Post-translational Modifications Required for Coagulation Factor Secretion and Function

• References

• 1 Ratnoff OD, Davie EW. Waterfall sequence for intrinsic blood clotting.. Science 1964; 145: 1310.
• 2 MacFarlane RG. An Enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier.. Nature 1964; 202: 498.
• 3 Connelly S, Kaleko M. Gene therapy for hemophilia A.. Thromb Haemost 1997; 78: 31-6.
• 4 Eisensmith RC, Woo SL. Viral vector-mediated gene therapy for hemophilia B.. Thromb Haemost 1997; 78: 24-30.
• 5 Davie EW. Biochemical and molecular aspects of the coagulation cascade.. Thromb Haemost 1995; 74: 1-6.
• 6 Vehar GA, Keyt B, Eaton D. et al. Structure of human factor VIII.. Nature 1984; 312: 337-42.
• 7 Toole JJ, Knopf JL, Wozney JM. et al. Molecular cloning of a cDNA encoding human antihemophilic factor.. Nature 1984; 312: 342-7.
• 8 Bihoreau N, Pin S, de Kersabiec AM, Vidot F, Fontaine-Aupart MP. Copper-atom identification in the active and inactive forms of plasma-derived FVIII and recombinant FVIII-delta II.. Eur J Biochem 1994; 222: 41-8.
• 9 Mann KG, Lawler CM, Vehar GA, Church WR. Coagulation Factor V contains copper ion.. J Biol Chem 1984; 259: 12949-51.
• 10 Tagliavacca L, Moon N, Dunham WR, Kaufman RJ. Identification and functional requirement of Cu(II) and its ligands within coagulation factor VIII.. J Biol Chem 1997; 272: 27428-34.
• 11 Esmon CT. The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity.. J Biol Chem 1979; 254: 964-73.
• 12 Nesheim ME, Myrmel KH, Hibbard L, Mann KG. Isolation and characterization of single chain bovine factor V.. J Biol Chem 1979; 254: 508-17.
• 13 Mannucci PM, Tenconi PM, Castaman G, Rodeghiero F. Comparison of four virus-inactivated plasma concentrates for treatment of severe von Willebrand disease: a cross-over randomized trial.. Blood 1992; 79: 3130-7.
• 14 Weiss HJ, Sussman II, Hoyer LW. Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand‘s disease.. J Clin Invest 1977; 60: 390-404.
• 15 Kaufman RJ, Wasley LC, Dorner AJ. Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells.. J Biol Chem 1988; 263: 6352-62.
• 16 Monkovic DD, Tracy PB. Activation of human factor V by factor Xa and thrombin.. Biochemistry 1990; 29: 1118-28.
• 17 Lollar P, Fay PF, Fass DN. Factor VIII and factor VIIIa.. Methods Enzymol 1993; 222: 128-42.
• 18 Eaton D, Rodriguez H, Vehar GA. Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity.. Biochemistry 1986; 25: 505-12.
• 19 Lollar P, Parker CG. Subunit structure of thrombin-activated porcine factor VIII.. Biochemistry 1987; 28: 666-74.
• 20 Fay PJ, Haidaris PJ, Smudzin TM. Human factor VIIIa subunit structure.. J Biol Chem 1991; 266: 8957-62.
• 21 Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites.. Protein Eng 1997; 10: 1-6.
• 22 Martoglio B, Hofmann MW, Brunner J, and Dobberstein B. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer.. Cell 1995; 81: 207-14.
• 23 Kemball-Cook G, Tuddenham EGD. The factor VIII mutation database on the World Wide Web: the Haemophilia A mutation search test and resource site. HAMSTeRS update (Version 3. 0).. Nucleic Acids Res 1997; 25: 128.
• 24 Giannelli F, Green PM, Sommer SS. et al. Haemophilia B: database of point mutations and short additions and deletions-eighth edition.. Nucleic Acids Res 1998; 26: 267-70.
• 25 Xue J, Kalafatis M, Silveira JR, Kung C, Mann KG. Determination of the disulfide bridges in factor Va heavy chain.. Biochemistry 1994; 33: 13109-16.
• 26 Xue J, Kalafatis M, Mann KG. Determination of the disulfide bridges in factor Va light chain.. Biochemistry 1993; 32: 5917-23.
