Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion

Journal of Thrombosis and Haemostasis

Volumn 2, Issue 7, 2004, Pages 1143-1154

  Enjolras, Nathalie ^a   Plantier, J L ^a   Rodriguez, M H ^a   Rea, M ^a   Attali, O ^a   Vinciguerra, C ^a   Negrier, C ^a  

^a UNIVERSITÉ LYON 1   (France)

Author keywords

Chaperone and lectin molecules; Factor IX; Hemophilia B; Impaired secretion; In vitro mutagenesis; Intracellular retention and degradation

Indexed keywords

BLOOD CLOTTING FACTOR 9; CALRETICULIN; CHAPERONE; CYSTEINE PROTEINASE; EPIDERMAL GROWTH FACTOR; GLUCOSE REGULATED PROTEIN 78; LECTIN; PROTEASOME;

ANIMAL CELL; ARTICLE; CELL ACTIVITY; CELL SECRETION; CELL STRAIN HEPG2; CELL TRANSPORT; CHO CELL; CONCENTRATION (PARAMETERS); CONFOCAL MICROSCOPY; CONTROLLED STUDY; CROSS REACTION; CULTURE MEDIUM; DISEASE SEVERITY; ENDOPLASMIC RETICULUM; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; GENE MUTATION; GENETIC TRANSFECTION; GLYCOSYLATION; GOLGI COMPLEX; HEMOPHILIA B; HUMAN; HUMAN CELL; IMMUNOBLOTTING; NONHUMAN; NORTHERN BLOTTING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN SYNTHESIS; SIALYLATION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

BIOLOGICAL TRANSPORT; CELL COMPARTMENTATION; CELL LINE, TUMOR; EPIDERMAL GROWTH FACTOR; FACTOR IX; HUMANS; LECTINS; MOLECULAR CHAPERONES; MUTATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; TRANSFECTION;

EID: 13244271981     PISSN: 15387933     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2004.00756.x     Document Type: Article

References (38)

