Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor
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 b...
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Veröffentlicht in: | The Journal of biological chemistry 1994-10, Vol.269 (42), p.26486-26491 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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 message are both down-regulated by exposure of endothelium to tumor necrosis factor.
Identification of endothelial cell protein C receptor as a member of the CD1/major histocompatibility complex superfamily
provides insights into the role of protein C in regulating the inflammatory response. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/s0021-9258(18)47220-1 |