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Related Concept Videos

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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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

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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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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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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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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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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...
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Related Experiment Video

Updated: Nov 23, 2025

Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

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Collagen Structure-Function Mapping Informs Applications for Regenerative Medicine.

James D San Antonio1, Olena Jacenko2, Andrzej Fertala3

  • 1Biocorda LLC, Media, PA 19063, USA.

Bioengineering (Basel, Switzerland)
|January 1, 2021
PubMed
Summary
This summary is machine-generated.

Type I collagen

Keywords:
angiogenesisconnective tissueextracellular matrixfibrosishemostasisinteractomeligand bindingmicrofibriltherapeutic antibodiestype I collagentype III collagen

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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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Engineering 3D Cellularized Collagen Gels for Vascular Tissue Regeneration
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Tissue Engineering

Background:

  • Type I collagen is a critical structural protein in vertebrates, essential for tissue integrity and function.
  • Collagen dysfunction is implicated in various diseases, including fibrosis, cancer metastasis, and brittle bone disease.
  • Understanding collagen's structure-function relationship is key to developing new therapeutic strategies.

Purpose of the Study:

  • To construct a type I collagen fibril interactome to elucidate its structure-function relationship.
  • To identify functional sites and disease-associated mutations within type I collagen.
  • To map collagen's roles in tissue structure, cell interactions, and disease pathogenesis.

Main Methods:

  • Construction of a type I collagen fibril interactome.
  • Projection of interactome data onto an X-ray diffraction model of native collagen microfibrils.
  • Corroboration using a type III collagen interactome.

Main Results:

  • Identification of a matrix interaction domain involved in collagen assembly, crosslinking, proteoglycan binding, and mineralization.
  • Identification of a cell interaction domain crucial for hemostasis, tissue remodeling, and cell adhesion.
  • A proposed model where tissue injury exposes collagen's cell and ligand binding sites.

Conclusions:

  • The type I collagen fibril interactome reveals distinct structural and cell interaction domains.
  • Collagen's functional face shifts from structural to dynamic upon tissue injury, facilitating regeneration.
  • Insights can guide the development of anti-fibrotic therapies and enhanced angiogenic biomaterials.