Protein folding in the secretory pathway of animal cells

  • Robert B. Freedman
  • Carole Greenall
  • Nigel Jenkins
  • Mick F. Tuite

Abstract

The exit of newly-synthesized proteins from the lumen of the endoplasmic reticulum (ER) is the rate-determining step in protein secretion. Only correctly-folded and fully-assembled proteins exit the ER and progress along the secretory pathway. Folding and assembly in the ER are mediated by a variety of factors including folding catalysts and molecular chaperones. The properties of these factors, and the nature of their interactions with folding substrates, are beginning to be clarified. Little work has been done to characterize these processes and these factors in cell lines employed for large-scale cell culture. Manipulation of these process may permit improvement in yield or productivity of recombinant proteins by cultured animal cells.

Key words

protein folding endoplasmic reticulum glycosylation disulphide bond formation folding catalysts chaperones protein disulphide-isomerase 

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Copyright information

© Springer Science+Business Media Dordrecht 1995

Authors and Affiliations

  • Robert B. Freedman
    • 1
  • Carole Greenall
    • 1
  • Nigel Jenkins
    • 1
  • Mick F. Tuite
    • 1
  1. 1.Research School of Biosciences, Biological LaboratoryUniversity of KentCanterburyUK

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