Related Experiment Video

Updated: Mar 3, 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

5.2K

Peripheral membrane associations of matrix metalloproteinases

Steven R Van Doren1, Tara C Marcink1, Rama K Koppisetti1

  • 1Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, United States.

Biochimica Et Biophysica Acta. Molecular Cell Research
|April 27, 2017
PubMed

Insights

Water-soluble matrix metalloproteinases (MMPs) are not just free-floating; they also bind to cell surfaces. This membrane association influences their activities and localization, impacting cellular processes.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Water-soluble matrix metalloproteinases (MMPs) were traditionally considered freely diffusing in the extracellular matrix.
  • However, multiple MMPs have been detected at cell surfaces, indicating a broader functional scope.

Purpose of the Study:

  • To investigate the membrane-associated behavior of soluble matrix metalloproteinases.
  • To explore how this association influences their biological activities and localization.

Main Methods:

  • Analysis of catalytic domain binding to lipid bilayers for MMP-7 and MMP-12.
  • Nuclear Magnetic Resonance (NMR) assays to study transient associations of MT1-MMP and MMP-12 hemopexin-like domains with lipid bilayers.

Main Results:

  • The catalytic domains of MMP-7 and MMP-12 bind peripherally to lipid bilayers in distinct orientations.
  • Soluble domains of MT1-MMP and MMP-12 exhibit transient associations with lipid bilayers.
  • Peripheral membrane association is predicted for other soluble MMPs.

Conclusions:

  • Soluble MMPs can associate peripherally with cell membranes, challenging the view of them as solely free-diffusing enzymes.
  • This membrane association may facilitate pericellular proteolysis, endocytosis, and interactions with membrane-bound proteins.
  • Concentration near the membrane increases the likelihood of MMPs forming complexes with target proteins.
Keywords:
CompartmentalizationMembrane recognitionMembrane traffickingPeripheral membrane proteinProteaseSheddase

More Related Videos

Detection of Functional Matrix Metalloproteinases by Zymography09:30

Detection of Functional Matrix Metalloproteinases by Zymography

Published on: November 8, 2010

85.1K
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

8.0K

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...
3.6K
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...
9.5K
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...
5.4K
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...
3.7K
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...
12.8K
The Extracellular Matrix01:42

The Extracellular Matrix

Overview
90.2K