Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Phases of Wound Repair01:28

Phases of Wound Repair

Following injury, the integrity of the injured tissues must be reestablished. For example, in skin tissue, wound repair involves coordination among resident skin cells, blood mononuclear cells, extracellular matrix, growth factors, and cytokines to complete the healing cascade.
Formation of Blood Clot
In case of deep injuries, trauma to blood vessels results in blood loss. In the meantime, phospholipids released from the ruptured endothelial cellular membrane are converted into arachidonic...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
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...
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Matrix metalloproteinase 13 (MMP-13) processing of type II collagen is altered by antibodies and citrullination found in the early stages of rheumatoid arthritis.

Matrix biology : journal of the International Society for Matrix Biology·2025
Same author

Pharmacogenomic Drug-Gene Interactions in Geriatric Emergency Department Patients Who Sustained Falls: A Pilot Study.

The western journal of emergency medicine·2025
Same author

Membrane-Type 5 Matrix Metalloproteinase (MT5-MMP): Background and Proposed Roles in Normal Physiology and Disease.

Biomolecules·2025
Same author

Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.

Biochemistry·2024
Same author

Editorial - FAU research on Alzheimer's disease.

Journal of cellular physiology·2024
Same author

Identification of binding partners that facilitate membrane-type 5 matrix metalloproteinase (MT5-MMP) processing of amyloid precursor protein.

Journal of cellular physiology·2024

Related Experiment Video

Updated: May 14, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Interstitial collagen catabolism.

Gregg B Fields1

  • 1Torrey Pines Institute for Molecular Studies, Port St. Lucie, FL 34987, USA. gfields@tpims.org

The Journal of Biological Chemistry
|February 23, 2013
PubMed
Summary
This summary is machine-generated.

Proteases break down collagen, a process vital for development and health but also linked to disease. Understanding these collagenolytic enzymes and their mechanisms is key to targeting related pathologies.

More Related Videos

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
07:28

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Published on: July 23, 2015

Related Experiment Videos

Last Updated: May 14, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
07:28

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Published on: July 23, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Interstitial collagen's mechanical and biological properties are modulated by proteases.
  • Collagenolysis, the hydrolysis of collagen's triple-helical structure, is essential for development and homeostasis.
  • Dysregulated collagenolysis contributes to various pathological conditions.

Purpose of the Study:

  • To elucidate the mechanisms of collagenolytic enzymes.
  • To understand how ancillary biomolecules influence collagenolysis.
  • To provide insights into the role of collagenolysis in health and disease.

Main Methods:

  • Experimental definition of the mechanism of action for matrix metalloproteinase-1 (MMP-1).
  • Comparative analysis of collagenolytic enzyme activities.
  • Investigation of ancillary biomolecule interactions with collagenolytic enzymes.

Main Results:

  • Components of the MMP-1 mechanism of action have been experimentally defined.
  • Insights into the mechanisms of other collagenolytic enzymes were provided.
  • Modulatory effects of ancillary biomolecules on collagenolytic enzyme action were observed.

Conclusions:

  • Collagenolysis is a critical biological process with implications in development, homeostasis, and pathology.
  • Matrix metalloproteinases, cathepsin K, and neutrophil elastase are key mammalian collagenolytic enzymes.
  • Further research into collagenolytic mechanisms and their regulation holds therapeutic potential.