Current mechanistic insights into the roles of matrix metalloproteinases in tumour invasion and metastasis

2015 ◽  
Vol 237 (3) ◽  
pp. 273-281 ◽  
Author(s):  
Gordon T Brown ◽  
Graeme I Murray
Keyword(s):  
Matrix Metalloproteinases ◽  
Tumour Invasion ◽  
Invasion And Metastasis

scholarly journals Matrix metalloproteinases and their inhibitors in gastric cancer

Gut ◽  
1998 ◽  
Vol 43 (6) ◽  
pp. 791-797 ◽  
Author(s):  
G I Murray ◽  
M E Duncan ◽  
E Arbuckle ◽  
W T Melvin ◽  
J E Fothergill
Keyword(s):  
Gastric Cancer ◽  
Matrix Metalloproteinases ◽  
Paraffin Wax ◽  
Tumour Invasion ◽  
Invasion And Metastasis ◽  
Gastric Cancers ◽  
Formalin Fixed Paraffin ◽  
The Matrix ◽  
Normal Stomach ◽  
Formalin Fixed

Background—The matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs) are strongly implicated in tumour invasion and metastasis.Aims—To investigate the presence of individual MMPs and TIMPs in gastric cancer.Methods—The presence of MMP-1, MMP-2, MMP-3, MMP-9, TIMP-1, and TIMP-2 was identified in a group of gastric cancers (n=74) by immunohistochemistry using monoclonal antibodies. These antibodies were effective on formalin fixed, paraffin wax embedded sections.Results—A large proportion (94%) of gastric cancers contained MMP-2; MMP-1 and MMP-9 were also detected in 73% and 70% of tumours respectively. MMP-3 was only present in 27% of tumours. MMP-1 and MMP-9 were found predominantly in intestinal type tumours. TIMP-1 and TIMP-2 were identified in 41% and 57% of tumours respectively. Immunoreactivity for individual MMPs or TIMPs was not identified in normal stomach.Conclusions—This study shows the presence of matrix metalloproteinases, particularly MMP-2, and TIMPs in stomach cancer. Antibodies which are effective in formalin fixed, paraffin wax embedded sections are useful for the identification of MMPs and TIMPs in diagnostic specimens.

scholarly journals Matrix metalloproteinases in the process of invasion and metastasis of breast cancer

2006 ◽  
Vol 14 (3-4) ◽  
pp. 136-140 ◽  
Author(s):  
Gordana Konjevic ◽  
Sandra Stankovic
Keyword(s):  
Breast Cancer ◽  
Matrix Metalloproteinases ◽  
Tumor Progression ◽  
Tumor Cells ◽  
Proteolytic Enzymes ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Collagen Type Iv ◽  
Cell Contact ◽  
Invasion And Metastasis ◽  
Mesenchymal Transition

Metastatic cascade in malignant tumors, including breast cancer, starts with localized invasion of the host tissue. This process, requiring that tumor cells separate from each other, includes loss of homotypic and heterotypic cell adhesion and cell-cell contact inhibition, acquisition of motility, exacerbated by "epithelial-to-mesenchymal transition", and production of proteolytic enzymes which degrade basal membrane and extracellular matrix. In this sense, aside from urokinase type plasminogen activator, increased expression and activity of matrix metalloproteinases (MMPs) is one of the earliest and most sustained events in tumor progression, playing a role in angiogenesis, invasion and metastasis. MMPs are a family of 23 zinc metalloproteinases, secreted as latent pro-enzymes, activated by proteolytic cleavage, and inhibited by the tissue inhibitors of metalloproteinases. The most commonly connected MMPs with the processes of metastasis are MMP-2 (gelatinase A) and MMP-9 (gelatinase B), due to their ability to degrade collagen type IV, major component of vascular basement membrane. MMP-2 and MMP-9 are also required for the switch to the "angiogenic phenotype" during tumor progression and activation of dormant tumor cells. The association of the increase in serum MMP-2 and MMP-9 activity and clinical stage suggests the usefulness of these parameters as markers in the follow-up and prognosis of breast cancer patients. The concept of "stromal-directed therapy" of cancer, with MMP-inhibitors directed against MMPs as targets, is based on the observed MMP up-regulation in tumors.

Dimethylfumarate inhibits tumor cell invasion and metastasis by suppressing the expression and activities of matrix metalloproteinases in melanoma cells

2009 ◽  
Vol 33 (10) ◽  
pp. 1087-1094 ◽  
Author(s):  
Yuzuru Yamazoe ◽  
Masanobu Tsubaki ◽  
Hiroshi Matsuoka ◽  
Takao Satou ◽  
Tatsuki Itoh ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Melanoma Cells ◽  
Tumor Cell Invasion ◽  
Invasion And Metastasis

scholarly journals ∆133p53 isoform promotes tumour invasion and metastasis via interleukin-6 activation of JAK-STAT and RhoA-ROCK signalling

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Hamish Campbell ◽  
Nicholas Fleming ◽  
Imogen Roth ◽  
Sunali Mehta ◽  
Anna Wiles ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Tumour Invasion ◽  
Invasion And Metastasis

Mechanisms of tumour invasion and metastasis: emerging targets for therapy

2002 ◽  
Vol 6 (2) ◽  
pp. 217-233 ◽  
Author(s):  
Erik W Thompson ◽  
John T Price
Keyword(s):  
Tumour Invasion ◽  
Invasion And Metastasis

Extracellular matrix 6: Role of matrix metalloproteinases in tumor invasion and metastasis

1993 ◽  
Vol 7 (15) ◽  
pp. 1434-1441 ◽  
Author(s):  
William G. Stetler‐Stevenson ◽  
Lance A. Liotta ◽  
David E. Kleiner
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinases ◽  
Tumor Invasion ◽  
Invasion And Metastasis
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