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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...
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...
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...
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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...

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Related Experiment Video

Updated: Jul 14, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

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

Published on: September 20, 2012

Collagen pretzels revealed by electron microscopy.

Karl Kadler1

  • 1Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK. karl.kadler@manchester.ac.uk

The Biochemical Journal
|May 25, 2007
PubMed
Summary

Researchers visualized collagen XV, a large structural protein, revealing its unique pretzel-like shape and complex multimerization. This provides new insights into collagen structure and function in tissues.

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Related Experiment Videos

Last Updated: Jul 14, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

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

Published on: September 20, 2012

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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Production of Nanofibrillar Patterned Collagen for Tissue Engineering
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Collagen XV is a large, multidomain structural protein crucial for skeletal muscle and capillaries.
  • Its complex structure and proteoglycan nature hinder high-resolution structural analysis.
  • Previous studies lacked detailed structural data due to collagen's inherent properties.

Discussion:

  • Rotary shadowing electron microscopy revealed detailed images of purified collagen XV molecules.
  • The N-terminus exhibits a distinct three-lobed structure, and individual glycosaminoglycan chains are visible.
  • Collagen XV molecules form unique, knotted, pretzel-like structures, challenging conventional views of collagen morphology.

Key Insights:

  • Collagen XV molecules multimerize into cruciform structures, with simpler complexes containing two to four molecules.
  • Immunoelectron microscopy demonstrated these complexes bridging collagen fibrils near basement membranes.
  • The study successfully purified collagen XV from human umbilical cord, despite its low abundance.

Outlook:

  • These findings offer unprecedented structural insights into collagen XV.
  • Understanding collagen XV's structure may elucidate its role in tissue integrity and disease.
  • Further research can explore the functional implications of its unique quaternary structure.