• 27 McMullen BA, Fujikawa K, Davie EW, Hedner U, Ezban M. Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A).. Protein Sci 1995; 4: 740-6.
• 28 Noiva R, Lennarz WJ. Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum.. J Biol Chem 1992; 267: 3553-6.
• 29 Silberstein S, Collins PG, Kelleher DJ, Rapiejko PJ, Gilmore R. Thesubunit of the Saccharomyces cerevisiae oligosaccharyltransferase complex is essential for vegetative growth of yeast and is homologous to mammalian ribophorin I.. J Cell Biol 1995; 128: 525-36.
• 30 Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.. Mol Biol Cell 1994; 5: 253-65.
• 31 Dorner AJ, Bole DG, Kaufman RJ. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins.. J Cell Biol 1987; 105: 2665-74.
• 32 Guan JL, Machamer CE, Rose JK. Glycosylation allows cell-surface transport of an anchored secretory protein.. Cell 1985; 42: 489-96.
• 33 Kelleher DJ, Kreibich G, Gilmore R. Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein.. Cell 1992; 69: 55-65.
• 34 Gavel Y, von Heijne G. Sequence differences between glycosylated and non-glycosylated Asn-X- Thr/Ser acceptor sites: implications for protein engineering.. Protein Eng 1990; 3: 433-42.
• 35 Hebert DN, Foellmer B, Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum.. Cell 1995; 81: 425-33.
• 36 Trombetta SE, Parodi AJ. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase.. J Biol Chem 1992; 267: 9236-40.
• 37 McClure DB, Walls JD, Grinnell BW. Post-translational processing events in the secretion pathway of human protein C, a complex vitamin K-dependent antithrombotic factor.. J Biol Chem 1992; 267: 19710-7.
• 38 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.
• 39 Elbein AD. Glycosidase inhibitors as antiviral and/or antitumor agents.. Semin Cell Biol 1991; 2: 309-17.
• 40 Wilson IB, Gavel Y, von Heijne G. Amino acid distributions around O-linked glycosylation sites.. Biochem J 1991; 275: 529-34.
• 41 Dorner AJ, Kaufman RJ. Analysis of synthesis, processing, and secretion of proteins expressed in mammalian cells.. Methods Enzymol 1990; 185: 577-96.
• 42 Tarentino AL, Maley F. Purification and properties of an endo-beta-Nacetylglucosaminidase from Streptomyces griseus.. J Biol Chem 1974; 249: 811-7.
• 43 Tarentino AL, Gomez CM, Plummer Jr. TH. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F.. Biochemistry 1985; 24: 4665-71.
• 44 Stanley P. Lectin-Resistant Glycosylation Mutants.. In: Gottesman MM. (Ed) Molecular Cell Genetics.. New York: John Wiley and Sons; 1985: 745-72.
• 45 Kaufman RJ, Swaroop M, Murtha-Riel P. Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells.. Biochemistry 1994; 33: 9813-9.
• 46 Wasley CL, Horgan P, Timony G, Stoudemier J, Krieger M, Kaufman RJ. The importance of N- and O-linked oligosaccharides in the biosynthesis and in vitro and in vivo biological activities of erythropoietin.. Blood 1991; 77: 2624-32.
• 47 Kingsley DM, Kozarsky KF, Hobbie L, Krieger M. Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant.. Cell 1986; 44: 749-59.
• 48 Umemoto J, Bhavanandan VP, Davidson EA. Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae.. J Biol Chem 1977; 252: 8609-14.
• 49 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.
• 50 White GC, Beebe A, Nielsen B. Recombinant factor IX.. Thromb Haemost 1997; 78: 261-5.
• 51 Bond MD, Huberty MC, Jankowski MA, Vath JE, Strang A-M, Scoble HA. Identification of O-glycosylation, sulfation and phosphorylation sites in the activation peptide of human plasma factor IX.. Blood 1994; 84: 531a.
• 52 Bjoern S, Foster DC, Thim L. et al. Human plasma and recombinant factor VII. Characterization of O- glycosylations at serine residues 52 and 60 and effects of site- directed mutagenesis of serine 52 to alanine.. J Biol Chem 1991; 266: 11051-7.
• 53 Hase S, Nishimura H, Kawabata S, Iwanaga S, Ikenaka T. The structure of (xylose)2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX.. J Biol Chem 1990; 265: 1858-61.
