Expression and glycosylation studies of human FGF receptor 4

Heidi Tuominen, Pirkko Heikinheimo, Britt-Marie Loo, Kari Kataja, Christian Oker-Blom, Marko Uutela, Markkku Jalkanen, Adrian Goldman

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8 Citations (Scopus)

Abstract

Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large amounts of FGFR4ed have been produced into inclusion bodies in Escherichia coli and refolded at least partly correctly but the refolded E. coli-produced FGFR4ed still aggregates.
Original languageEnglish
Pages (from-to)275-285
JournalProtein Expression and Purification
Volume21
Issue number2
DOIs
Publication statusPublished - 2001
MoE publication typeA1 Journal article-refereed

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    Tuominen, H., Heikinheimo, P., Loo, B-M., Kataja, K., Oker-Blom, C., Uutela, M., Jalkanen, M., & Goldman, A. (2001). Expression and glycosylation studies of human FGF receptor 4. Protein Expression and Purification, 21(2), 275-285. https://doi.org/10.1006/prep.2000.1375