Abstract:
:Coagulation factor VII contains ten gamma-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nicolaisen EM,Petersen LC,Thim L,Jacobsen JK,Christensen M,Hedner Udoi
10.1016/0014-5793(92)80989-tkeywords:
subject
Has Abstractpub_date
1992-07-20 00:00:00pages
157-60issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(92)80989-Tjournal_volume
306pub_type
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