Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein.

Article Details

Citation

Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R

Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein.

Ann Hematol. 2008 Feb;87(2):107-12. Epub 2007 Sep 26.

PubMed ID
17899080 [ View in PubMed
]
Abstract

Recently, it was shown that glycoproteins with N-glycans close to the NH(2) terminus can directly enter the calnexin/calreticulin cycle and bypass BiP binding. This should allow efficient secretion of glycoproteins such as factor VIII (FVIII) whose secretion is negatively affected by BiP interaction. Examination of the glycosylation pattern of the NH(2) terminus of FV and FVIII revealed N-glycans at positions 23 and 27 in FV and at position 41 in FVIII. To improve FVIII secretion, a 14-amino-acid-long polypeptide with (G3) or without (G0; control) three N-linked glycosylation consensus sites was inserted upstream of the NH(2) terminus of a B-domain deleted FVIII protein. Expression of G3- and G0-constructs in three different cell lines resulted in the same or even higher expression rate of protein as found for the B-domain deleted FVIII. However, as demonstrated by Western blot analysis, the G3- as well as the G0-protein variants were mainly retained inside the cells in similar amounts. Thus, glycosylation alone does not automatically lead to higher secretion rates, but must be in context to the normal structure of the FVIII protein.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Antihemophilic factor, human recombinantCalnexinProteinHumans
Unknown
Chaperone
Details
Antihemophilic factor, human recombinantCalreticulinProteinHumans
Unknown
Chaperone
Details
Lonoctocog alfaCalnexinProteinHumans
Unknown
Chaperone
Details
Lonoctocog alfaCalreticulinProteinHumans
Unknown
Chaperone
Details
Moroctocog alfaCalnexinProteinHumans
Unknown
Chaperone
Details
Moroctocog alfaCalreticulinProteinHumans
Unknown
Chaperone
Details