Differential investigations from plasma-derived and recombinant Factor IX revealed major differences in post-translational modifications of activation peptides

Vox Sanguinis

Volumn 104, Issue 2, 2013, Pages 171-174

  Chevreux, G ^a   Faid, V ^a   Andre, M H ^b   Tellier, Z ^b   Bihoreau, N ^a  

^a LFB Biotechnologies   (France)

^b Immunology Therapeutic Unit   (France)

Author keywords

Coagulation factor concentrate; Hemostasis; Plasma derivatives; Proteomics; Recombinant proteins

Indexed keywords

RECOMBINANT BLOOD CLOTTING FACTOR 9;

ARTICLE; GLYCOSYLATION; IN VIVO STUDY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PLASMA; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING;

ANIMALS; CHO CELLS; CRICETINAE; FACTOR IX; HUMANS; PEPTIDE FRAGMENTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 84872599371     PISSN: 00429007     EISSN: 14230410     Source Type: Journal    
DOI: 10.1111/j.1423-0410.2012.01649.x     Document Type: Article

References (14)

1. Hansson K, Stenflo J: Post-translational modifications in proteins involved in blood coagulation. J Thromb Haemost 2005; 3:2633-2648
2. Kurachi K, Davie EW: Isolation and characterization of a cDNA coding for human factor IX. Proc Natl Acad Sci USA 1982; 79:6461-6464
3. Bond M, Jankowski M, Patel H, et al. : Biochemical characterization of recombinant factor IX. Semin Hematol 1998; 35:11-17
4. Ashwell G, Harford J: Carbohydrate-specific receptors of the liver. Annu Rev Biochem 1982; 51:531-554
5. Pittman DD, Wang JH, Kaufman RJ: Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII. Biochemistry 1992; 31:3315-3325
6. Johansson L, Karpf DM, Hansen L, et al. : Activation peptides prolong the murine plasma half-life of human factor VII. Blood 2011; 117:3445-3452
7. White GC 2nd, Beebe A, Nielsen B: Recombinant factor IX. Thromb Haemost 1997; 78:261-265
8. Ewenstein BM, Joist JH, Shapiro AD, et al. : Pharmacokinetic analysis of plasma-derived and recombinant F IX concentrates in previously treated patients with moderate or severe hemophilia B. Transfusion 2002; 42:190-197
9. McGraw RA, Davis LM, Noyes CM, et al. : Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX. Proc Natl Acad Sci USA 1985; 82:2847-2851
10. Ciucanu I, Kerek F: A simple and rapid method for the permethylation of carbohydrates. Carbohydr Res 1984; 131:209-217
11. Grabenhorst E, Schlenke P, Pohl S, et al. : Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells. Glycoconj J 1999; 16:81-97
12. Fischer BE, Dorner F: Recombinant coagulation factor IX: glycosylation analysis and in vitro conversion into human-like sialylation pattern. Thromb Res 1998; 89:147-150
13. Stanley P, Raju TS, Bhaumik M: CHO cells provide access to novel N-glycans and developmentally regulated glycosyltransferases. Glycobiology 1996; 6:695-699
14. Rodgers SD, Camphausen RT, Hammer DA: Sialyl Lewis(x)-mediated, PSGL-1-independent rolling adhesion on P-selectin. Biophys J 2000; 79:694-706