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Matrix Metalloproteinases: Multifunctional Contributors To Tumor Progression.

L. Mccawley, L. Matrisian
Published 2000 · Medicine

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Matrix metalloproteinases (MMPs) are a family of extracellular matrix degrading proteinases. Owing to their matrix-degrading abilities and high expression in advanced tumors, MMPs were originally implicated in invasion and metastasis during cancer progression. However, recent work extends a role for MMPs during multiple stages of tumor progression to include other functions such as growth, angiogenesis and migration. Based on studies in animal models implicating MMP activity in cancer, synthetic MMP inhibitors are currently being tested in a clinical setting.
This paper references
10.1073/PNAS.48.6.1014
Collagenolytic activity in amphibian tissues: a tissue culture assay.
J. Gross (1962)
10.1038/284067A0
Metastatic potential correlates with enzymatic degradation of basement membrane collagen
L. Liotta (1980)
10.1097/00000421-198602000-00020
Cancer : Principles and Practice of Oncology
V. Devita (1982)
10.1128/MCB.6.5.1679
Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts.
L. Matrisian (1986)
Degradation of basement membrane type IV collagen and lung subendothelial matrix by rat mammary adenocarcinoma cell clones of differing metastatic potentials.
M. Nakajima (1987)
10.1093/JNCI/82.7.589
Inhibition of collagenolytic activity and metastasis of tumor cells by a recombinant human tissue inhibitor of metalloproteinases.
O. Alvarez (1990)
10.1002/JCP.1041570219
Tissue inhibitor of metalloproteinases‐2 inhibits bFGF‐induced human microvascular endothelial cell proliferation
Anne N. Murphy (1993)
10.1016/s0021-9258(18)53168-9
Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins.
R. Sánchez-López (1993)
10.1016/s0021-9258(18)99931-x
Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin.
V. Baragi (1994)
10.1016/s0021-9258(18)47310-3
Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures.
J. Fowlkes (1994)
10.1042/BJ3040263
Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.
R. Ward (1994)
10.1038/370061A0
A matrix metalloproteinase expressed on the surface of invasive tumour cells
H. Sato (1994)
Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth.
S. Koop (1994)
10.1016/s0021-9258(17)37419-7
Assessment of the role of the fibronectin-like domain of gelatinase A by analysis of a deletion mutant.
G. Murphy (1994)
10.1073/PNAS.91.19.8856
Integrin alpha v beta 3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen.
A. Montgomery (1994)
10.1126/SCIENCE.8278810
Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor.
B. Lovejoy (1994)
10.1093/JNCI/86.4.299
Suppression of the tumorigenic and metastatic abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of the metalloproteinases-1.
R. Khokha (1994)
10.1002/BIES.950170203
E-cadherin as a tumor (invasion) suppressor gene.
W. Birchmeier (1995)
10.1128/MCB.15.10.5732
Collagenase expression in transgenic mouse skin causes hyperkeratosis and acanthosis and increases susceptibility to tumorigenesis
J. D’Armiento (1995)
The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily.
C. Biswas (1995)
10.1159/000468614
Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells.
H. Crawford (1996)
10.1006/SCBI.1996.0020
Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic.
W. Stetler-Stevenson (1996)
The roles of tissue inhibitors of metalloproteinases in tissue remodelling and cell growth.
D. Edwards (1996)
10.1016/0167-4838(95)00259-6
Comparison of cleavage site specificity of gelatinases A and B using collagenous peptides.
T. Xia (1996)
10.1073/PNAS.93.14.7069
Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1.
E. Levi (1996)
10.1172/JCI119435
Inhibition of osteolytic bone metastasis of breast cancer by combined treatment with the bisphosphonate ibandronate and tissue inhibitor of the matrix metalloproteinase-2.
T. Yoneda (1997)
10.1093/MOLEHR/3.1.27
Matrix metalloproteinases as mediators of reproductive function.
