PMID: 9546651Apr 18, 1998Paper

In vitro characterisation of the interaction between newly synthesised proteins and a pancreatic isoform of protein disulphide isomerase

European Journal of Biochemistry
J G ElliottS High

Abstract

The lumen of the endoplasmic reticulum (ER) contains an array of molecular chaperones and folding factors that modulate the folding and assembly of newly synthesised proteins entering the secretory pathway. One of these components, protein disulphide isomerase (PDI), facilitates the formation of the correct disulphide bonds within newly synthesised polypeptides, and is the archetype for a family of sequence related PDI-like proteins. We have investigated the interaction between a recently identified, pancreas-specific PDI-like protein (PDIp), and in vitro synthesised secretory and membrane proteins produced in the presence of ER-derived canine pancreatic microsomes. We have previously established that a second PDI-like protein, ERp57, interacts specifically with N-glycosylated proteins. In contrast, we find that the interaction of PDIp with newly synthesised proteins occurs independently of any requirement for N-linked glycosylation. In this respect, the properties of PDIp mirror those of archetypal PDI. When the carbohydrate-dependent interactions between glycoproteins and ERp57 are blocked by drug treatment, the association of these precursors with both PDIp and PDI is enhanced. We propose that PDI-like proteins have overlapp...Continue Reading

Citations

Nov 18, 1998·Current Opinion in Structural Biology·E S Trombetta, A Helenius
May 30, 2009·Antioxidants & Redox Signaling·Feras Hatahet, Lloyd W Ruddock
Dec 21, 2007·Biochimica Et Biophysica Acta·Christian Appenzeller-Herzog, Lars Ellgaard
Aug 28, 1999·The Journal of Biological Chemistry·M I NdubuisiP B Sehgal

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