Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion

Juan Carlos Rodríguez-Manzaneque*, Darren Carpizo, María del Carmen Plaza-Calonge, Antoni Xavier Torres-Collado, Shelley N.M. Thai, Michael Simons, Arie Horowitz, M. Luisa Iruela-Arispe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations


Syndecan-4 is a membrane-bound heparan sulfate proteoglycan that participates in cell-cell and cell-matrix interactions and modulates adhesion and migration of many cell types. Through its extracellular domain, syndecan-4 cooperates with adhesion molecules and binds matrix components relevant for cell migration. Importantly, syndecan-4 is a substrate of extracellular proteases, however the biological significance of this cleavage has not been elucidated. Here, we show that the secreted metalloprotease ADAMTS1, involved in angiogenesis and inflammatory processes, cleaves the ectodomain of syndecan-4. We further showed that this cleavage results in altered distribution of cytoskeleton components, functional loss of adhesion, and gain of migratory capacities. Using syndecan-4 null cells, we observed that ADAMTS1 proteolytic action mimics the outcome of genetic deletion of this proteoglycan with regards to focal adhesion. Our findings suggest that the shedding of syndecan-4 by ADAMTS1 disrupts cell adhesion and promotes cell migration.

Original languageEnglish (US)
Pages (from-to)800-810
Number of pages11
JournalInternational Journal of Biochemistry and Cell Biology
Issue number4
StatePublished - Apr 2009


  • Endothelial cell
  • Extracellular proteolysis
  • Metalloprotease
  • Proteoglycan

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


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