The effect of the chemical chaperone 4-phenylbutyrate on secretion and activity of the p.Q160R missense variant of coagulation factor FVII.

Chemical chaperones Endoplasmic reticulum Factor VII deficiency Mutations Protein misfolding Trafficking

Journal

Cell & bioscience
ISSN: 2045-3701
Titre abrégé: Cell Biosci
Pays: England
ID NLM: 101561195

Informations de publication

Date de publication:
2019
Historique:
received: 18 02 2019
accepted: 17 08 2019
entrez: 31 8 2019
pubmed: 31 8 2019
medline: 31 8 2019
Statut: epublish

Résumé

Congenital coagulation factor (F) VII deficiency is a rare bleeding disorder caused by mutations in the Through screening of compounds, we identified 4-phenylbutyrate (4-PBA) to increase the secretion of recombinant (r) FVII-160R by ~ 2.5-fold. Additionally, treatment with 4-PBA resulted in a modest increase in specific biological activity. Intracellular localization studies revealed that upon treatment with 4-PBA, rFVII-160R was secreted through Golgi and Golgi reassembly-stacking protein (GRASP)-structures. The present study demonstrates that the chemical chaperone 4-PBA, restores intracellular trafficking and increases the secretion of a missense FVII variant with functional properties in the extrinsic coagulation pathway.

Sections du résumé

BACKGROUND BACKGROUND
Congenital coagulation factor (F) VII deficiency is a rare bleeding disorder caused by mutations in the
RESULTS RESULTS
Through screening of compounds, we identified 4-phenylbutyrate (4-PBA) to increase the secretion of recombinant (r) FVII-160R by ~ 2.5-fold. Additionally, treatment with 4-PBA resulted in a modest increase in specific biological activity. Intracellular localization studies revealed that upon treatment with 4-PBA, rFVII-160R was secreted through Golgi and Golgi reassembly-stacking protein (GRASP)-structures.
CONCLUSIONS CONCLUSIONS
The present study demonstrates that the chemical chaperone 4-PBA, restores intracellular trafficking and increases the secretion of a missense FVII variant with functional properties in the extrinsic coagulation pathway.

Identifiants

pubmed: 31467667
doi: 10.1186/s13578-019-0333-8
pii: 333
pmc: PMC6712599
doi:

Types de publication

Journal Article

Langues

eng

Pagination

69

Déclaration de conflit d'intérêts

Competing interestsThe authors declare that they have no competing interests.

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Auteurs

Elisabeth Andersen (E)

1Department of Haematology, Oslo University Hospital, Oslo, Norway.
2Research Institute of Internal Medicine, Oslo University Hospital, Oslo, Norway.
3Institute of Clinical Medicine, University of Oslo, Oslo, Norway.

Maria Eugenia Chollet (ME)

1Department of Haematology, Oslo University Hospital, Oslo, Norway.
2Research Institute of Internal Medicine, Oslo University Hospital, Oslo, Norway.

Marcello Baroni (M)

Department of Life Sciences and Biotechnology, and LTTA Centre, University of Ferrara, Oslo, Norway.

Mirko Pinotti (M)

Department of Life Sciences and Biotechnology, and LTTA Centre, University of Ferrara, Oslo, Norway.

Francesco Bernardi (F)

Department of Life Sciences and Biotechnology, and LTTA Centre, University of Ferrara, Oslo, Norway.

Ellen Skarpen (E)

5Core Facility for Advanced Light Microscopy, Institute for Cancer Research, Oslo University Hospital, Ferrara, Italy.

Per Morten Sandset (PM)

1Department of Haematology, Oslo University Hospital, Oslo, Norway.
2Research Institute of Internal Medicine, Oslo University Hospital, Oslo, Norway.
3Institute of Clinical Medicine, University of Oslo, Oslo, Norway.

Grethe Skretting (G)

1Department of Haematology, Oslo University Hospital, Oslo, Norway.
2Research Institute of Internal Medicine, Oslo University Hospital, Oslo, Norway.

Classifications MeSH