TAILIEUCHUNG - Báo cáo khoa học: Mouse recombinant protein C variants with enhanced membrane affinity and hyper-anticoagulant activity in mouse plasma

Mouse anticoagulant protein C (461 residues) shares 69% sequence identity with its human ortholog. Interspecies experiments suggest that there is an incompatibility between mouse and human protein C, such that human protein C does not function efficiently in mouse plasma, nor does mouse protein C function efficiently in human plasma. | ễFEBS Journal Mouse recombinant protein C variants with enhanced membrane affinity and hyper-anticoagulant activity in mouse plasma 1 2 2 -2 Michael J. Krisinger Li Jun Guo Gian Luca Salvagno Gian Cesare Guidi Giuseppe Lippi and Bjorn Dahlback1 1 Department of Laboratory Medicine Division of ClinicalChemistry Lund University University Hospital Malmo Sweden 2 ClinicalChemistry Section Department of Morphological-BiomedicalSciences University Hospitalof Verona Italy Keywords anticoagulation Gla domain mouse protein C mouse plasma protein-membrane interactions Correspondence B. Dahlback Department of Laboratory Medicine Division of ClinicalChemistry Wallenberg Laboratory Entrance 46 Floor 6 Lund University University Hospital S-20502 Malmo Sweden Fax 46 40 337044 Tel 46 40 331501 E-mail Received 1 July 2009 revised 4 September 2009 accepted 9 September 2009 doi Mouse anticoagulant protein C 461 residues shares 69 sequence identity with its human ortholog. Interspecies experiments suggest that there is an incompatibility between mouse and human protein C such that human protein C does not function efficiently in mouse plasma nor does mouse protein C function efficiently in human plasma. Previously we described a series of human activated protein C APC Gla domain mutants . QGNSEDY-APC with enhanced membrane affinity that also served as superior anticoagulants. To characterize these Gla mutants further in mouse models of diseases the analogous mutations were now made in mouse protein C. In total seven mutants mutated at one or more of positions P10S12D23Q32N33 and wild-type protein C were expressed and purified to homogeneity. In a surface plasmon resonance-based membranebinding assay several high affinity protein C mutants were identified. In Ca2 titration experiments the high affinity variants had a significantly reduced four-fold Ca2 requirement for half-maximum binding. In a tissue factor-initiated .

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