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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...
Cadherins in Tissue Organization01:19

Cadherins 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...
Catenins01:23

Catenins

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.
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Structure 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...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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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.
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Development of Amelogenin-chitosan Hydrogel for In Vitro Enamel Regrowth with a Dense Interface
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MMP20 modulates cadherin expression in ameloblasts as enamel develops.

X Guan1, J D Bartlett

  • 1Department of Mineralized Tissue Biology and Harvard School of Dental Medicine, The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA.

Journal of Dental Research
|September 27, 2013
PubMed
Summary

Matrix metalloproteinase-20 (MMP20) is crucial for dental enamel formation. This study reveals MMP20 cleaves E- and N-cadherin, facilitating ameloblast movement essential for healthy enamel structure.

Keywords:
ameloblastcadherinsenamel biomineralization/formationgene expressionjunctional complexesmatrix metalloproteinases (MMPs)

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Published on: July 8, 2021

Area of Science:

  • Biochemistry
  • Developmental Biology
  • Oral Biology

Background:

  • Matrix metalloproteinase-20 (enamelysin, MMP20) is vital for dental enamel development.
  • Mutations in MMP20 cause amelogenesis imperfecta, leading to enamel malformations.
  • Mice lacking Mmp20 exhibit thin, brittle enamel with abnormal rod patterns.

Purpose of the Study:

  • To investigate the mechanism by which MMP20 facilitates ameloblast movement during enamel development.
  • To determine if MMP20 cleaves cell-cell adhesion proteins involved in ameloblast migration.

Main Methods:

  • Analysis of MMP20's enzymatic activity on E-cadherin and N-cadherin.
  • Quantitative assessment of E- and N-cadherin transcript levels in Mmp20 null versus wild-type mice.
  • Examination of ameloblast cadherin expression during different developmental stages in Mmp20 ablated mice.

Main Results:

  • MMP20 was shown to cleave the extracellular domains of E-cadherin and N-cadherin.
  • Mmp20 null mice displayed significantly higher E- and N-cadherin transcript levels compared to wild-type.
  • Ameloblast N-cadherin expression remained high during maturation in Mmp20 ablated mice, and an E- to N-cadherin switch occurred during development.

Conclusions:

  • MMP20 facilitates ameloblast movement by cleaving E- and N-cadherin, essential for proper enamel rod formation.
  • The observed E- to N-cadherin switch during enamel development is critical for ameloblast migration.
  • This mechanism highlights a key process in achieving healthy dental enamel structure.