Identification and characterization of soluble isoform of fibroblast growth factor receptor 3 in human SaOS-2 osteosarcoma cells

Biochemical and Biophysical Research Communications
Jun-Hyeog Jang

Abstract

We have previously reported the alternatively spliced transcripts of fibroblast growth factor 3 (FGFR3 ATs and MTs) derived by aberrant splicing and usage of cryptic splicing sites. Here, we describe a soluble variant of FGFR3 (FGFR3 AT-III) arising from skipping exons 8, 9, and 10 in human SaOS-2 osteosarcoma cell. This splicing event leads to the generation of an mRNA encoding a FGFR3 in which the COOH-terminal portion of the Ig-like-III domain and transmembrane domain are deleted while the remainder of the mature molecule is fused in-frame to the COOH-terminal cytoplasmic kinases domains. Sf9 cells transfected with the corresponding cDNA express the soluble form of FGFR3 AT-III into the condition medium and its secreted form was able to bind both FGF-1 and FGF-2 leading to loss of ligand binding specificity. These results indicate that the FGFR3 AT-III mRNAs are transcribed due to exon skipping with altered ligand binding specificity. These results suggest that the presence of soluble transcripts of FGFRs gene is a common feature due to mRNA splicing and this splicing plays an important role in the regulation of FGFRs function.

Citations

Jul 8, 2011·Future Oncology·Katayoon Kasaian, Steven Jm Jones
Apr 9, 2005·Experimental Cell Research·R BauerA K Bosserhoff
Dec 23, 2009·Bulletin of Experimental Biology and Medicine·I V BabkinaN E Kushlinsky
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