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Related Concept Videos

Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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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...
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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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...
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Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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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...
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Structural Protein Function01:56

Structural Protein Function

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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...
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Phases of Wound Repair01:28

Phases of Wound Repair

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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...
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Extracellular Matrix01:26

Extracellular Matrix

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Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
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Related Experiment Video

Updated: Apr 3, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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Collagen VI at a glance.

Matilde Cescon1, Francesca Gattazzo1, Peiwen Chen1

  • 1Department of Molecular Medicine, University of Padova, Padova 35131, Italy.

Journal of Cell Science
|September 18, 2015
PubMed
Summary
This summary is machine-generated.

Collagen VI is a vital extracellular matrix molecule with diverse roles in tissue mechanics and cell protection. Its functions extend to maintaining stemness and are linked to various human disorders.

Keywords:
CollagenExtracellular matrixSkeletal muscle

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An Improved Method for the Preparation of Type I Collagen From Skin
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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Last Updated: Apr 3, 2026

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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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An Improved Method for the Preparation of Type I Collagen From Skin
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Extracellular Matrix Research

Background:

  • Collagen VI is a crucial extracellular matrix protein involved in numerous tissues and diseases.
  • It forms a distinctive beaded microfilament network essential for tissue structure.
  • Collagen VI has multifaceted roles, including biomechanical support and cytoprotection.

Purpose of the Study:

  • To review current knowledge on collagen VI.
  • To highlight its significance in maintaining tissue mechanical properties.
  • To discuss its role in stemness and connections to human disorders.

Main Methods:

  • Literature review and synthesis of existing research on collagen VI.
  • Analysis of collagen VI's biosynthesis, assembly, and functional roles.
  • Examination of its involvement in cellular processes and disease pathology.

Main Results:

  • Collagen VI network provides unique biomechanical functions.
  • It offers cytoprotective effects against apoptosis and oxidative stress.
  • Collagen VI influences tumor growth, autophagy, cell differentiation, and stemness.

Conclusions:

  • Collagen VI is critical for tissue integrity and cellular health.
  • Its roles in stemness and mechanical preservation are key areas of research.
  • Understanding collagen VI's functions offers insights into human disease mechanisms.