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Updated: Aug 30, 2026

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
07:32

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

FGFR3IIIS: a novel soluble FGFR3 spliced variant that modulates growth is frequently expressed in tumour cells

L-M Sturla1, A E Merrick, S A Burchill

  • 1Candlelighter's Children's Cancer Research Laboratory, Cancer Research UK Clinical Centre, St James's University Hospital, Beckett Street, Leeds LS9 7TF, UK.

British Journal of Cancer
|October 2, 2003
PubMed

Insights

A novel Fibroblast Growth Factor Receptor 3 (FGFR3) variant, FGFR3IIIS, was identified. This variant may inhibit FGFR3-induced growth arrest, potentially contributing to cancer development.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Signaling

Background:

  • Fibroblast Growth Factor Receptor 3 (FGFR3) is a tyrosine kinase receptor involved in cell growth and differentiation.
  • Ligand binding specificity is determined by alternative splicing of exons IIIb and IIIc in the FGFR3 Ig-like domain III.
  • Aberrant FGFR3 signaling is implicated in various cancers.

Purpose of the Study:

  • To identify and characterize novel FGFR3 variants.
  • To investigate the functional role of the newly identified FGFR3IIIS variant.
  • To explore the potential contribution of FGFR3IIIS to malignant phenotypes.

Main Methods:

  • Reverse transcriptase polymerase chain reaction (RT-PCR) for variant identification.
  • Analysis of protein expression in membrane and soluble cell fractions.
  • In vitro studies using antisense technology to assess functional impact.

Main Results:

  • A novel FGFR3IIIc variant, FGFR3IIIS, was identified, predominantly expressed in tumors.
  • FGFR3IIIS produces a novel, in-frame protein coexpressed with FGFR3IIIc.
  • Knockout of FGFR3IIIS demonstrated in vitro growth inhibition, suggesting a dominant-negative function.

Conclusions:

  • Alternative splicing of FGFR3 Ig-domain III generates receptor diversity.
  • FGFR3IIIS may play a regulatory role in FGF and FGFR trafficking and function.
  • FGFR3IIIS is a potential contributor to the development of a malignant phenotype.

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