Related Experiment Video

Updated: Jun 23, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
07:32

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

Published on: March 30, 2022

Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity

Denis Gingras1, Richard Béliveau

  • 1Laboratoire de Médecine Moléculaire, Université du Québec à Montréal, C.P. 8888, Succ. Centre-ville, Montréal, Québec, Canada H3C 3P8.

Biochimica Et Biophysica Acta
|May 5, 2009
PubMed

Insights

Membrane-type 1 matrix metalloproteinase (MT1-MMP) aids tumor cell invasion by degrading extracellular matrix. Its intracellular domain also regulates cell invasion by controlling MT1-MMP localization and signaling pathways.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Oncology

Background:

  • Membrane-type 1 matrix metalloproteinase (MT1-MMP) facilitates tumor cell invasion by degrading extracellular matrix (ECM).
  • While MT1-MMP's proteolytic activity is well-studied, its intracellular domain's role in invasion is emerging.
  • The cytoplasmic domain influences MT1-MMP cell surface localization and signal transduction.

Purpose of the Study:

  • To investigate the role of the intracellular domain of MT1-MMP in tumor cell invasion.
  • To elucidate how MT1-MMP's intracellular domain links ECM proteolysis to cellular function modification.
  • To provide new insights into the mechanisms controlling neoplastic cell invasion.

Main Methods:

  • Focus on identifying molecular events linking intracellular MT1-MMP function to cell behavior.
  • Analysis of signaling cascades regulated by the cytoplasmic domain of MT1-MMP.
  • Studies on the regulation of MT1-MMP cell surface localization.

Main Results:

  • The cytoplasmic domain of MT1-MMP plays an active role in tumor cell invasion.
  • Intracellular MT1-MMP regulates enzyme localization and activates signaling pathways.
  • Linking ECM degradation to cellular function modification through intracellular mechanisms.

Conclusions:

  • MT1-MMP's intracellular domain is crucial for its role in tumor cell invasion.
  • Understanding these intracellular mechanisms can reveal new therapeutic targets for cancer.
  • MT1-MMP's dual role (proteolytic and signaling) is key to its invasive function.

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

Related Concept Videos

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...
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.
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...
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...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...