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Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells

Jossé, Lyne, Smales, Christopher Mark, Tuite, Mick F. (2010) Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells. Biotechnology and Bioengineering, 105 (3). pp. 556-566. ISSN 0006-3592. (doi:10.1002/bit.22572) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:29222)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1002/bit.22572

Abstract

Cultured mammalian cells, particularly Chinese hamster ovary (CHO) cells, are widely exploited as hosts for the production of recombinant proteins, but often yields are limiting. Such limitations may be due in part to the misfolding and subsequent degradation of the heterologous proteins. Consequently we have determined whether transiently co-expressing yeast and/or mammalian chaperones that act to disaggregate proteins, in CHO cell lines, improve the levels of either a cytoplasmic (Fluc) or secreted (Gluc) form of luciferase or an immunoglobulin IgG4 molecule. Over-expression of the yeast ‘protein disaggregase’ Hsp104 in a CHO cell line increased the levels of Fluc more significantly than for Gluc although levels were not further elevated by over-expression of the yeast or mammalian Hsp70/40 chaperones. Over-expression of TorsinA, a mammalian protein related in sequence to yeast Hsp104, but located in the ER, significantly increased the level of secreted Gluc from CHO cells by 2.5-fold and to a lesser extent the secreted levels of a recombinant IgG4 molecule. These observations indicate that the over-expression of yeast Hsp104 in mammalian cells can improve recombinant protein yield and that over-expression of TorsinA in the ER can promote secretion of heterologous proteins from mammalian cells.

Item Type: Article
DOI/Identification number: 10.1002/bit.22572
Uncontrolled keywords: molecular chaperone;Hsp104;protein secretion;luciferase;protein disaggregation;TorsinA
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Lyne Josse
Date Deposited: 28 Mar 2012 13:28 UTC
Last Modified: 16 Nov 2021 10:07 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/29222 (The current URI for this page, for reference purposes)

University of Kent Author Information

Jossé, Lyne.

Creator's ORCID:
CReDIT Contributor Roles:

Smales, Christopher Mark.

Creator's ORCID: https://orcid.org/0000-0002-2762-4724
CReDIT Contributor Roles:

Tuite, Mick F..

Creator's ORCID: https://orcid.org/0000-0002-5214-540X
CReDIT Contributor Roles:
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