Related Experiment Video
Updated: Jun 2, 2026
10:37
Induction and Analysis of Epithelial to Mesenchymal Transition
Published on: August 27, 2013
MMP20 cleaves E-cadherin and influences ameloblast development
John D Bartlett1, Yasuo Yamakoshi, James P Simmer
1Department of Cytokine Biology, Forsyth Institute and Department of Developmental Biology, Harvard School of Dental Medicine, Cambridge, Mass., USA. jbartlett@forsyth.org
Cells, Tissues, Organs
|April 29, 2011
Summary
Matrix metalloproteinase-20 (MMP20) is crucial for proper dental enamel formation. MMP20-deficient mice exhibit abnormal ameloblast cell layer morphology, suggesting MMP20 regulates developmental progression.
Area of Science:
- Biochemistry
- Developmental Biology
- Cell Biology
Background:
- Dental enamel formation is a complex process involving ameloblasts.
- Matrix metalloproteinase-20 (MMP20) is essential for enamel matrix secretion and maturation.
- Mutations in MMP20 cause autosomal recessive amelogenesis imperfecta, highlighting its critical role.
Purpose of the Study:
- To investigate the detailed morphology of ameloblasts in Mmp20-null mice during the secretory stage.
- To explore the potential mechanism by which MMP20 influences ameloblast behavior and enamel development.
Main Methods:
- Microscopic examination of ameloblast cell layer morphology in Mmp20-null mice.
- Biochemical assays to determine MMP20's substrate specificity, specifically its interaction with E-cadherin.
Main Results:
- Mmp20-null ameloblasts exhibited unusual morphological changes, retracting and reextending Tomes' processes during the secretory stage.
- MMP20 was found to cleave epithelial cadherin (E-cadherin).
- Cleavage of E-cadherin can release β-catenin, a known transcription factor.
Conclusions:
- MMP20 plays a significant role in regulating ameloblast morphology and developmental progression.
- MMP20 may influence ameloblast differentiation and enamel formation by cleaving E-cadherin and potentially affecting β-catenin signaling.
- These findings provide new insights into the molecular mechanisms underlying amelogenesis.
Related Concept Videos
01:23Role 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...
A...
01:19Cadherins in Tissue Organization
The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...
Cell Sorting During Development
Cell sorting plays an...
01:29The 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...
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...
01:42The 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.
01:25Structure of Cadherins
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
01:23Catenins
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...