• 54 Harris RJ, van Halbeek H, Glushka J. et al. Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)-GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.. Biochemistry 1993; 32: 6539-47.
• 55 Bond MD, Jankowski MA, Huberty MC, Patel H, Scoble HA. Structural Analysis of Recombinant Human Factor IX.. Blood 1994; 84: 194a.
• 56 Brandstetter H, Bauer M, Huber R, Lollar P, Bode W. X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.. Proc Natl Acad Sci U S A 1995; 92: 9796-800.
• 57 Kaufman RJ, Wasley LC, Dorner AJ. Synthesis processing and secretion of factor VIII expressed in mammalian cells.. J Biol Chem 1988; 263: 6352-62.
• 58 Hironaka T, Furukawa K, Esmon PC. et al. Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells.. J Biol Chem 1992; 267: 8012-20.
• 59 Pittman DD, Tomkinson KN, Kaufman RJ. Post-translational requirements for functional factor V and factor VIII secretion in mammalian cells.. J Biol Chem 1994; 269: 17329-37.
• 60 Rosing J, Bakker HM, Thomassen MC, Hemker HC, Tans G. Characterization of two forms of human factor Va with different cofactor activities.. J Biol Chem 1993; 268: 21130-6.
• 61 Bruin T, Sturk A, Ten Cate JW, Cath M. The function of the human factor V carbohydrate moiety in blood coagulation.. Eur J Biochem 1987; 170: 305-10.
• 62 Fernandez JA, Hackeng TM, Kojima K, Griffin JH. The carbohydrate moiety of factor V modulates inactivation by activated protein C.. Blood 1997; 89: 4348-54.
• 63 Nelsestuen GL, Suttie JW. The purification and properties of an abnormal prothrombin protein produced by dicumarol-treated cows. A comparison to normal prothrombin.. J Biol Chem 1972; 247: 8176-82.
• 64 Stenflo J, Ferlund P, Egan W, Roepstorff P. Vitamin K dependent modifications of glutamic acid residues in prothrombin.. Proc Natl Acad Sci USA 1974; 71: 2730-3.
• 65 Jorgensen MJ, Cantor AB, Furie BC, Brown CL, Shoemaker CB, Furie B. Recognition site directing vitamin K-dependent gamma-carboxylation resides on the propeptide of factor IX.. Cell 1987; 48: 185-91.
• 66 Sanford DG, Kanagy C, Sudmeier JL, Furie BC, Furie B, Bachovchin WW. Structure of the propeptide of prothrombin containing the gamma-carboxylation recognition site determined by two-dimensional NMR spectroscopy.. Biochemistry 1991; 30: 9835-41.
• 67 Soriano-Garcia M, Park CH, Tulinsky A, Ravichandran KG, SkrzypczakJankun E. Structure of Ca2+ prothrombin fragment 1 including the conformation of the Gla domain.. Biochemistry 1989; 28: 6805-10.
• 68 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.
• 69 Li L, Darden TA, Freedman SJ. et al. Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.. Biochemistry 1997; 36: 2132-8.
• 70 Bode W, Brandstetter H, Mather T, Stubbs MT. Comparative analysis of haemostatic proteinases: structural aspects of thrombin, factor Xa, factor IXa and protein C.. Thromb Haemost 1997; 78: 501-11.
• 71 Sunnerhagen M, Forsen S, Hoffren AM, Drakenberg T, Teleman O, Stenflo J. Structure of the Ca(2+)-free Gla domain sheds light on membrane binding of blood coagulation proteins [published erratum appears in Nat Struct Biol 1996 Jan;3(1):103].. Nature Structural Biology 1995; 2: 504-9.
• 72 Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX.. J Biol Chem 1996; 271: 16227-36.
• 73 Jacobs M, Freedman SJ, Furie BC, Furie B. Membrane binding properties of the factor IX-carboxyglutamic acid rich domain prepared by chemical synthesis.. J Biol Chem 1994; 269: 25494-501.
• 74 Suttie JW. Synthesis of vitamin K-dependent proteins.. FASEB J 1993; 7: 445-52.
• 75 Rehemtulla A, Roth DA, Wasley LC. et al. In vitro and in vivo functional characterization of bovine vitamin K- dependent gamma-carboxylase expressed in Chinese hamster ovary cells.. Proc Natl Acad Sci USA 1993; 90: 4611-5.
