Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6000795 | Thrombosis Research | 2015 | 9 Pages |
Abstract
The 163Val and 163Glu mutants had undetectable levels in the culture media, showed intracellular co-localization with the 26S proteasome and were polyubiquitinated. The 77Gly mutant was secreted to the media showing similar activity as the wild type. There was no difference among intracellular PC levels of wild type and mutant proteins. The 163Val and 163Glu mutations caused significant changes in the relative positions of the EGF2 domains suggesting misfolding with the consequence of secretion defect. No major structural alteration was observed in case of 77Gly mutant; it might influence the stability of protein complexes in which PC participates and may have an impact on the clearance of PC requiring further research.
Keywords
FCSFVIIIaactivated factor VPROCFIXaFVIIPPAdNTPVTEAPCGLAFVAPPIHEKACAAPTTDABPVDFPBSEGFDMEMCLSM3,3′-diaminobenzidineDMSODNALp(a)Anticardiolipin antibodyantithrombingamma-carboxyglutamic acidSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisMRIVenous thromboembolismDVTDeep venous thrombosisMagnetic resonance imagingMissense mutationpolyvinylidene difluorideParticle mesh Ewaldactivated partial thromboplastin timethrombin timefetal calf serumSerine proteasehuman embryonic kidney cellsendoplasmic reticulumPMEepidermal growth factorFactor VIIPhosphate buffered salinelupus anticoagulantLipoprotein aDulbecco’s modified eagle’s mediumMolecular modelingExpression studyconfocal laser scanning microscopypolymerase chain reactionPCRProtein CProtein SActivated protein CProtein C deficiency
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Authors
Kitti B. Kovács, István Pataki, Helga Bárdos, Attila Fekete, György Pfliegler, Gizella Haramura, Réka Gindele, István Komáromi, György Balla, Róza Ádány, László Muszbek, Zsuzsanna Bereczky,