Related Experiment Video

Updated: Jul 29, 2026

Detection of Functional Matrix Metalloproteinases by Zymography
09:30

Detection of Functional Matrix Metalloproteinases by Zymography

Published on: November 8, 2010

Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many

M P d'Ortho1, H Will, S Atkinson

  • 1INSERM U296, Faculté de Médecine, Créteil, France. dortho@im3.inserm.fr

European Journal of Biochemistry
|February 14, 1998
PubMed

Insights

Membrane-type matrix metalloproteinases (MT-MMPs) degrade various extracellular matrix components, including collagens. MT1-MMP, with its hemopexin domain, specifically cleaves type-I and type-III collagens, impacting cell-matrix interactions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Matrix metalloproteinases (MMPs) are crucial for extracellular matrix (ECM) remodeling.
  • Membrane-type MMPs (MT-MMPs) are implicated in cell invasion and tissue remodeling.
  • Understanding MT-MMP substrate specificity is key to their biological function.

Purpose of the Study:

  • To investigate the substrate degradation profiles of MT1-MMP and MT2-MMP catalytic domains.
  • To determine the role of the hemopexin domain in MT1-MMP collagenolytic activity.
  • To explore the capacity of MT-MMPs to process tumor necrosis factor-alpha (TNF-α).

Main Methods:

  • Expression and purification of soluble recombinant catalytic and full-domain MT1-MMP and MT2-MMP.
  • Enzymatic assays using various ECM proteins (fibronectin, tenascin, nidogen, aggrecan, perlecan, laminin, type-I and type-III collagens).
  • Analysis of pro-TNF-α processing and subsequent degradation.

Main Results:

  • Activated MT-MMPs degraded fibronectin, tenascin, nidogen, aggrecan, and perlecan.
  • MT2-MMP uniquely degraded laminin.
  • MT1-MMP with the hemopexin domain specifically cleaved type-I and type-III collagens, unlike its catalytic domain alone.
  • MT-MMPs processed pro-TNF-α but the mature TNF-α was further degraded.

Conclusions:

  • MT-MMPs possess broad substrate specificity for ECM macromolecules.
  • The hemopexin domain is essential for MT1-MMP's collagenase activity.
  • MT-MMPs contribute to ECM degradation and may modulate cell-matrix interactions.
  • MT-MMPs can process TNF-α, but its stability is limited.

More Related Videos

Measuring Global Cellular Matrix Metalloproteinase and Metabolic Activity in 3D Hydrogels07:39

Measuring Global Cellular Matrix Metalloproteinase and Metabolic Activity in 3D Hydrogels

Published on: January 22, 2019

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography07:32

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

Published on: March 30, 2022

Related Concept Videos

The Extracellular Matrix01:42

The Extracellular Matrix

In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.Composition of the Extracellular MatrixThe extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse molecules.
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Extracellular Matrix01:29

The Extracellular Matrix

Overview
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...