• 76 Wu SM, Cheung WF, Frazier D, Stafford DW. Cloning and expression of the cDNA for human gamma-glutamyl carboxylase.. Science 1991; 254: 1634-6.
• 77 Roth DA, Rehemtulla A, Kaufman RJ, Walsh CT, Furie B, Furie BC. Expression of bovine vitamin K-dependent carboxylase activity in baculovirus-infected insect cells.. Proc Natl Acad Sci USA 1993; 90: 8372-6.
• 78 Yamada M, Kuliopulos A, Nelson NP. et al. Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators.. Biochemistry 1995; 34: 481-9.
• 79 Kuliopulos A, Nelson NP, Yamada M. et al. Localization of the affinity peptide-substrate inactivator site on recombinant vitamin K-dependent carboxylase.. J Biol Chem 1994; 269: 21364-70.
• 80 Roth DA, Whirl ML, Velazquez-Estades LJ, Walsh CT, Furie B, and Furie BC. Mutagenesis of vitamin K-dependent carboxylase demonstrates a carboxyl terminus-mediated interaction with vitamin K hydroquinone.. J Biol Chem 1995; 270: 5305-11.
• 81 Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ. PACE/furin processes the vitamin K-dependent pro-factor IX precursor within the secretory pathway.. J Biol Chem 1993; 268: 8458-65.
• 82 Kaufman RJ, Wasley LC, Furie BC, Furie B, Shoemaker CB. Expression, purification, and characterization of recombinant -carboxylated factor IX synthesized in Chinese hamster ovary cells.. J Biol Chem 1986; 261: 9622-8.
• 83 Berkner KL. Expression of Recombinant Vitamin K-Dependent Proteins in Mammalian Cells: Factors IX and VII.. Methods in Enzymology 1993; 222: 450-77.
• 84 Gillis S, Furie BC, Furie B. et al. gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function.. Protein Sci 1997; 6: 185-196.
• 85 Stenflo J, Lundwall A, Dahlbäck B. beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S.. Proc Natl Acad Sci USA 1987; 84: 368-72.
• 86 McGinnis K, Ku GM, Van Dusen WJ. et al. Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+.. Biochemistry 1996; 35: 3957-62.
• 87 Jia S, Van Dusen WJ, Diehl RE. et al. cDNA cloning and expression of bovine aspartyl (asparaginyl) beta- hydroxylase.. J Biol Chem 1992; 267: 14322-7.
• 88 Thim L, Bjoern S, Christensen M. et al. Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells.. Biochemistry 1988; 27: 7785-93.
• 89 Gronke RS, Van Dusen WJ, Garsky VM. et al. Aspartyl B-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.. Proc Natl Acad Sci 1989; 86: 3609-13.
• 90 Stenflo J, Holme E, Lindstedt S. et al. Hydroxylation of aspartic acid in domains homologous to the epidermal grwoth factor precursor is catalyzed by a 2-oxoglutarate dependent dioxygenase.. Proc Natl Acad Sci 1989; 86: 4440-7.
• 91 Derian CK, VanDusen W, Przysiecki CT. et al. Inhibitors of 2-ketoglutarate-dependent dioxygenase block aspartyl beta-hydroxylation of recombinant human factor IX in several mammalian expression systems.. J Biol Chem 1989; 264: 6615-8.
• 92 Sunnerhagen MS, Persson E, Dahlqvist I. et al. The effect of aspartate hydroxylation on calcium binding to epidermal growth factor-like modules in coagulation factors IX and X.. J Biol Chem 1993; 268: 23339-44.
• 93 Huttner WB. Tyrosine sulfation and the secretory pathway.. Annu Rev Physiol 1988; 50: 363-76.
• 94 Baeuerle PA, Huttner WB. Tyrosine sulfation is a trans-Golgi-specific protein modification.. J Cell Biol 1987; 105: 2655-64.
• 95 Niehrs C, Huttner WB. Purification and characterization of tyrosylprotein sulfotransferase.. EMBO J 1990; 9: 35-42.
• 96 Braun PJ, Dennis S, Hofsteenge J, Stone SR. Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin.. Biochemistry 1988; 27: 6517-22.
