细胞外免疫球蛋白样结构域、一个不寻常的酸性区域和一个细胞内酪氨酸激酶结构域。这些结构域的排列模式不同于所描述的任何生长因子受体。
Basic fibroblast growth factor (bFGF) participates in many processes including early developmental events, angiogenesis, wound healing, and maintenance of neuronal cell viability. A 130-kilodalton protein was isolated on the basis of its ability to specifically bind to bFGF. A complementary DNA clone was isolated with an oligonucleotide probe corresponding to determined amino acid sequences of tryptic peptide fragments of the purified protein. The putative bFGF receptor encoded by this complementary DNA is a transmembrane protein that contains three extracellular immunoglobulin-like domains, an unusual acidic region, and an intracellular tyrosine kinase domain. These domains are arranged in a pattern that is different from that of any growth factor receptor described.