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Matrix Metalloproteinases

Current Protocols in Cell Biology, 2003
AbstractMatrix metalloproteinases are a class of enzymes that play an important role in the remodeling of the extracellular matrix in development and cancer metastasis. This unit describes a set of methods‐cell‐mediated dissolution of type I collagen fibrils, direct and reverse zymography, enzyme capture based on a‐2 macroglubulin and TIMP‐1 and ‐2 ...
Henning, Birkedal-Hansen   +6 more
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Matrix metalloproteinases

Current Opinion in Chemical Biology, 1998
Matrix metalloproteinases are a family of highly regulated peptidases that are collectively responsible for the degradation of extracellular matrix during tissue remodeling. Dysregulated activity has long been implicated in the pathologies of cancer and arthritis, and the number of diseases more recently associated with these enzymes has been ...
L L, Johnson, R, Dyer, D J, Hupe
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Metalloproteinases and tissue inhibitors of metalloproteinases

Breast Cancer Research and Treatment, 1998
Because the proteolytic degradation of extracellular matrix is required for invasion and metastasis, it would appear that the important family of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) might be prognostic indicators of the invasive potential of a breast tumor.
M, Toi, S, Ishigaki, T, Tominaga
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Labelling Matrix Metalloproteinases

Current Medicinal Chemistry, 2023
Abstract: Matrix metalloproteinases (MMPs) are a family of zinc-containing proteases that participate in many physiological and pathological processes in vivo. Recently, the MMP network has been established according to a deeper understanding of its functions. Some MMPs have been also regarded as biomarkers of various diseases, including inflammation,
Run-Fu Zhang   +3 more
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Matrix Metalloproteinases

2012
Remodeling of extracellular matrix is crucial for many physiological (cell migration, proliferation, growth, and development) and pathological (remodeling of heart, carcinogenesis, metastasis, etc.) events. Thus, the interaction between cells and extracellular matrix plays a key role in normal development and differentiation of organism and many ...
Viola, Vargová   +2 more
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Matrix degrading metalloproteinases

Journal of Neuro-Oncology, 1994
Matrix degrading metalloproteinases are enzymes that degrade proteins in tissue extracellular matrices. These proteinases exhibit specific, well defined properties that allow them to be classified into a family of enzymes. They are secreted by various cell types as the cells effect their surrounding extracellular matrix.
B W, Ennis, L M, Matrisian
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Matrix metalloproteinase inhibitors

Current Oncology Reports, 2004
Matrix metalloproteinases (MMPs) are a family of zinc-dependent proteinases that are associated with the tumorigenic process. MMPs degrade the extracellular matrix, promoting tumor invasion and metastasis. They also regulate host defense mechanisms and normal cell function; blocking all MMPs may not lead to a positive therapeutic outcome. Most clinical
Nithya, Ramnath, Patrick J, Creaven
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Snake venom metalloproteinases

Toxicon, 2013
Recent proteomic analyses of snake venoms show that metalloproteinases represent major components in most of the Crotalid and Viperid venoms. In this chapter we discuss the multiple activities of the SVMPs. In addition to hemorrhagic activity, members of the SVMP family also have fibrin(ogen)olytic activity, act as prothrombin activators, activate ...
Francis S, Markland, Stephen, Swenson
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Matrix metalloproteinase inhibitors

Breast Cancer Research and Treatment, 1997
Matrix metalloproteinases (MMPs) are a family of enzymes responsible for the breakdown of proteins of connective tissue. Through this action they play an important role in growth, development and tissue repair. Recent studies also suggest that MMPs are utilised in cancer, facilitating both local tumour invasion and metastasis.
S M, Wojtowicz-Praga   +2 more
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Agavain: A metalloproteinase

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
Summary 1. Crystalline agavain has been shown to be inhibited by metal binding agents and DFP, but not by sulfhydryl reagents. 2. The activity of agavain is sensitive to the nature of the buffer solution used in the assay medium, this inhibitory effect being a function of the buffer anions. 3.
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