• 97 Farrell DH, Mulvihill ER, Huang SM, Chung DW, Davie EW. Recombinant human fibrinogen and sulfation of the gamma’ chain.. Biochemistry 1991; 30: 9414-20.
• 98 Hortin G, Tollefsen DM, Strauss AW. Identification of two sites of sulfation of human heparin cofactor II.. J Biol Chem 1986; 261: 15827-30.
• 99 Hortin G, Fok KF, Toren PC, Strauss AW. Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin.. J Biol Chem 1987; 262: 3082-5.
• 100 Jenne D, Hille A, Stanley KK, Huttner WB. Sulfation of two tyrosine-residues in human complement S-protein (vitronectin).. Eur J Biochem 1989; 185: 391-5.
• 101 Morita T, Jackson CM. Localization of the structural difference between bovine blood coagulation factors X1 and X2 to tyrosine 18 in the activation peptide.. J Biol Chem 1986; 261: 4008-14.
• 102 Pittman DD, Wang JH, Kaufman RJ. Identification and functional importance of tyrosine-sulfate residues within recombinant factor VIII.. Biochemistry 1992; 31: 3315-23.
• 103 Pittman DD, Tomkinson KN, Michnick D, Selighsohn U, Kaufman RJ. Post-translational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity.. Biochemistry 1994; 33: 6952-9.
• 104 Michnick DA, Pittman DD, Wise RJ, Kaufman RJ. Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage.. J Biol Chem 1994; 269: 20095-102.
• 105 Mutt V. In: Gastrointestinal Hormones. Glass GBJ. (Ed) New York: Raven Press; 1980: 169.
• 106 Niehrs C, Huttner WB, Carvallo D, Degryse E. Conversion of recombinant hirudin to the natural form by in vitro tyrosine sulfation. Differential substrate specificities of leech and bovine tyrosylprotein sulfotransferases.. J Biol Chem 1990; 265: 9314-8.
• 107 Rydel TJ, Ravichandran KG, Tulinsky A. et al. The structure of a complex of recombinant hirudin and human alpha-thrombin.. Science 1990; 249: 277-80.
• 108 Friederich E, Gritz HJ, Huttner WB. Inhibition of tyrosine sulfaction in the trans-Golgi retards the transport of a constitutively secreted protein to the cell surface.. J Cell Biol 1988; 107: 1655-67.
• 109 Leyte A, van Schijndel HB, Niehrs C. et al. Sulfation of Tyr 1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor.. J Biol Chem 1991; 266: 740-6.
• 110 Higuchi M, Wong C, Kochhan L. et al. Characterization of mutations in factor VIII gene by direct sequencing of amplified genomic DNA.. Genomics 1990; 6: 65-71.
• 111 Barrow RT, Healey JF, Lollar P. Inhibition by heparin of thrombin-catalyzed activation of the factor VIII-von Willebrand factor complex.. J Biol Chem 1994; 269: 593-8.
• 112 Esmon CT, Lollar P. Involvement of Thrombin Anion-binding Exosites 1 and 2 in the Activation of Factor V and Factor VIII.. J Biol Chem 1996; 271: 13882-7.
• 113 Rand MD, Kalafatis M, Mann KG. Platelet coagulation factor Va: The major secretory platelet phosphoprotein.. Blood 1994; 83: 2180-90.
• 114 Kalafatis M, Rand MD, Jenny RJ, Ehrlich YH, Mann KG. Phosphorylation of factor Va and factor VIIIa by activated platelets.. Blood 1993; 81: 704-19.
• 115 Diuguid DL, Rabiet MJ, Furie BC, Liebman HA, Furie B. Molecular basis of hemophilia B: a defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor.. Proc Natl Acad Sci USA 1986; 83: 5803-7.
• 116 Bentley AK, Rees DJ, Rizza C, Brownlee GG. Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4.. Cell 1986; 45: 343-8.
• 117 Sugimoto M, Miyata T, Kawabata S, Yoshioka A, Fukui H, Iwanaga S. Factor IX Kawachinagano: impaired function of the Gla-domain caused by attached propeptide region due to substitution of arginine by glutamine at position -4.. Br J Haematol 1989; 72: 216-21.
• 118 Foster DC, Holly RD, Sprecher CA, Walker KM, Kumar AA. Endoproteolytic processing of the human protein C precursor by the yeast Kex2 endopeptidase coexpressed in mammalian cells.. Biochemistry 1991; 30: 367-72.