1. Choo KH, Gould KG, Rees DJ, Brownlee GG. Molecular cloning of the gene for human anti-haemophilic factor IX. Nature 1982; 29 178-80.
2. Kurachi K, Davie EW. Isolation and characterization of a cDNA coding for human factor IX. Proc Natl Acad Sci USA 1982; 79: 6461-4.
3. Freedman SJ, Furie BC, Furie B, Baleja JD. Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem 1995; 270: 7980-7.
4. Agarwala KL, Kawabata S, Takao T, Murata H, Shimonishi Y, Nishimura H, Iwanaga S. Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169. Biochemistry 1994; 33: 5167-71.
5. Bharadwaj D, Harris RJ, Kisiel W, Smith KJ. Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity. J Biol Chem 1995; 270: 6537-42.
6. Kaufman RJ. Post-translational modifications required for coagulation factor secretion and function. Thromb Haemost 1998; 79: 1068-79.
7. Bond M, Jankowski M, Patel H, Karnik S, Strang A, Xu B, Rouse J, Koza S, Letwin B, Steckert J, Amphlett G, Scoble H. Biochemical characterization of recombinant factor IX. Semin Hematol 1998; 35: 11-7.
8. Ruddon RW, Bedows E. Assisted protein folding. J Biol Chem 1997; 272: 3125-8.
9. Sidrauski C, Chapman R, Walter P. The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol 1998; 8: 245-9.
10. Ellgaard L, Helenius A. ER quality control: towards an understanding at the molecular level. Curr Opin Cell Biol 2001; 13: 431-7.
11. Morris JA, Dorner AJ, Edwards CA, Hendershot LM, Kaufman RJ. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J Biol Chem 1997; 272: 4327-34.
12. Lee AS. Mammalian stress response: induction of the glucose-regulated protein family. Curr Opin Cell Biol 1992; 4 267-73.
13. Lee AS. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 2001; 26: 504-10.
14. Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 1999; 10: 465-72.
15. Argon Y, Simen BB. GRP94, an ER chaperone with protein and peptide binding properties. Semin Cell Dev Biol 1999; 10: 495-505.
16. Attali O, Vinciguerra C, Trzeciak MC, Durin A, Pernod G, Gay V, Menart C, Sobas F, Dechavanne M, Negrier C. Factor IX gene analysis in 70 unrelated patients with haemophilia B: description of 13 new mutations. Thromb Haemost 1999; 82: 1437-42.
17. Enjolras N, Rodriguez MH, Plantier JL, Maurice M, Attali O, Negrier C. The three in-frame ATG, clustered in the translation initiation sequence of human factor IX gene, are required for an optimal protein production. Thromb Haemost 1999; 82: 1264-9.
18. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K. Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 1985; 24: 3736-50.
19. Anson DS, Choo KH, Rees DJ, Giannelli F, Gould K, Huddleston JA, Brownlee GG. The gene structure of human anti-haemophilic factor IX. EMBO J 1984; 3: 1053-60.
20. Pittman DD, Kaufman RJ. Site-directed mutagenesis and expression of coagulation factors VIII and V in mammalian cells. Methods Enzymol 1993; 222: 236-60.
21. Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999; 286: 1882-8.
22. Van den Steen P, Rudd PM, Dwek RA, Opdenakker G. Concepts and principles of O-tinked glycosylation. Crit Rev Biochem Mol Biol 1998; 33: 151-208.
23. Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ. PACE/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J Biol Chem 1993; 268: 8458-65.
24. Bottema CD, Bottema MJ, Ketterling RP, Yoon HS, Janco RL, Phillips JA 3rd, Sommer SS. Why does the human factor IX gene have a G + C content of 40%? Am J Hum Genet 1991; 49: 839-50.
25. Drost JB, Scaringe WA, Jaloma-Cruz AR, Li X, Ossa DF, Kasper CK, Sommer SS. Novel hotspot detector software reveals a non-CpG hotspot of germline mutation in the factor IX gene (F9) in Latin Americans. Hum Mutat 2000; 16: 203-10.
26. Tartary M, Vidaud D, Piao, Y, Costa JM, Bahnak BR, Fressinaud E, Congard B, Laurian Y, Meyer D, Lavergne JM, Vidaud M. Detection of a molecular defect in 40 of 44 patients with haemophilia B by PCR and denaturing gradient gel electrophoresis. Br J Haematol 1993; 84 662-9.
27. Hunault M, Arbini AA, Carew JA, Peyvandi F, Bauer KA. Characterization of two naturally occurring mutations in the second epidermal growth factor-like domain of factor VII. Blood 1999; 93: 1237-44.
28. Debiasi RL, Squier MK, Pike B, Wynes M, Dermody TS, Cohen JJ, Tyler KL. Reovirus-induced apoptosis is preceded by increased cellular calpain activity and is blocked by calpain inhibitors. J Virol 1999; 73: 695-701.
29. Milligan SA, Owens MW, Grisham MB. Inhibition of IkappaB-alpha and IkappaB-beta proteolysis by calpain inhibitor I blocks nitric oxide synthesis. Arch Biochem Biophys 1996; 335: 388-95.
30. Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78: 761-71.
31. Frydman J, Hard FU. Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science 1996; 272: 1497-502.
32. Wu X, Sakata N, Lele KM, Zhou M, Jiang H, Ginsberg HN. A two-site model for ApoB degradation in HepG2 cells. J Biol Chem 1997; 272: 11575-80.
33. Brostrom CO, Brostrom MA. Regulation of translational initiation during cellular responses to stress. Prog Nucl Acid Res Mol Biol 1998; 58: 79-125.
34. Iwawaki T, Hosoda A, Okuda T, Kamigori Y, Nomura-Furuwatari C, Kimata Y, Tsuru A, Kohno K. Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress. Nat Cell Biol 2001; 3: 158-64.
35. Pipe SW, Morris JA, Shah J, Kaufman RJ, Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem 1998; 273: 8537-44.
36. Arbini AA, Mannucci M, Bauer KA. A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 1996; 87: 5085-94.
37. Katsumi A, Senda T, Yamashita Y, Yamazaki T, Hamaguchi M, Kojima, T, Kobayashi S, Saito H. Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 1996; 87: 4164-75.
38. Allen S, Goodeve AC, Peake IR, Daly ME. Prolonged association of Arg273Trp von Willbrand factor with ERp57 and calnexin. Thromb Haemost 2001 (Suppl. July): OC888.