Publication details for Dr Martin SchroderS. U. Khan & M. Schröder (2008). Engineering of chaperone systems and of the unfolded protein response. Cytotechnology 57(3): 207-231.
- Publication type: Journal papers: academic
- ISSN/ISBN: 0920-9069
- DOI: 10.1007/s10616-008-9157-9
- Keywords: Unfolded protein response; endoplasmic reticulum; chaperone; recombinant protein production
- View online: Online version
Author(s) from Durham
Production of recombinant proteins in mammalian cells is a successful technology that delivers protein pharmaceuticals for therapies and for diagnosis of human disorders. Cost effective production of protein biopharmaceuticals requires extensive optimization through cell and fermentation process engineering at the upstream and chemical engineering of purification processes at the downstream side of the production process. The majority of protein pharmaceuticals are secreted proteins. Accumulating evidence suggests that the folding and processing of these proteins in the endoplasmic reticulum (ER) is a general rate- and yield limiting step for their production. We will summarize our knowledge of protein folding in the ER and of signal transduction pathways activated by accumulation of unfolded proteins in the ER, collectively called the
unfolded protein response (UPR). On the basis of this knowledge we will evaluate engineering approaches to increase cell specific productivities through engineering of the ER-resident protein folding machinery and
of the UPR.