Matrix Metalloproteinases

Matrix metalloproteinases (MMPs) are zinc-dependent enzymes that remodel the extracellular matrix by selectively degrading proteins such as collagen, elastin, and fibronectin. Cells typically produce MMPs as inactive zymogens, which become activated when cleavage exposes the catalytic site; their activity is regulated by tissue inhibitors of metalloproteinases. In bioengineering, researchers use MMP-responsive materials and engineered scaffolds to control matrix degradation, cell migration, and tissue remodeling. Understanding MMP activity supports the design of biomaterials for wound healing, drug delivery, and tissue regeneration while providing ways to investigate how dysregulated matrix turnover contributes to disease.

Matrix Metalloproteinases - Related Videos

Research

JoVE Journal - Biology
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Detection of Functional Matrix Metalloproteinases by Zymography

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Cited by 128 •

2010

This protocol describes an activity-based assay for detecting matrix metalloproteinases in culture supernatants or body fluids.

Research

JoVE EoE - Electrophoresis Techniques

Zymography Gel Electrophoresis: An Electrophoretic Technique to Detect Matrix Metalloproteinases by Assessing the Enzymatic Activity

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2025

This video demonstrates the zymography gel electrophoresis technique to assess the activity of matrix metalloproteinases (MMPs) present in cell culture supernatant. The active MMPs degrade the MMP-specific substrate embedded in a polyacrylamide gel, which appears as clear bands against a dark stained background following staining.

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

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Cited by 4 •

2019

Here, a protocol is presented for encapsulating and culturing cells in poly(ethylene glycol) (PEG) hydrogels functionalized with a fluorogenic matrix metalloproteinase (MMP)-degradable peptide. Cellular MMP and metabolic activity are measured directly from the hydrogel cultures using a standard microplate reader.

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

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Cited by 5 •

2022

His-tag purification, dialysis, and activation are employed to increase yields of soluble, active matrix metalloproteinase-3 catalytic domain protein expression in bacteria. Protein fractions are analyzed via SDS-PAGE gels.

Education

JoVE Core - Anatomy and Physiology

The Bone Matrix

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2025

Bone contains a relatively small number of cells entrenched in a matrix of collagen fibers that provide an adherent surface for inorganic salt crystals. Both components of the matrix, organic and inorganic, contribute to the unusual properties of bone. Without collagen, bones would be brittle and shatter easily. Without mineral crystals, bones would flex and provide little support. This can be observed by an experiment: when the minerals of a bone are dissolved by soaking the bone in acid or...

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