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

European Journal of Biochemistry

Volumn 252, Issue 3, 1998, Pages 372-377

  Elliott, John G ^a   Oliver, Jason D ^a   Volkmer, Jorg ^b   Zimmermann, Richard ^b   High, Stephen ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b SAARLAND UNIVERSITY   (Germany)

Author keywords

Cross linking; Endoplasmic reticulum; Molecular chaperone; N linked glycosylation; Protein disulphide isomerase

Indexed keywords

MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE;

ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; ENZYME ACTIVITY; GLYCOSYLATION; PLASMID; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SYNTHESIS;

ANIMALS; DOGS; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HEAT-SHOCK PROTEINS; HUMANS; ISOENZYMES; ISOMERASES; MEMBRANE PROTEINS; MICROSOMES; PANCREAS; PROTEIN BIOSYNTHESIS; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; RECOMBINANT PROTEINS; TRANSCRIPTION, GENETIC;

EID: 0032521621     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520372.x     Document Type: Article

References (26)

1. Gething, M.-J. & Sambrook, J. (1992) Protein folding in the cell, Nature 355, 33-45.
2. Helenius, A., Marquardt, T. & Braakman, I. (1992) The endoplasmic reticulum as a protein-folding compartment, Trends Cell Biol. 2, 227-231.
3. Hammond, C. & Helenius, A. (1995) Quality control in the secretory pathway, Curr. Opin. Cell Biol. 7, 523-529.
4. Kopito, R. R. (1997) ER quality control: the cytoplasmic connection, Cell 88, 427-430.
5. Freedman, R. B., Hirst, T. R. & Tuite, M. F. (1994) Protein disulphide isomerase: building bridges in protein folding, Trends Biochem. Sci. 19, 331-336.
6. Noiva, R. & Lennarz, W. J. (1992) Protein disulphide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum, J. Biol. Chem. 267, 3553-3556.
7. LaMantia, M. & Lennarz, W. J. (1993) The essential function of yeast protein disulphide isomerase does not reside in its isomerase activity, Cell 74, 899-908.
8. Yao, Y., Zhou, Y. C. & Wang, C. C. (1997) Both the isomerase and chaperone activities of protein disulphide isomerase are required for the reactivation of reduced and denatured acidic phopholipase A2, EMBO J. 16, 651-658.
9. Puig, A. & Gilbert, H. F. (1994) Protein disulphide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme, J. Biol. Chem. 269, 7764-7771.
10. John, D. C. A., Grant, M. E. & Bulleid, N. J. (1993) Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-subunit, EMBO J. 12, 1587-1595.
11. Vuori, K., Pihlajaniemi, T., Myllylyä, R. & Kivirikko, K. I. (1992) Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity, and endoplasmic reticulum retention of human prolyl-4-hydroxylase in Spodoptera frugiperda insect cells, EMBO J. 11, 4213-4217.
12. Oliver, J. D., van der Wal, F. J., Bulleid, N. J. & High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins, Science 275, 86-88.
13. Elliott, J. G., Oliver, J. D. & High, S. (1997) The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins, J. Biol. Chem. 272, 13 849-13 855.
14. DeSilva, M. G., Lu, J., Donadel, G., Modi, W. S., Xie, H., Notkins, A. L. & Lan, M. S. (1996) Characterisation and chromosomal localization of a new protein disulphide isomerase, PDIp, highly expressed in human pancreas, DNA Cell Biol. 15, 9-16.
15. DeSilva, M. G., Notkins, A. L. & Lan, M. S. (1997) Molecular characterisation of a pancreas- specific protein disulphide isomerase, PDIp, DNA Cell Biol. 16, 269-274.
16. Volkmer, J., Guth, S., Nastainczyk, W., Knippel, P., Klappa, P., Gnau, V. & Zimmermann, R. (1997) Pancreas specific protein disulphide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation, FEBS Lett. 406, 291-295.
17. Oliver, J. D., Hresko, R. C., Mueckler, M. & High, S. (1996) The Glut 1 glucose transporter interacts with calnexin and calreticulin, J. Biol. Chem. 271, 13 691-13 696.
18. Klappa, P., Freedman, R. B. & Zimmermann, R. (1995) Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation, Eur. J. Biochem. 232, 755-764.
19. Song, J. L. & Wang, C. C. (1995) Chaperone-like activity of protein disulphide-isomerase in the refolding of rhodanese, Eur. J. Biochem. 231, 312-316.
20. Craig, E. A., Baxter, B. K., Becker, J., Halladay, J. & Ziegelhoffer, T. (1994) in The biology of heat shock proteins and molecular chaperones (Morimoto, R. I., Tissieres, A. & Georgopoulos, C., eds) pp. 31-52, Cold Spring Harbour Laboratory Press, Cold Spring Harbour NY.
21. Iida, K. I., Miyaishi, O., Iwata, Y., Kozaki, K. I., Matsuyama, M. & Saga, S. (1996) Distinct distribution of protein disulphide isomerase family proteins from rat tissues, J. Histochem. Cytochem. 44, 751-759.
22. Ou, W.-J., Cameron, P. H., Thomas, D. Y. & Bergeron, J. J. M. (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776.
23. Peterson, J. R., Ora, A., Van, P. N. & Helenius, A. (1995) Transient, lectin-like association of calreticulin with folding intermedaites of cellular and viral glycoproteins, Mol. Biol. Cell 6, 1173-1184.
24. Melnick, J., Dul, J. L. & Argon, Y. (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum, Nature 370, 373-375.
25. Hebert, D. N., Foellmer, B. & Helenius, A. (1996) Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes, EMBO J. 15, 2961-2968.
26. Helenius, A., Trombetta, E. S., Hebert, D. N. & Simons, J. F. (1996) Calnexin, calreticulin and the folding of glycoproteins, Trends Cell Biol. 7, 193-200.