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Plasmin releases the anti-tumor peptide from the NC1 domain of collagen XIX.

Abstract
During tumor invasion, tumor cells degrade the extracellular matrix. Basement membrane degradation is responsible for the production of peptides with anti-tumor properties. Type XIX collagen is associated with basement membranes in vascular, neuronal, mesenchymal and epithelial tissues. Previously, we demonstrated that the non-collagenous NC1, C-terminal, domain of collagen XIX [NC1(XIX)] inhibits the migration capacities of tumor cells and exerts a strong inhibition of tumor growth. Here, we demonstrate that plasmin, one of the most important enzyme involved in tumor invasion, was able to release a fragment of NC1(XIX), which retained the anti-tumor activity. Molecular modeling studies showed that NC1(XIX) and the anti-tumor fragment released by plasmin (F4) adopted locally the same type I β-turn conformation. This suggests that the anti-tumor effect is conformation-dependent. This study demonstrates that collagen XIX is a novel proteolytic substrate for plasmin. Such release may constitute a defense of the organism against tumor invasion.
AuthorsJean-Baptiste Oudart, Sylvie Brassart-Pasco, Alexia Vautrin, Christèle Sellier, Carine Machado, Aurelie Dupont-Deshorgue, Bertrand Brassart, S Baud, Manuel Dauchez, Jean-Claude Monboisse, Dominique Harakat, François-Xavier Maquart, Laurent Ramont
JournalOncotarget (Oncotarget) Vol. 6 Issue 6 Pg. 3656-68 (Feb 28 2015) ISSN: 1949-2553 [Electronic] United States
PMID25668817 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Peptides
  • Collagen
  • Fibrinolysin
Topics
  • Amino Acid Sequence
  • Animals
  • Cell Culture Techniques
  • Cell Line, Tumor
  • Chromatography, High Pressure Liquid (methods)
  • Collagen (chemistry, metabolism)
  • Fibrinolysin (metabolism)
  • Humans
  • Melanoma (chemistry, metabolism, pathology)
  • Mice, Inbred C57BL
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Neoplasm Invasiveness
  • Neoplasms (chemistry, metabolism, pathology)
  • Peptides (chemistry, metabolism)
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteolysis
  • Transfection

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