The Z type variation of human -α1 antitrypsin causes a protein folding defect

Nature Structural Biology

Volumn 2, Issue 5, 1995, Pages 363-367

  Yu, Myeong Hee ^a   Lee, Kee Nyung ^a   Kim, Jeongho ^a,b  

^a Korea Institute of Science and Technology   (South Korea)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN;

ALPHA 1 ANTITRYPSIN DEFICIENCY; ARTICLE; CONFORMATIONAL TRANSITION; EMPHYSEMA; HUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN POLYMERIZATION; PROTEIN STABILITY;

ALPHA 1-ANTITRYPSIN; AMINO ACIDS; ANIMAL; CRYSTALLIZATION; ELECTROPHORESIS; EMPHYSEMA; HUMAN; LIVER; MUTATION; PANCREATIC ELASTASE; PROTEIN FOLDING; RADIOISOTOPES; SUPPORT, NON-U.S. GOV'T;

EID: 0029048542     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0595-363     Document Type: Article

References (30)

1. Huber, R. and Carrell, R.W. Implications of the three-dimensional structure of cq-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966 (1989).
2. Loebermann, H., Tokuoka, R., Deisenhofer, J. and Huber, R. Human a-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J molec. Biol. 177, 531-556 (1984).
3. Crystal, R.G. The oq-antitrypsin gene and Its deficiency states. Trends Genet. 5, 411-417 (1989).
4. Stein, P.E. and Carrell, R.W. What do dysfunctional serpins tell usabout molecular mobility and disease? Nature struct. Biol. 2, 96-113 (1995).
5. Lomas, D.A., Evans, D.L., Finch, J.T. and Carrell, R.W. The mechanism of Z a,-antitrypsin accumulation In the liver. Nature 357, 605-607 (1992).
6. Lomas, D.A., Evans, D.L., Stone, S.R., Chang, W.-S.W. and Carrell, R.W. Effect of the Z mutation on the physical and Inhibitory properties of oq-antitrypsin. Biochemistry 32, 500-508 (1993).
7. Carrell, R.W., Evans, D.L. and Stein, P.E. Mobile reactive centre of serpins and the control of thrombosis. Nature 353, 576-578 (1991).
8. Carrell, R.W. and Evans, D.L.I. Serpins: mobile conformations in a family of proteinase inhibitors. Curr. Opin. struct. Biol. 2, 438-446 (1992).
9. Verbanac, K.M. and Heath, E.C. Biosynthesis, processing, and secretion of M and Z variant human a,-antitrypsin. J. biol. Chem. 261, 9979-9989 (1986).
10. Le, A., Ferrell, D.A., Dishon, D.S., Le, Q.-Q.A. and Sifers, R.N. Soluble aggregates of the human PiZcq-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J biol. Chem. 267, 1072-1080 (1992).
11. Creighton, T.E. Electrophoretic analysis of the unfolding of proteins by urea. J molec. Biol. 129, 235-264 (1979).
12. Creighton, T.E. Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J molec. Biol. 137, 61-80 (1980).
13. Craig, S., Hollecker, M., Creighton, T.E. and Pain, R.H. Single amino acid mutations block a late step in the folding of p-lactamase from Staphylococcus aureus. J. molec. Biol. 185, 681-687 (1985).
14. Bathurst, I.C., Travis, J, George, P.M. and Carrell, R.W. Structural and functional characterization of the abnormal Z oq-antitrypsin Isolated from human liver. FEBS Lett. 177, 179-183 (1984).
15. Ogushi, F., Fells, G. A., Hubbard, R. C., Straus, S. D., and Crystal, R. G. Z-type oq-antitrypsin is less competent than M1 -typea,-antitrypsin as an inhibitor of neutrophil elastase. J. din. Invest. 80, 1366-1374 (1987).
16. Carrell, R.W., Stein, P.E., Fermi, G. and Wardell, M.R. Biological implications of a 3 Â structure of dimeric antithrombin. Structure 2, 257-270 (1994).
17. Schreuder, H. A. etal. The intact and cleaved human antithrombin III complex as a model for serpin-protease interactions. Nature Struct. Biol. 1, 48-54 (1994).
18. Ou, W.-J., Cameron, P.H., Thomas, D.Y., and Bergeron, J.J.M. Association of folding Intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776 (1993).
19. 1-antitrypsin. J biol. Chem. 269, 7514-7519 (1994).
20. Hammond, C., Braakman, I., and Helenius, A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. natn. Acad. Sci. U.S.A 91, 913-917 (1994).
21. Wu, Y. et al. A lag In Intracellular degradation of mutant oq- antltrypsin correlates with the liver disease phenotype in homozygous PiZZ oq-antitrypsin deficiency. Proc. natn. Acad. Sci. U.S.A. 91, 9014-9018 (1994).
22. Thomas, P.J., Ko, Y.H. and Pedersen, PL. Altered protein folding may be the molecular basis of most cases of cystic fibrosis. FEBS Lett. 312, 7-9 (1992).
23. Welsh, M.J. and Smith, A.E. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73, 1251-1254 (1993).
24. Thomas, PJ. and Pedersen, P.L. Effects of the AF508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR. J Bioenergetics Biomembr. 25, 11-19 (1993).
25. Kocisko, D.A. et al. Cell-free formation of protease-resistant prion protein. Nature 370, 471-474 (1994).
26. Cohen, F.E. et al. Structural clues to prion replication. Science 264, 530-531 (1994).
27. Goldenberg, D P Analysis of protein conformation by gel electrophoresis, in Protein Structure: A practical Approach, (ed. Creighton, T.E.) 225-250 (IRL press. New York; 1989).
28. Kwon, K.-S., Kim, J., Shin, H.S. and Yu, M.-H. Single amino acid substitutions of oq-antitrypsin that confer enhancement in thermal stability. J biol. Chem. 269, 9627-9631 (1994).
29. Kunkel, T. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. natn. Acad. Sci. U.S.A. 82, 488-492 (1985).
30. Edelhoch, H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954 (1967).