Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation.
We have deduced the entire 575-amino acid sequence of the human thrombomodulin precursor from cDNA clones. The precursor starts with an 18-residue signal peptide domain, followed by the NH2-terminal domain, a domain with six epidermal growth factor-like structures, an O-glycosylation site-rich domain, a 24-residue transmembrane domain and a cytoplasmic domain. Simian COS cells transfected with the expression vector pSV2 containing thrombomodulin cDNA synthesized immunoreactive and functionally active thrombomodulin.
Suzuki
K
K
Department of Laboratory Medicine, Mie University School of Medicine, Japan.
Kusumoto
H
H
Deyashiki
Y
Y
Nishioka
J
J
Maruyama
I
I
Zushi
M
M
Kawahara
S
S
Honda
G
G
Yamamoto
S
S
Horiguchi
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010957:Plasmids; D014176:Protein Biosynthesis; D011486:Protein C / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000235:genetics* / Q000378:metabolism; D018179:Receptors, Thrombin; D012689:Sequence Homology, Nucleic Acid; D013917:Thrombin / Q000378:metabolism*; D014158:Transcription, Genetic
D011486:Protein C; D011956:Receptors, Cell Surface; D018179:Receptors, Thrombin; D004247:DNA; D013917:Thrombin