D. Hulboy (1997)
10.1083/JCB.139.7.1861
Matrix Metalloproteinase Stromelysin-1 Triggers a Cascade of Molecular Alterations That Leads to Stable Epithelial-to-Mesenchymal Conversion and a Premalignant Phenotype in Mammary Epithelial Cells
A. Lochter (1997)
10.1074/jbc.272.50.31730
Matrix Metalloproteinase-3 Releases Active Heparin-binding EGF-like Growth Factor by Cleavage at a Specific Juxtamembrane Site*
M. Suzuki (1997)
10.1042/BJ3220809
Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release.
K. Imai (1997)
10.1093/JNCI/89.17.1260
Changing views of the role of matrix metalloproteinases in metastasis.
A. Chambers (1997)
10.1006/EXCR.1997.3711
Cleavage of β4 Integrin by Matrilysin
D. V. Bredow (1997)
10.1126/SCIENCE.277.5323.225
Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5.
G. Giannelli (1997)
Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.
D. Gomez (1997)
10.1073/PNAS.94.4.1402
Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin.
C. Wilson (1997)
10.1021/BI9728708
Proteolytic cleavage of urokinase-type plasminogen activator by stromelysin-1 (MMP-3).
F. Ugwu (1998)
10.1083/JCB.140.6.1535
In Vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy
R. Masson (1998)
Generation of Biologically Active IL-1β by Matrix Metalloproteinases: A Novel Caspase-1-Independent Pathway of IL-1β Processing
U. Schönbeck (1998)
Reduced angiogenesis and tumor progression in gelatinase A-deficient mice.
T. Itoh (1998)
10.1096/fasebj.12.12.1075
Matrix metalloproteinases: structures, evolution, and diversification
I. Massova (1998)
10.1016/S0092-8674(00)80931-9
Disruption of Angiogenesis by PEX, a Noncatalytic Metalloproteinase Fragment with Integrin Binding Activity
P. Brooks (1998)
The matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis.
L. Rudolph-Owen (1998)
10.1016/S0962-8924(98)01362-2
ECM signalling: orchestrating cell behaviour and misbehaviour.
M. Lukashev (1998)
10.1016/S0960-9822(99)80153-5
Basement membrane: Putting up the barriers
J Schwarzbauer (1999)
10.1111/j.1749-6632.1999.tb09533.x
The Matrix Metalloproteinases and Their Inhibitors in the Treatment of Pancreatic Cancer
L. Jones (1999)
10.1016/S0092-8674(00)81009-0
The Stromal Proteinase MMP3/Stromelysin-1 Promotes Mammary Carcinogenesis
M. Sternlicht (1999)
10.1172/JCI6870
Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention.
W. Stetler-Stevenson (1999)
10.1111/j.1749-6632.1999.tb07688.x
Preclinical and Clinical Studies of MMP Inhibitors in Cancer
ALAN H. DRUMMOND (1999)
10.1126/SCIENCE.284.5415.808
Effects of angiogenesis inhibitors on multistage carcinogenesis in mice.
G. Bergers (1999)
10.1111/j.1749-6632.1999.tb07689.x
Broad Antitumor and Antiangiogenic Activities of AG3340, a Potent and Selective MMP Inhibitor Undergoing Advanced Oncology Clinical Trials
D. Shalinsky (1999)



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Kun Peng (2021)
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Jie Wang (2021)
10.1002/ADFM.202009765
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T. Hattori (2021)
10.1002/jum.15738
Low-Intensity Pulsed Ultrasound Stimulation for Bone Fractures Healing: A Review.
P. Palanisamy (2021)
10.3892/br.2021.1446
Adipose-PAS interactions in the context of its localised bio-engineering potential (Review)
M. Nohawica (2021)
10.3390/toxins12110713
Biological Activity of Berberine—A Summary Update
Anna Och (2020)
10.1007/s10585-019-10017-y
Tissue inhibitor of matrix metalloproteinase-3 has both anti-metastatic and anti-tumourigenic properties
G. Rai (2020)
10.1016/j.biopha.2020.111136
EnDuo, a novel derivative of Endostar, inhibits the migration of colon cancer cells, suppresses matrix metalloproteinase-2/9 expression and impedes AKT/ERK activation.
