Effects of fibronectin cleaved by neuropsin on cell adhesion and migration

Naoyuki Tani, Kazumasa Matsumoto, Ichiro Ota, Shigetaka Yoshida, Yoshikazu Takada, Sadao Shiosaka, Nariaki Matsuura

Research output: Contribution to journalReview articlepeer-review

12 Citations (Scopus)


Neuropsin is a serine protease cloned from the mouse hippocampus. Since neuropsin is a secreted protein which effectively cleaves fibronectin, it may affect cell adhesion or cell migration by modulating the content and/or chemical characteriscs of fibronectin in extracellular matrix (ECM). In adhesion assays, α5B2 cells expressing integrin α5β1 bound less effectively to fibronectin teated with neuropsin than intact fibronectin. In Boyden chamber chemotaxis assays, the fibronectin-induced migration of α5B2 cells was not affected by neuropsin treatment. These findings suggest that neuropsin regulates the local microenvironment by modulating the interaction between cells and fibronectin in ECM.

Original languageEnglish
Pages (from-to)247-251
Number of pages5
JournalNeuroscience Research
Issue number2
Publication statusPublished - 2001
Externally publishedYes


  • Cell adhesion
  • Cell migration
  • Fibronectin
  • Neural plasticity
  • Neuropsin
  • Serine protease

ASJC Scopus subject areas

  • General Neuroscience


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