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

doi:10.1006/prep.2000.1375

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

VTT Technical Research Centre of Finland

University of Turku
Åbo Akademi University
University of Jyväskylä
University of Helsinki
BioTie Therapies Ltd.

Research output: Contribution to journal › Article › Scientific › peer-review

11 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 (FGFR4_ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4_edis 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 FGFR4_ed, but was still heterogeneous. Large amounts of FGFR4_edhave been produced into inclusion bodies in Escherichia coli and refolded at least partly correctly but the refolded E. coli-produced FGFR4_edstill aggregates.

Original language	English
Pages (from-to)	275-285
Journal	Protein Expression and Purification
Volume	21
Issue number	2
DOIs	https://doi.org/10.1006/prep.2000.1375
Publication status	Published - 2001
MoE publication type	A1 Journal article-refereed

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10.1006/prep.2000.1375

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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.",

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

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doi = "10.1006/prep.2000.1375",

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T1 - Expression and glycosylation studies of human FGF receptor 4

AU - Tuominen, Heidi

AU - Heikinheimo, Pirkko

AU - Loo, Britt-Marie

AU - Kataja, Kari

AU - Oker-Blom, Christian

AU - Uutela, Marko

AU - Jalkanen, Markkku

AU - Goldman, Adrian

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

U2 - 10.1006/prep.2000.1375

DO - 10.1006/prep.2000.1375

M3 - Article

SN - 1046-5928

VL - 21

SP - 275

EP - 285

JO - Protein Expression and Purification

JF - Protein Expression and Purification

IS - 2

ER -

Expression and glycosylation studies of human FGF receptor 4

Abstract

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