Elina Idiiatullina (2020)
10.1177/0300060520980211
A polymorphism in the 3′-untranslated region of the matrix metallopeptidase 9 gene is associated with susceptibility to idiopathic calcium nephrolithiasis in the Chinese population
Q. Bu (2020)
10.7150/jca.38624
Curcumol inhibits the proliferation and metastasis of melanoma via the miR-152-3p/PI3K/AKT and ERK/NF-κB signaling pathways
Ning Ning (2020)
10.22456/1679-9216.100451
Morphometric and Vascular Analyses and MMP-2 Expression in Bladders of Animals with Bovine Enzootic Haematuria
A. B. Archanjo (2020)
10.1038/s41388-020-01463-0
MBIP (MAP3K12 binding inhibitory protein) drives NSCLC metastasis by JNK-dependent activation of MMPs
J. Ochieng (2020)
10.3390/jcm9020479
Role of Endogenous Regulators of Hem- And Lymphangiogenesis in Corneal Transplantation
T. Clahsen (2020)
10.1002/adma.201907210
Engineering Stimuli-Activatable Boolean Logic Prodrug Nanoparticles for Combination Cancer Immunotherapy.
Bo Hou (2020)
10.1155/2020/8180261
Antimetastatic Potential of Rhodomyrtone on Human Chondrosarcoma SW1353 Cells
Malatee Tayeh (2020)
10.1016/j.phrs.2020.104964
Effect of Carbonic Anhydrase IX inhibitors on human endothelial cell survival.
Shirley Genah (2020)
10.1002/jcp.28936
The novel non‐immunological role and underlying mechanisms of B7‐H3 in tumorigenesis
Xiangqin Zhou (2019)
10.1016/j.urolonc.2019.04.017
Immunohistochemical expression of CD44, matrix metalloproteinase2 and matrix metalloproteinase9 in renal cell carcinomas.
Yong-Moon Lee (2019)
Programming Stimuli-Responsive Behavior into Biomaterials
Nikhil Jain (2019)
10.1007/978-3-030-21477-7_2
Targeting the Tumor Microenvironment to Overcome Resistance to Therapy
Bessi Qorri (2019)
10.1016/j.bbcan.2019.01.005
Potential roles and targeted therapy of the CXCLs/CXCR2 axis in cancer and inflammatory diseases.
Yuan Cheng (2019)
10.1039/c8md00375k
Molecular modelling studies of quinazolinone derivatives as MMP-13 inhibitors by QSAR, molecular docking and molecular dynamics simulations techniques.
Shanshan Huang (2019)
10.1016/j.matbio.2019.11.005
The role of extracellular matrix in biomechanics and its impact on bioengineering of cells and 3D tissues.
Max Urbanczyk (2019)
10.1016/j.bmc.2019.03.043
Identification of highly potent and selective MMP2 inhibitors addressing the S1' subsite with d-proline-based compounds.
E. Lenci (2019)
10.1016/j.compbiolchem.2018.10.017
Enzymatic inhibitory activity of iridoid glycosides from Picrorrhiza kurroa against matrix metalloproteinases: Correlating in vitro targeted screening and docking
Dharmender Rathee (2019)
10.1002/jcp.29014
New trends in glioma cancer therapy: Targeting Na+/H + exchangers
O. Tamtaji (2019)
10.1016/j.preteyeres.2019.07.001
Immune reactions after modern lamellar (DALK, DSAEK, DMEK) versus conventional penetrating corneal transplantation
Deniz Hos (2019)
10.3390/ph12020079
Targeting MMP-9 in Diabetic Foot Ulcers
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