2011
DOI: 10.1182/blood-2010-06-290098
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Abstract: Coagulation factors VII (FVII),

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Cited by 15 publications
(21 citation statements)
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“…Indeed we observed normal levels for the rFX‐482X and rFX‐480X variants and poor secretion for the swapped rFX FVII chimera. In contrast, swapping of other domains, producing chimeric FX‐FVII or FX‐FIX variants, did not affect protein levels in media.…”
Section: Resultsmentioning
confidence: 79%
“…Indeed we observed normal levels for the rFX‐482X and rFX‐480X variants and poor secretion for the swapped rFX FVII chimera. In contrast, swapping of other domains, producing chimeric FX‐FVII or FX‐FIX variants, did not affect protein levels in media.…”
Section: Resultsmentioning
confidence: 79%
“…It should be noted that our previous study revealed that the carboxy-terminal region of 19 residues of the FX AP, which includes both N-glycosylation sites, is sufficient to preserve a normal survival of the protein [13]. Moreover, Johansson et al demonstrated that insertion of FX AP into the sequence of other vitamin K-dependent proteases substantially extends their half-lifes [14]. Taken together, these observations not only emphasize the importance of the N-glycosylated part of the FX AP in the survival of the protein, but also show that FX AP can be used as a tool to increase the mean circulating time of plasma proteins and therefore improve their therapeutic potential.…”
Section: Discussionmentioning
confidence: 79%
“…First, we have shown that the carboxy-terminal end of the activation peptide plays a crucial role in FX catabolism, both in recovery and half-life of the protein [13]. Moreover, it was also shown that insertion of the FX activation peptide in FVII increased the terminal half-life of the latter 4-fold [14]. Interestingly, both studies demonstrated that the two sole N-linked glycans of FX at positions 181 and 191 of its activation peptide represent important structural determinants for the recovery and half-life of the injected protein.…”
Section: Introductionmentioning
confidence: 97%
“…The blood coagulation cascade involves several trypsin-like proteases, which leads to the activation of prothrombin by factor Xa, resulting eventually in thrombin cleavage of fibrinogen and formation of fibrin clots, which stop bleeding [70]. N -glycosylated variants of factor VII propeptides prolong its half-life significantly, while corresponding variants of factor IX can also play a role in the treatment of hemophilia [71,72]. Regulation of the fibrinolytic plasmin depends on differential N - and O -glycosylation, which alters the structure significantly [73,74].…”
Section: Glycosylated Proteasesmentioning
confidence: 99%