The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Generation and degradation of human endostatin proteins by various proteinases
Abstract
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.
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New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
TUMOR STROMA AND REGULATION OF CANCER DEVELOPMENT
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Matrix metalloproteinases and angiogenesis
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Matrix Metalloproteinases As Novel Biomarker s and Potential Therapeutic Targets in Human Cancer
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Cathepsin D--many functions of one aspartic protease
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Metadata
- Authors
- Ferreras, M., Felbor, U., Lenhard, T., Olsen, B. R., & Delaissé, J.-M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2000-12-12
- Volume
- 486
- Issue
- 3
- Pages
- 247-251
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2058873146
- Cited by
- 377
- References
- 30
- FWCI
- 3.94
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ferreras, M., Felbor, U., Lenhard, T., Olsen, B. R., & Delaissé, J.-M. (2000). Generation and degradation of human endostatin proteins by various proteinases. FEBS Letters. https://doi.org/10.1016/s0014-5793(00)02249-3
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