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Related Concept Videos

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.
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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...
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...
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 Bone Matrix01:18

The Bone Matrix

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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Related Experiment Video

Updated: Jul 22, 2026

Detection of Functional Matrix Metalloproteinases by Zymography
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Published on: November 8, 2010

Role of matrix proteases in processing enamel proteins.

J F Woessner1

  • 1Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101, USA. fwoessne@mednet.med.miami.edu

Connective Tissue Research
|November 4, 2000
PubMed
Summary

Researchers are studying enamel proteases, crucial for processing enamel matrix proteins. Key findings include the identification and classification of two specific proteases, EMSP-1 and enamelysin, advancing our understanding of enamel development and degradation.

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Area of Science:

  • Biochemistry
  • Dental Research
  • Enamel Matrix Biology

Background:

  • Enamel matrix proteins undergo significant processing during tooth development.
  • Proteases play a critical role in the degradation of these matrix proteins.
  • Understanding enamel proteases is key to comprehending enamel formation and maturation.

Purpose of the Study:

  • To review the current research status of enamel proteases.
  • To summarize the historical development and current understanding of enamel matrix proteases.
  • To identify and characterize key proteases involved in enamel protein processing.

Main Methods:

  • Literature review of historical and current research on enamel proteases.
  • Identification and classification of recently cloned proteases.
  • Outline of the major features of identified protease families.

Main Results:

  • Two proteases have been cloned: enamel matrix serine protease-1 (EMSP-1) and enamelysin.
  • EMSP-1 is classified as a serine protease (chymotrypsin family S1, clan SA).
  • Enamelysin is classified as a metalloprotease (matrixin family/matrix metalloproteinase family, M10, clan MB).

Conclusions:

  • The identification of EMSP-1 and enamelysin represents significant progress in enamel protease research.
  • Further research is needed to identify additional enamel proteases.
  • Characterization of known proteases requires continued investigation to fully understand their roles.