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- Title
Secreted cathepsin L generates endostatin from collagen XVIII.
- Authors
Felbor, U; Dreier, L; Bryant, R A; Ploegh, H L; Olsen, B R; Mothes, W
- Abstract
Endostatin, an inhibitor of angiogenesis and tumor growth, was identified originally in conditioned media of murine hemangioendothelioma (EOMA) cells. N-terminal amino acid sequencing demonstrated that it corresponds to a fragment of basement membrane collagen XVIII. Here we report that cathepsin L is secreted by EOMA cells and is responsible for the generation of endostatin with the predicted N-terminus, while metalloproteases produce larger fragments in a parallel processing pathway. Efficient endostatin generation requires a moderately acidic pH similar to the pericellular milieu of tumors. The secretion of cathepsin L by a tumor cell line of endothelial origin suggests that this cathepsin may play a role in angiogenesis. We propose that cleavage within collagen XVIII's protease-sensitive region evolved to regulate excessive proteolysis in conditions of induced angiogenesis.
- Publication
The EMBO journal, 2000, Vol 19, Issue 6, p1187
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/19.6.1187