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 The hepatitis B virus X protein promotes tumor cell invasion by inducing membrane-type matrix metalloproteinase-1 and cyclooxygenase-2 expression

2002 ◽  
Vol 110 (12) ◽  
pp. 1831-1838 ◽  
Author(s):  
Enrique Lara-Pezzi ◽  
Maria Victoria Gómez-Gaviro ◽  
Beatriz G. Gálvez ◽  
Emilia Mira ◽  
Miguel A. Iñiguez ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Tumor Cell Invasion ◽  
X Protein ◽  
Matrix Metalloproteinase 1 ◽  
B Virus ◽  
Membrane Type

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.

scholarly journals Lack of Association between Membrane-Type 1 Matrix Metalloproteinase Expression and Clinically Relevant Molecular or Morphologic Tumor Characteristics at the Leading Edge of Invasive Colorectal Carcinoma

2015 ◽  
Vol 2015 ◽  
pp. 1-7 ◽  
Author(s):  
Annette Arndt ◽  
Klaus Kraft ◽  
Eva Wardelmann ◽  
Konrad Steinestel
Keyword(s):  
Matrix Metalloproteinase ◽  
Protein Expression ◽  
Tumor Growth ◽  
Tumor Cell ◽  
Growth Pattern ◽  
Leading Edge ◽  
Tumor Characteristics ◽  
Mutation Status ◽  
Membrane Type

Colorectal cancer (CRC) is one of the leading causes of death from cancer in the western world, but tumor biology and clinical course show great interindividual variation. Molecular and morphologic tumor characteristics, such asKRAS/BRAFmutation status, mismatch repair (MMR) protein expression, tumor growth pattern, and tumor cell budding, have been shown to be of key therapeutic and/or prognostic relevance in CRC. Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a membrane-anchored zinc-binding endopeptidase that is expressed at the leading edge of various invasive carcinomas and promotes tumor cell invasion through degradation of the extracellular matrix. The aim of this study was to investigate possible associations between MT1-MMP expression and molecular tumor characteristics as well as morphologic features of tumor aggressiveness in a consecutive series of 79 CRC tissue samples. However, although MT1-MMP was expressed in 41/79 samples (52%), there was no significant association between MT1-MMP expression andKRAS/BRAFmutation status, MMR protein expression, presence of lymphovascular invasion, tumor growth pattern, tumor-infiltrating lymphocytes, or tumor cell budding in our sample cohort (P>0.05). Thus, we conclude that although MT1-MMP may play a role in CRC invasion, it is not of key relevance to the current models of CRC invasion and aggressiveness.

scholarly journals Matrix Metalloproteinase-9 Regulates Tumor Cell Invasion through Cleavage of Protease Nexin-1

2010 ◽  
Vol 70 (17) ◽  
pp. 6988-6998 ◽  
Author(s):  
Danmei Xu ◽  
Chad M. McKee ◽  
Yunhong Cao ◽  
Yunchuan Ding ◽  
Benedikt M. Kessler ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Matrix Metalloproteinase 9 ◽  
Tumor Cell Invasion ◽  
Protease Nexin ◽  
Metalloproteinase 9

Potentiation of tumor cell invasion by co-culture with monocytes accompanying enhanced production of matrix metalloproteinase and fibronectin

2012 ◽  
Vol 30 (3) ◽  
pp. 289-297 ◽  
Author(s):  
Go Kamoshida ◽  
Ayaka Matsuda ◽  
Risa Miura ◽  
Yuri Takashima ◽  
Arisa Katsura ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Tumor Cell Invasion ◽  
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