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Generation of Gla‐domainless FVIIa by cathepsin G‐mediated cleavage
Author(s) -
Nicolaisen Else Marie,
Petersen Lars Christian,
Thim Lars,
Jacobsen Jes Kristian,
Christensen Mogens,
Hedner Ulla
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80989-t
Subject(s) - cleavage (geology) , cathepsin , chemistry , biochemistry , cathepsin o , cathepsin d , cathepsin h , cathepsin a , microbiology and biotechnology , biology , enzyme , paleontology , fracture (geology)
Cougulation factor VII contains ten λ‐carboxyglutamic acid residues in the N‐terminal region (Gla‐domain) which are essential for the hemostatic function of FVII. The present study shows that granulocyte cathepsin G degrades the Gla‐domain of FVIIa in vitro. Characterization of the truncated FVIIa by SDS‐PAGE and N‐terminal amino acid sequence analysis revealed that cleavage had occurred between Tyr‐44 and Ser‐45 and that further cleavage was only obtained on extensive cathepsin G exposure. Cleavage of vitamin K‐dependent coagulation factors by cathepsin G may play a role in vivo, and it offers a convenient way of obtaining proteins deprived of their Gla‐domain for functional and structural studies.