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

doi:10.1016/S0168-0102(00)00213-3

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 journal › Review article › peer-review

12 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	247-251
Number of pages	5
Journal	Neuroscience Research
Volume	39
Issue number	2
DOIs	https://doi.org/10.1016/S0168-0102(00)00213-3
Publication status	Published - 2001
Externally published	Yes

Keywords

Cell adhesion
Cell migration
Fibronectin
Neural plasticity
Neuropsin
Serine protease

ASJC Scopus subject areas

General Neuroscience

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10.1016/S0168-0102(00)00213-3

Cite this

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title = "Effects of fibronectin cleaved by neuropsin on cell adhesion and migration",

abstract = "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.",

keywords = "Cell adhesion, Cell migration, Fibronectin, Neural plasticity, Neuropsin, Serine protease",

author = "Naoyuki Tani and Kazumasa Matsumoto and Ichiro Ota and Shigetaka Yoshida and Yoshikazu Takada and Sadao Shiosaka and Nariaki Matsuura",

year = "2001",

doi = "10.1016/S0168-0102(00)00213-3",

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volume = "39",

pages = "247--251",

journal = "Neuroscience Research",

issn = "0168-0102",

publisher = "Elsevier Ireland Ltd",

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TY - JOUR

T1 - Effects of fibronectin cleaved by neuropsin on cell adhesion and migration

AU - Tani, Naoyuki

AU - Matsumoto, Kazumasa

AU - Ota, Ichiro

AU - Yoshida, Shigetaka

AU - Takada, Yoshikazu

AU - Shiosaka, Sadao

AU - Matsuura, Nariaki

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

KW - Cell adhesion

KW - Cell migration

KW - Fibronectin

KW - Neural plasticity

KW - Neuropsin

KW - Serine protease

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U2 - 10.1016/S0168-0102(00)00213-3

DO - 10.1016/S0168-0102(00)00213-3

M3 - Review article

C2 - 11223470

AN - SCOPUS:0035132339

SN - 0168-0102

VL - 39

SP - 247

EP - 251

JO - Neuroscience Research

JF - Neuroscience Research

IS - 2

ER -

Effects of fibronectin cleaved by neuropsin on cell adhesion and migration

Abstract

Keywords

ASJC Scopus subject areas

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