Activation of Endoplasmic Reticulum-Specific Stress Responses Associated with the Conformational Disease Z α1-Antitrypsin Deficiency

Journal of Immunology

Volumn 172, Issue 9, 2004, Pages 5722-5726

  Lawless, Matthew W ^a   Greene, Catherine M ^a   Mulgrew, Alan ^a   Taggart, Clifford C ^a   O'Neill, Shane J ^a   McElvaney, Noel G ^a  

^a BEAUMONT HOSPITAL   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN;

ALPHA 1 ANTITRYPSIN DEFICIENCY; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DRUG DESIGN; ENDOPLASMIC RETICULUM; ENZYME DEFICIENCY; GENETIC DISORDER; HUMAN; HUMAN CELL; IN VITRO STUDY; LIVER CELL; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN FOLDING; STRESS;

EID: 2142768895     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.9.5722     Document Type: Article

References (27)

1. Brantly, M., T. Nukiwa, and R. G. Crystal. 1988. Molecular basis of α-1 antitrypsin deficiency. Am. J. Med. 84:13.
2. Sveger, T. 1976. Liver disease in α-1-antitrypsin deficiency detected by screening of 200,000 infants. N. Engl. J. Med. 294:1316.
3. Sveger, T. 1988. The natural history of liver disease in α-1-antitrypsin deficient children. Acta Pediatr. Scand. 77:847.
4. Eriksson, S., J. Carlson, and R. Velez. 1986. Risk of cirrhosis and primary liver cancer in α1-antitrypsin deficiency N. Engl. J. Med. 314:736.
5. Birrer, P., N. G. McElvaney, L. M. Chang-Stroman, and R. G. Crystal. 1991. α-1-Antitrypsin deficiency and liver disease. J. Inherit. Metab. Dis. 14:512.
6. McCracken, A. A., K. B. Kruse, and J. L. Brown. 1989. Molecular basis for defective secretion of the Z variant of human α-1-proteinase inhibitor: secretion of variants having altered potential for salt bridge formation between amino acids 290 and 342. Mol. Cell. Biol. 9:1406.
7. Lomas, D. A., D. L. Evans, J. T. Finch, and R. W. Carrell. 1992. The mechanism of Z α-1-antitrypsin accumulation in the liver. Nature 357:605.
8. Le, A., K. S. Graham, and R. N. Sifers. 1990. Intracellular degradation of the transport-impaired human PiZ α1-antitrypsin variant: biochemical mapping of the degradative event among compartments of the secretory pathway. J. Biol. Chem. 265:14001.
9. Le, A., G. A. Ferrell, D. S. Dishon, Q. Q. Le, and R. N Sifers. 1992. Soluble aggregates of the human PiZ α1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J. Biol. Chem. 267:1072
10. Welihinda, A. A., W. Tirasophon, and R. J. Kaufman. 1999. The cellular response to protein misfolding in the endoplasmic reticulum. Gene Expression 7:293.
11. Pahl, H. L., and P. A. Baeuerle. 1995. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB. EMBO J. 14:2580.
12. Kozutsumi, Y., M. Segal, K. Normington, M. J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332:462.
13. Yoshida, H., K. Haze, H. Yanagi, T. Yura, and K. Mori. 1998. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins: involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273:33741.
14. McElvaney, N. G., R. C. Hubbard, P. Birrer, M. S. Chernick, D. B. Caplan, M. M. Frank, and R. G. Crystal. 1991. Aerosol α1-antitrypsin treatment for cystic fibrosis. Lancet 337:392.
15. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.
16. Novoradovskaya, N., J. Lee, Z. X. Yu, V. J. Ferrans, and M. Brantly. 1998. Inhibition of intracellular degradation increases secretion of a mutant form of α1-antitrypsin associated with profound deficiency. J. Clin. Invest. 101:2693.
17. Jiang, H.-Y., S. A. Wek, B. C. McGrath, D. Scheuner, R. J. Kaufman, D. R. Cavaner, and R. C. Wek. 2003. Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses. Mol. Cell. Biol. 23:5651.
18. Sveger, T. 1978. α1-Antitrypsin deficiency in early childhood. Pediatrics 62:22.
19. McMillan, D. R., M. J. Gething, and J. Sambrook. 1994. The cellular response to unfolded proteins: intercompartmental signaling. Curr. Opin. Biotechnol. 5:540.
20. Berridge, M. J. 2002. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32:235.
21. Ron, D. 2002. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. 110:1383.
22. 2+-ATPase. Proc. Natl. Acad. Sci. USA 87:2466.
23. Teckman, J. H., J. Burrows, T. Hidvegi, B. Schmidt, P. D. Hale, and D. H. Perlmutter. The proteasome participates in degradation of mutant of α1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes. J. Biol. Chem. 276:44865.
24. Burrows, J. A., L. K. Willis, and D. H. Perlmutter. 2000. Chemical chaperones mediate increased secretion of mutant of α1-antitrypsin (α1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency. Proc. Natl. Acad. Sci. USA 97:1796.
25. Bucciantini, M., E. Giannoni, F. Chiti. F. Baroni, L. Formigli, J. Zurdo, N. Taddei, G. Ramponi, C. M. Dobson, and M. Stefani. 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416:507.
26. Chen, L., and X. Gao. 2002. Neuronal apoptosis induced by endoplasmic reticulum stress. Neurochem. Res. 27:891.
27. 1-antitrypsin-related cirrhosis. J. Biol. Chem. 277:6771.