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Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation.
Author(s) -
Suzuki K.,
Kusumoto H.,
Deyashiki Y.,
Nishioka J.,
Maruyama I.,
Zushi M.,
Kawahara S.,
Honda G.,
Yamamoto S.,
Horiguchi S.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02448.x
Subject(s) - thrombomodulin , biology , thrombin , complementary dna , microbiology and biotechnology , transfection , peptide sequence , signal peptide , transmembrane domain , glycosylation , protein c , transmembrane protein , egf like domain , thrombin receptor , biochemistry , receptor , gene , immunology , platelet
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.