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Volume 270,
Number 10,
Issue of March 10, 1995 pp. 5571-5577
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Molecular
Cloning and Expression of Murine and Bovine Endothelial Cell Protein
C/Activated Protein C Receptor (EPCR)
THE STRUCTURAL AND FUNCTIONAL CONSERVATION IN HUMAN, BOVINE, AND
MURINE EPCR
(Received for publication, December
1, 1994; and in revised form, January 9, 1995)
Kenji
Fukudome,
Charles
T.
Esmon
Recently, we identified and cloned a human endothelial cell
protein C/activated protein C receptor (EPCR). EPCR was predicted to be
a type 1 transmembrane glycoprotein and a novel member of the CD1/major
histocompatibility complex superfamily with 28% identity with CD1d.
Even greater homology (62% identity) was detected with the murine
protein, CCD41, which was previously characterized as a
centrosome-associated, cell cycle-dependent protein. This raised the
possibility that CCD41 was the murine homologue of EPCR. To address
this possibility, to better understand structure-function
relationships, and to facilitate physiological experiments on EPCR
function, we cloned and sequenced murine and bovine EPCR from
endothelial cell cDNA libraries. The nucleotide sequence of murine EPCR
and CCD41 exhibited five differences corresponding to one base change,
three single-base insertions, and one base deletion in the protein
coding region. As a result, the predicted structures of EPCR and CCD41
differed in their amino and carboxyl termini but were identical in the
central portion of the coding sequence. Based on comparison of the
murine, bovine, and human EPCR sequences and the regions where
discrepancies between murine EPCR and CCD41 were detected, we believe
that CCD41 is probably identical to murine EPCR and that the reported
sequence differences are likely the result of compression on the
sequencing gel. Compared with human EPCR, the murine and bovine
sequences were 69 and 73% identical, respectively, and 57% of the
residues were identical between all three species. Both bovine and
murine EPCR could bind human activated protein C when the cDNA clones
were transfected into 293T cells. Like human EPCR, of the cell lines
tested, the murine EPCR message was restricted to endothelium. Cloning
of the murine and bovine homologue of EPCR will facilitate in vivo and in vitro studies of the role of EPCR in the protein C
pathway.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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