Calnexin inhibits thermal aggregation and neurotoxicity of prion protein

Journal of Cellular Biochemistry

Volumn 111, Issue 2, 2010, Pages 343-349

  Wang, Wenxi ^a   Chen, Rui ^a   Luo, Kan ^a   Wu, Di ^a   Huang, Liqin ^a   Huang, Tao ^a   Xiao, Gengfu ^a,b  

^a WUHAN UNIVERSITY   (China)

^b WUHAN INSTITUTE OF VIROLOGY   (China)

Author keywords

Apoptosis; Calnexin; Cytotoxicity; Molecular chaperone; Prion

Indexed keywords

CALNEXIN; CASPASE 3; CHAPERONE; PRION PROTEIN;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY; ENZYME ACTIVITY; FLOW CYTOMETRY; HUMAN; HUMAN CELL; NEUROTOXICITY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN INTERACTION; TURBIDITY;

CALNEXIN; CASPASE 3; HOT TEMPERATURE; HUMANS; PRION DISEASES; PRIONS; PROTEIN BINDING; PROTEIN MULTIMERIZATION;

EID: 77957270373     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.22698     Document Type: Article

References (37)

1. Aguzzi A, Heikenwalder M, Polymenidou M. 2007. Insights into prion strains and neurotoxicity. Nat Rev Mol Cell Biol 8:552-561.
2. Barducci A, Chelli R, Procacci P, Schettino V. 2005. Misfolding pathways of the prion protein probed by molecular dynamics simulations. Biophys J 88:1334-1343.
3. Collinge J, Clarke AR. 2007. A general model of prion strains and their pathogenicity. Science 318:930-936. (Pubitemid 350098981)
4. Danilczyk UG, Williams DB. 2001. The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. J Biol Chem 276:25532-25540. (Pubitemid 37413043)
5. Ellgaard L, Helenius A. 2003. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4:181-191.
6. Ellgaard L, Molinari M, Helenius A. 1999. Setting the standards: Quality control in the secretory pathway. Science 286:1882-1888. (Pubitemid 129515888)
7. Hammond C, Braakman I, Helenius A. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 91:913-917. (Pubitemid 24048478)
8. Harris DA, Gorodinsky A, Lehmann S, Moulder K, Shyng SL. 1996. Cell biology of the prion protein. Curr Top Microbiol Immunol 207:77-93.
9. Hartl FU. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-579.
10. Hebert DN, Molinari M. 2007. In and out of the ER: Protein folding, quality control, degradation, and related human diseases. Physiol Rev 87:1377-1408. (Pubitemid 350041473)
11. Hetz C, Soto C. 2003. Protein misfolding and disease: The case of prion disorders. Cell Mol Life Sci 60:133-143. (Pubitemid 36223122)
12. Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. 2003. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 22:5435-5445. (Pubitemid 37279953)
13. Hetz C, Russelakis-Carneiro M, Walchli S, Carboni S, Vial-Knecht E, Maundrell K, Castilla J, Soto C. 2005. The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity. J Neurosci 25:2793-2802. (Pubitemid 40389237)
14. Hirsch C, Jarosch E, Sommer T, Wolf DH. 2004. Endoplasmic reticulumassociated protein degradation-one model fits all? Biochim Biophys Acta 1695:215-223.
15. Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. 1999. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell 4:331-341. (Pubitemid 29499786)
16. Jin T, Gu Y, Zanusso G, Sy M, Kumar A, Cohen M, Gambetti P, Singh N. 2000. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J Biol Chem 275:38699-38704. (Pubitemid 32009203)
17. Kang SJ, Cresswell P. 2002. Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain. J Biol Chem 277:44838-44844. (Pubitemid 36159078)
18. Lehmann S, Harris DA. 1997. Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J Biol Chem 272:21479-21487. (Pubitemid 27374021)
19. Ma J, Lindquist S. 2001. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci USA 98:14955-14960. (Pubitemid 34013951)
20. Ma J, Wollmann R, Lindquist S. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785. (Pubitemid 35404120)
21. Ou WJ, Cameron PH, Thomas DY, Bergeron JJ. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771-776.
22. Prusiner SB. 1997. Prion diseases and the BSE crisis. Science 278:245-251.
23. Rajagopalan S, Xu Y, Brenner MB. 1994. Retention of unassembled components of integral membrane proteins by calnexin. Science 263:387-390. (Pubitemid 24067946)
24. Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB. 1999. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and nonglycosylated proteins. EMBO J 18:6718-6729.
25. Sitia R, Braakman I. 2003. Quality control in the endoplasmic reticulum protein factory. Nature 426:891-894.
26. Soto C. 2003. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4:49-60.
27. Soto C, Estrada LD. 2008. Protein misfolding and neurodegeneration. Arch Neurol 65:184-189.
28. Spiro RG, Zhu Q, Bhoyroo V, Soling HD. 1996. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J Biol Chem 271:11588-11594.
29. Sun G, Guo M, Shen A, Mei F, Peng X, Gong R, Guo D, Wu J, Tien P, Xiao G. 2005. Bovine PrPC directly interacts with alphaB-crystalline. FEBS Lett 579:5419-5424.
30. Suzuki T, Park H, Hollingsworth NM, Sternglanz R, Lennarz WJ. 2000. PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. J Cell Biol 149:1039-1052.
31. Thammavongsa V, Mancino L, Raghavan M. 2005. Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein. J Biol Chem 280:33497-33505.
32. Wada I, Rindress D, Cameron PH, Ou WJ, Doherty JJ II, Louvard D, Bell AW, Dignard D, Thomas DY, Bergeron JJ. 1991. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem 266:19599-19610.
33. Ware FE, Vassilakos A, Peterson PA, Jackson MR, Lehrman MA, Williams DB. 1995. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J Biol Chem 270:4697-4704.
34. Williams DB. 2006. Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119:615-623.
35. Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A. 2001. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J 20:5383-5391.
36. Yin SM, Zheng Y, Tien P. 2003. On-column purification and refolding of recombinant bovine prion protein: Using its octarepeat sequences as a natural affinity tag. Protein Expr Purif 32:104-109.
37. Zapun A, Petrescu SM, Rudd PM, Dwek RA, Thomas DY, Bergeron JJ. 1997. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88:29-38.