Characterization and suppression of dysfunctional human α1-antitrypsin variants

Biochemical and Biophysical Research Communications

Volumn 343, Issue 1, 2006, Pages 295-302

  Kim, Min Jung ^a   Jung, Chan Hun ^a   Im, Hana ^a  

^a Sejong University   (South Korea)

Author keywords

1 Antitrypsin; Conformational stability; Dysfunctional variants; Inhibitory activity; Pathogenic mutations; Serine protease inhibitors

Indexed keywords

ALPHA 1 ANTITRYPSIN;

ARTICLE; EMPHYSEMA; GEL ELECTROPHORESIS; LIVER; MUTATION; PRIORITY JOURNAL; PROTEIN VARIANT; WILD TYPE;

ALPHA 1-ANTITRYPSIN; HEAT; HUMANS; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 33645101994     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.151     Document Type: Article

References (32)

1. 1-antitrypsin Nat. Struct. Biol. 3 1996 676 681
2. 1-antitrypsin is in the canonical inhibitory conformation J. Mol. Biol. 275 1998 419 425
3. 1-proteinase inhibitor J. Biol. Chem. 253 1978 7142 7144
4. 1-antitrypsin: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function J. Mol. Biol. 177 1984 531 556
5. E. Stratikos, and P.G.W. Gettins Major proteinase movement upon stable serpin-proteinase complex formation Proc. Natl. Acad. Sci. USA 94 1997 453 458
6. J.A. Huntington, R.J. Read, and R.W. Carrell Structure of a serpin-protease complex shows inhibition by deformation Nature 407 2000 923 926
7. M.I. Plotnick, L. Mayne, N.M. Schecter, and H. Rubin Distortion of the active site of chymotrypsin complexed with a serpin Biochemistry 35 1996 7586 7590
8. M. Bruch, V. Weiss, and J. Engel Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites J. Biol. Chem. 263 1988 16626 16630
9. 1-antitrypsin for structure and function of serpins Biochemistry 28 1989 8951 8966
10. P.E. Stein, and R.W. Carrell What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2 1995 96 113
11. 1-antitrypsin J. Biol. Chem. 274 1999 11072 11077
12. C. Lee, S.-H. Park, M.-Y. Lee, and M.-H. Yu Regulation of protein function by native metastability Proc. Natl. Acad. Sci. USA 97 2000 7727 7731
13. 1-antitrypsin by the native strain distributed throughout the molecule J. Biol. Chem. 277 2002 14216 14220
14. 1-antitrypsin and its association with protease inhibitor function J. Biol. Chem. 275 2000 16904 16909
15. 1- antitrypsin Nature 298 1982 329 334
16. 1-antitrypsin deficiency Am. J. Med. 84 1988 13 31
17. 1-antitrypsin null allele involving aberrant mRNA splicing Hum. Mol. Genet. 2 1993 1001 1005
18. 1-antitrypsin causes a protein folding defect Nat. Struct. Biol. 2 1995 363 367
19. 1-antitrypsin D256V and L41P variants Protein Sci. 13 2004 694 702
20. malton by stabilizing mutations Biochem. Biophys. Res. Commun. 325 2004 744 750
21. J. Mottonen, A. Strand, J. Symersky, R.M. Sweet, D.E. Danley, K.F. Geoghegan, R.D. Gerard, and E.J. Goldsmith Structural basis of latency in plasminogen activator inhibitor-1 Nature 355 1992 270 273
22. 1-antitrypsin Pittsburgh (358Met → Arg), a fatal bleeding disorder N. Engl. J. Med. 309 1983 694 698
23. 1-antitrypsin deficiency N. Engl. J. Med. 314 1986 736 739
24. D.A. Lomas, J.T. Finch, K. Seyama, T. Nukiwa, and R.W. Carrell Alpha 1-antitrypsin Siiyama (Ser53 → Phe): further evidence for intracellular loop-sheet polymerization J. Biol. Chem. 268 1993 15333 15335
25. H. Im, and M.-H. Yu Role of Lys335 in the metastability and function of inhibitory serpins Protein Sci. 9 2000 934 941
26. T.A. Kunkel, J.D. Roberts, and R.A. Zakour Rapid and efficient site-specific mutagenesis without phenotypic selection Methods Enzymol. 154 1987 367 382
27. 1-antitrypsin that confer enhancement in thermal stability J. Biol. Chem. 269 1994 9627 9631
28. H. Edelhoch Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6 1967 1948 1954
29. D.P. Goldenberg Analysis of protein conformation by gel electrophoresis T.E. Creighton Protein Structure: A Practical Approach 1989 IRL Press, Oxford University Press Oxford, UK 225 250
30. J. Bieth, B. Spiess, and C.G. Wermuth The synthesis and analytical use of a highly sensitive and convenient substrate of elastase Biochem. Med. 11 1974 350 357
31. 1-antitrypsin accumulation in the liver Nature 357 1992 605 607
32. H. Im, M.-S. Woo, K.Y. Hwang, and M.-H. Yu Interactions causing the kinetic trap in serpin protein folding J. Biol. Chem. 277 2002 46347 46354