• 119 Bathurst IC, Brennan SO, Carrell RW, Cousens LS, Brake AJ, Barr PJ. Yeast KEX2 protease has the properties of a human proalbumin converting enzyme.. Science 1987; 235: 348-50.
• 120 Julius D, Brake A, Blair L, Kunisawa R, Thorner J. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor.. Cell 1984; 37: 1075-89.
• 121 Wise RJ, Barr PJ, Wong PA, Kiefer MC, Brake AJ, Kaufman RJ. Expression of human proprotein processing enzyme: Correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site.. Proc Natl Acad Sci USA 1990; 87: 9378-82.
• 122 van de Ven WJ, Voorberg J, Fontijn R. et al. Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes.. Mol Biol Rep 1990; 14: 265-75.
• 123 Bresnahan PA, Leduc R, Thomas L. et al. Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo.. J Cell Biol 1990; 111: 2851-9.
• 124 Brennan SO, Peach RJ. The processing of human proinsulin and chicken proalbumin by rat hepatic vesicles suggests a convertase specific for X-Y-Arg-Arg or Arg-X-Y-Arg sequences.. J Biol Chem 1991; 266: 21504-8.
• 125 Misumi Y, Ohkubo K, Sohda M, Takami N, Oda K, Ikehara Y. Intracellular processing of complement pro-C3 and proalbumin is inhibited by rat alpha 1-protease inhibitor variant (Met352----Arg) in transfected cells.. Biochem Biophys Res Commun 1990; 171: 236-42.
• 126 Halban PA, Irminger JC. Sorting and processing of secretory proteins.. Biochem J 1994; 299: 1-18.
• 127 Benjannet S, Rondeau N, Day R, Chretien M, Seidah NG. PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues.. Proc Natl Acad Sci USA 1991; 88: 3564-8.
• 128 Thomas L, Leduc R, Thorne BA, Smeekens SP, Steiner DF, Thomas G. Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: evidence for a common core of neuroendocrine processing enzymes.. Proc Natl Acad Sci USA 1991; 88: 5297-301.
• 129 Roebroek AJ, Schalken JA, Leunissen JA, Onnekink C, Bloemers HP, van de Ven WJ. Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein.. EMBO J 1986; 5: 2197-202.
• 130 Kiefer MC, Tucker JE, Joh R, Landsberg KE, Saltman D, Barr PJ. Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15.. DNA Cell Biol 1991; 10: 757-69.
• 131 Rehemtulla A, Dorner AJ, Kaufman RJ. Regulation of PACE pro-peptide-processing activity: Requirement for a post endoplasmic reticulum compartment and autoproteolytic activation.. Proc Natl Acad Sci USA 1992; 89: 8235-9.
• 132 Leduc R, Molloy SS, Thorne BA, Thomas G. Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage.. J Biol Chem 1992; 267: 14304-8.
• 133 Anderson ED, VanSlyke JK, Thulin CD, Jean F, Thomas G. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage.. EMBO J 1997; 16: 1508-18.
• 134 Molloy SS, Thomas L, Van Slyke JK, Stenberg PE, Thomas G. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface.. EMBO J 1994; 13: 18-33.
• 135 Rehemtulla A, Kaufman RJ. Preferred sequence requirements for cleavage of pro-vWF by propeptide processing enzymes.. Blood 1992; 9: 2349-55.
• 136 Rehemtulla A, Barr PJ, Rhodes C, Kaufman RJ. PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE.. Biochemistry 1993; 32: 11586-90.
• 137 Drews R, Paleyanda RK, Lee TK. et al. Alteration of the posttranslational capacity of the mammary gland.. Proc Natl Acad Sci USA 1995; 92: 10462-6.
• 138 Ganz PR, Tackaberry ES, Palmer DS, Rock G. Human factor VIII from heparinized plasma. Purification and characterization of a single-chain form.. Eur J Biochem 1988; 170: 521-8.
• 139 Furie B, Furie BC. The molecular basis of blood coagulation.. Cell 1988; 53: 505-18.
• 140 Swaroop M, Moussalli M, Pipe SW, Kaufman RJ. Mutagenesis of a potential BiP binding site enhances secretion of coagulation factor VIII.. J Biol Chem 1997; 272: 24121-4.