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Generation and degradation of human endostatin proteins by various proteinases
Author(s) -
Ferreras Mercedes,
Felbor Ute,
Lenhard Thomas,
Olsen Bjorn R.,
Delaissé Jean-Marie
Publication year - 2000
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/s0014-5793(00)02249-3
Subject(s) - endostatin , angiogenesis , proteolysis , cathepsin l , chemistry , cathepsin , microbiology and biotechnology , angiogenesis inhibitor , cathepsin d , biochemistry , biology , enzyme , cancer research
The angiogenesis inhibitor endostatin is a fragment of the NC1 domain of collagen XVIII. The generation of endostatin has been investigated only in murine hemangioendothelioma cell cultures and was ascribed to cathepsin L. Distinct endostatin‐like fragments were detected in human tissues and serum. To identify proteinases able to generate such fragments, we incubated human NC1 with proteinases of all classes, including cathepsin L. Eleven out of 12 generate fragments with an N‐terminus within the same 15 residue stretch as those occurring physiologically, indicating that this region is sensitive to many proteinases. None correspond to mouse endostatin. However, the efficiencies of these proteinases differed markedly. Some proteinases also proved to degrade endostatin, pointing to another regulatory loop of angiogenesis.