Proteolytic processing regulates placental growth factor activities

Daniel C. Hoffmann, Sebastian Willenborg, Manuel Koch, Daniela Zwolanek, Stefan Müller, Ann Kathrin A. Becker, Stephanie Metzger, Martin Ehrbar, Peter Kurschat, Martin Hellmich, Jeffrey A. Hubbell, Sabine A. Eming

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Background: The mechanisms of placental growth factor (PlGF)-mediated blood vessel formation are incompletely understood. Results: Plasmin cleaves the heparin-binding domain of PlGF-2. Conclusion: Plasmin regulates PlGF-2/Neuropilin-1-mediated tissue vascularization and growth. Significance: Plasmin-mediated carboxyl-terminal processing of VEGF family members may be considered as a principal mechanism to regulate their biological activity.

Original languageEnglish (US)
Pages (from-to)17976-17989
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number25
DOIs
StatePublished - Jun 21 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Hoffmann, D. C., Willenborg, S., Koch, M., Zwolanek, D., Müller, S., Becker, A. K. A., Metzger, S., Ehrbar, M., Kurschat, P., Hellmich, M., Hubbell, J. A., & Eming, S. A. (2013). Proteolytic processing regulates placental growth factor activities. Journal of Biological Chemistry, 288(25), 17976-17989. https://doi.org/10.1074/jbc.M113.451831