Influence of molecular and chemical chaperones on protein folding

Cell Stress and Chaperones

Volumn 1, Issue 2, 1996, Pages 109-115

  Welch, William J ^a   Brown, C Randell ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

HUMAN; PHYSIOLOGY; PROTEIN FOLDING; REVIEW;

HUMANS; MOLECULAR CHAPERONES; PROTEIN FOLDING;

EID: 0030154323     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(1996)001<0109:IOMACC>2.3.CO;2     Document Type: Review

References (34)

1. Brown CR, Hong-Brown LQ, Biwersi J, Verkman AS and Welch WJ (1996) Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chap. 1 (2), 117-125.
2. Burg MB (1995) Molecular basis of osmotic regulation. Am. J. Physiol. 268, F983-F996.
3. Cheng SH, Gregory RJ, Marshall J, et al (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63, 827-834.
4. Cohen DM, Wasserman JC and Gullans SR (1991) Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells. Am J. Physiol. 261, C594-C601.
5. Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ and Prusiner SB (1994) Structural clues to prion replication. Science 264, 530-531.
6. Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE and Welsh MJ (1992) Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358, 761-764.
7. Edington BV, Whelan SA and Hightower LE (1989) Inhibition of heat shock (stress) protein induction by deuterium oxide and glycerol: additional support for the abnormal protein hypothesis of induction. J. Cell. Physiol. 139, 219-228.
8. Ellis RJ and van der Vies SM (1991) Molecular chaperones. Ann. Rev. Biochem. 60, 321-347.
9. Garcia-Perez A and Burg MB (1991) Renal medullary organic osmolytes. Physiol. Rev. 71, 1081-1115.
10. Gekko K and Timasheff SN (1981a) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20, 4667-4676.
11. Gekko K and Timasheff SN (1981b) Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry 20, 4677-4686.
12. Georgopoulos C and Welch WJ (1993) Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634.
13. Hammond C and Helenius A (1995) Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
14. Henle KJ, Peck JW and Higashibuko R (1983) Protection against heat-induced cell killing by polyols in vitro. Cancer Res. 43, 1624-1633.
15. Kenward N, Landon M, Lajos L and Mayer RJ (1996) Heat shock proteins, molecular chaperones and the prion encephalopathies. Cell Stress Chap. 1, 18-23.
16. 1-amitrypsin. J. Biol. Chem. 269 (10), 7514-7519.
17. Lin PS, Kwock L, and Hefter K (1981) Protection of heat induced cytotoxicity by glycerol. J. Cell. Physiol. 108, 439-448.
18. Pan KM, Baldwin M, Nguyen J, et al (1993) Conversion of a-helices into b-sheets features in the formation of the scrapie prion protein. Proc. Natl. Acad. Sci. USA 90, 10962-10966.
19. Pind S, Riordan JR and Williams DB (1994) Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269, 12784-12788.
20. Prusiner SB and DeArmond SJ (1994) Prion diseases and neurodegeneration. Annu. Rev. Neurosci. 17, 311-339.
21. Riordan JR (1993) The cystic fibrosis transmembrane conductance regulator. Annu. Rev. Physiol. 55, 609-630.
22. Riordan JR, Rommens JM, Kerem BS, et al (1989) Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066-1072.
23. Sadis SE and Hightower LE (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31, 9406-9412.
24. Sato S, Ward CL, Krouse ME, Wine JJ and Kopito RR (1996) Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271 (2), 635-638.
25. Schein CH (1990) Solubility as a function of protein structure and solvent components. Bio/Technol. 8, 308-316.
26. Selkoe DJ (1994) Normal and abnormal biolgy of beta-amyloid precursor protein. Annu. Rev. Neurosci. 17, 489-517.
27. Scheik-Hamad D, Garcia-Perez A, Ferraris JD, Peters EM and Burg MB (1994) Induction of gene expression by heat shock versus osmotic stress. Am. J. Physiol. 267, F28-F34.
28. Somero G (1986) Protons, osmolytes, and fitness of internal milieu for protein function. Am J. Physiol. 251, R197-R213.
29. Tatzelt J, Prusiner SB and Welch WJ (1996) Chemical chaperones interfere with the formation of scrapie prion protein. Mol. Cell. Biol. (submitted).
30. Teckman J and Perlmutter DH (1995) Conceptual advances in the pathogenesis and treatment of childhood metabolic liver disease. Gastroenterology 108, 1263-1279.
31. Thomas PJ, Qu BH and Pedersen PL (1995) Defective protein folding as a basis of human disease. TIBS 20, 456-459.
32. Yancey PH, Clark ME, Hand SC, Bowlus RD and Somero GN (1982) Living with water stress: evolution of osmolyte systems. Science 217, 1214-1222.
33. Yang Y, Janich S, Cohn JA and Wilson JM (1993) The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. USA 90, 9480-9484.
34. 1-antitrypsin causes a protein folding defect Struct. Biol. 2, 363-367