Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor
K Fukudome, CT Esmon - Journal of Biological Chemistry, 1994 - ASBMB
Human protein C and activated protein C are shown to bind to endothelium specifically,
selectively and saturably (Kd= 30 nM, 7000 sites per cell) in a Ca (2+)-dependent fashion.
Expression cloning revealed a 1.3-kilobase pair cDNA that coded for a novel type 1
transmembrane glycoprotein capable of binding protein C. This protein appears to be a
member of the CD1/major histocompatibility complex superfamily. Like thrombomodulin, the
receptor involved in protein C activation, the endothelial cell protein C receptor function and …
selectively and saturably (Kd= 30 nM, 7000 sites per cell) in a Ca (2+)-dependent fashion.
Expression cloning revealed a 1.3-kilobase pair cDNA that coded for a novel type 1
transmembrane glycoprotein capable of binding protein C. This protein appears to be a
member of the CD1/major histocompatibility complex superfamily. Like thrombomodulin, the
receptor involved in protein C activation, the endothelial cell protein C receptor function and …