A novel celecoxib analog UTX-121 inhibits HT1080 cell invasion by modulating membrane-type 1 matrix metalloproteinase

2020 ◽  
Vol 521 (1) ◽  
pp. 137-144
Author(s):  
Hirari Yamahana ◽  
Takahisa Takino ◽  
Yoshio Endo ◽  
Hisatsugu Yamada ◽  
Takeshi Suzuki ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Ht1080 Cell ◽  
Membrane Type

Neutrophil-derived serine proteinases enhance membrane type-1 matrix metalloproteinase–dependent tumor cell invasion

Surgery ◽  
2000 ◽  
Vol 127 (2) ◽  
pp. 142-147 ◽  
Author(s):  
Peter Shamamian ◽  
Ben J.Z. Pocock ◽  
Jess D. Schwartz ◽  
Sara Monea ◽  
Neal Chuang ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Tumor Cell Invasion ◽  
Serine Proteinases ◽  
Membrane Type

scholarly journals SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1–matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion

2014 ◽  
Vol 25 (13) ◽  
pp. 2061-2070 ◽  
Author(s):  
Karla C. Williams ◽  
Rachael E. McNeilly ◽  
Marc G. Coppolino
Keyword(s):  
Membrane Protein ◽  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Cellular Invasion ◽  
Protein Receptor ◽  
Ecm Degradation ◽  
Membrane Type ◽  
Regulated Trafficking

Movement through the extracellular matrix (ECM) requires cells to degrade ECM components, primarily through the action of matrix metalloproteinases (MMPs). Membrane type 1–matrix metalloproteinase (MT1-MMP) has an essential role in matrix degradation and cell invasion and localizes to subcellular degradative structures termed invadopodia. Trafficking of MT1-MMP to invadopodia is required for the function of these structures, and here we examine the role of N-ethylmaleimide–sensitive factor–activating protein receptor (SNARE)–mediated membrane traffic in the transport of MT1-MMP to invadopodia. During invadopodium formation in MDA-MB-231 human breast cancer cells, increased association of SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) is detected by coimmunoprecipitation. Blocking the function of these SNAREs perturbs invadopodium-based ECM degradation and cell invasion. Increased level of SNAP23-Syntaxin4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation. These results reveal an important role for SNARE-regulated trafficking of MT1-MMP to invadopodia during cellular invasion of ECM.

scholarly journals Tetraspanin Proteins Regulate Membrane Type-1 Matrix Metalloproteinase-dependent Pericellular Proteolysis

2009 ◽  
Vol 20 (7) ◽  
pp. 2030-2040 ◽  
Author(s):  
Marc A. Lafleur ◽  
Daosong Xu ◽  
Martin E. Hemler
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Three Dimensional ◽  
Tumor Cell Invasion ◽  
Collagen Gels ◽  
Invasion And Metastasis ◽  
Lysosomal Degradation ◽  
Membrane Type ◽  
Pericellular Proteolysis

Membrane type-1 matrix metalloproteinase (MT1-MMP) supports tumor cell invasion through extracellular matrix barriers containing fibrin, collagen, fibronectin, and other proteins. Here, we show that simultaneous knockdown of two or three members of the tetraspanin family (CD9, CD81, and TSPAN12) markedly decreases MT1-MMP proteolytic functions in cancer cells. Affected functions include fibronectin proteolysis, invasion and growth in three-dimensional fibrin and collagen gels, and MMP-2 activation. Tetraspanin proteins (CD9, CD81, and TSPAN2) selectively coimmunoprecipitate and colocalize with MT1-MMP. Although tetraspanins do not affect the initial biosynthesis of MT1-MMP, they do protect the newly synthesized protein from lysosomal degradation and support its delivery to the cell surface. Interfering with MT1-MMP-tetraspanin collaboration may be a useful therapeutic approach to limit cancer cell invasion and metastasis.

Sign in / Sign up

Export Citation Format

Share Document