Christensen Claus, Berezin Vladimir, Bock Elisabeth
Department of Neuroscience and Pharmacology, Protein Laboratory, University of Copenhagen, Copenhagen N, Denmark.
Neuroreport. 2011 Oct 26;22(15):727-32. doi: 10.1097/WNR.0b013e3283491682.
The fibroblast growth factor receptor (FGFR) can be activated through direct interactions with various fibroblast growth factors or through a number of cell adhesion molecules, including the neural cell adhesion molecule (NCAM). We produced recombinant proteins comprising the ligand-binding immunoglobulin-like modules 2 and 3 of FGFR1b, FGFR1c, FGFR2b, FGFR2c, FGFR3b, FGFR3c, and FGFR4, and found that all FGFR isoforms, except for FGFR4, interacted with NCAM. The binding affinity of NCAM-FGFR interactions was considerably higher for splice variant 'b' than for splice variant 'c'. We suggest that the expression pattern of various FGFR isoforms determines the cell context-specific effects of NCAM signaling through FGFR.
成纤维细胞生长因子受体（FGFR）可通过与多种成纤维细胞生长因子直接相互作用或通过多种细胞黏附分子（包括神经细胞黏附分子（NCAM））被激活。我们制备了包含FGFR1b、FGFR1c、FGFR2b、FGFR2c、FGFR3b、FGFR3c和FGFR4的配体结合免疫球蛋白样模块2和3的重组蛋白，发现除FGFR4外，所有FGFR异构体均与NCAM相互作用。NCAM与FGFR相互作用的结合亲和力，剪接变体“b”比剪接变体“c”高得多。我们认为，各种FGFR异构体的表达模式决定了NCAM通过FGFR信号传导的细胞背景特异性效应。
