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一种新型的成纤维细胞生长因子受体-5,在胰腺中优先表达(1)。

A novel fibroblast growth factor receptor-5 preferentially expressed in the pancreas(1).

作者信息

Kim I, Moon S, Yu K, Kim U, Koh G Y

机构信息

National Creative Research Initiatives Center for Cardiac Regeneration, Chonbuk National University School of Medicine, San 2-20, Keum-Am-Dong, Chonju 560-180, South Korea.

出版信息

Biochim Biophys Acta. 2001 Mar 19;1518(1-2):152-6. doi: 10.1016/s0167-4781(00)00282-7.

DOI:10.1016/s0167-4781(00)00282-7
PMID:11267671
Abstract

Using the polymerase chain reaction on human embryonic cDNAs, we isolated a cDNA encoding a novel 504 amino acid protein, termed fibroblast growth factor receptor (FGFR)-5, which is highly homologous to known FGFRs. The NH(2)-terminal portion of FGFR5 contains a putative secretory signal sequence, three typical immunoglobulin-like domains, six cysteines, and an acidic box, but no HAV motif. The COOH-terminal portion of FGFR5 contains one transmembrane domain but no intracellular kinase domain. Recombinant FGFR5 expressed in COS-7 cells is not secreted, but recombinant truncated FGFR5 lacking the predicted transmembrane domain is secreted. Acidic fibroblast growth factor (aFGF) and basic fibroblast growth factor (bFGF) do not bind to FGFR5. Among 23 adult human tissues, FGFR5 mRNA is preferentially expressed in the pancreas. These results suggest that FGFR5 may provide a binding site for some other fibroblast growth factors and may regulate some pancreatic function.

摘要

通过对人胚胎cDNA进行聚合酶链反应,我们分离出了一个编码新型504个氨基酸蛋白质的cDNA,该蛋白质被称为成纤维细胞生长因子受体(FGFR)-5,它与已知的FGFR高度同源。FGFR5的NH2末端部分包含一个推定的分泌信号序列、三个典型的免疫球蛋白样结构域、六个半胱氨酸和一个酸性盒,但没有HAV基序。FGFR5的COOH末端部分包含一个跨膜结构域,但没有细胞内激酶结构域。在COS-7细胞中表达的重组FGFR5不分泌,但缺乏预测跨膜结构域的重组截短型FGFR5是分泌的。酸性成纤维细胞生长因子(aFGF)和碱性成纤维细胞生长因子(bFGF)不与FGFR5结合。在23种成人组织中,FGFR5 mRNA在胰腺中优先表达。这些结果表明,FGFR5可能为其他一些成纤维细胞生长因子提供结合位点,并可能调节某些胰腺功能。

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