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Related Concept Videos

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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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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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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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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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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Collagen XV preserves heart function and protects from pathological remodelling after myocardial infarction.

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A systematic approach to study the effects of acquisition parameters and biological factors on computerized mammography analysis using ex vivo human tissue: A protocol description.

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Corrigendum to Targeting collagen XVIII improves the efficiency of ErbB inhibitors in breast cancer models.

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Mass spectrometric insights into the protein composition of human cutaneous neurofibromas: comparison of neurofibromas with the overlying skin.

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Contribution of collagen XIII to lung function and development of pulmonary fibrosis.

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Related Experiment Video

Updated: Jan 16, 2026

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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Transmembrane and multiplexin collagens in development and pathobiology.

Taina Pihlajaniemi1

  • 1ECM-Hypoxia Research Unit, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7, Oulu 90230, Finland.

Matrix Biology : Journal of the International Society for Matrix Biology
|October 3, 2025
PubMed
Summary
This summary is machine-generated.

This review details the discovery of novel nonfibrillar collagens (types XIII, XV, and XVIII) and their roles in tissue stability and cell function. Research spans decades, utilizing molecular biology and mouse models to understand extracellular matrix contributions to health and disease.

Keywords:
Basement membraneCollagenExtracellular matrixMacitMultiplexinType XIII collagenType XV collagenType XVIII collagen

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

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Area of Science:

  • Extracellular matrix biology
  • Collagen research
  • Molecular and cell biology

Background:

  • The field of extracellular matrix biology, particularly collagen research, has seen significant advancements since 1978.
  • Early work focused on enzymes involved in collagen biosynthesis.

Purpose of the Study:

  • To review a scientific journey in collagen research, highlighting the discovery and characterization of new nonfibrillar collagen types.
  • To explore the in vivo significance and roles of these collagens in various tissues and disease models.

Main Methods:

  • Molecular biological approaches to define primary structures of novel collagens.
  • Biochemical and cell biological methods to understand collagen properties.
  • Generation and study of mouse models across multiple tissues (adipose, bone, eye, heart, kidney, liver, nerves, skin) and cancer models.

Main Results:

  • Discovery of type XIII collagen (MACIT subgroup) and types XV and XVIII collagens (multiplexin subgroup).
  • Established the roles of these collagens in maintaining extracellular matrix and tissue structure stability (e.g., basement membrane, motor synapse).
  • Demonstrated unexpected, major roles as extrinsic regulators of cell fate and function.

Conclusions:

  • Nonfibrillar collagens contribute significantly to tissue structural integrity.
  • These collagens act as crucial extrinsic regulators influencing cellular behavior.
  • Findings provide a basis for understanding collagen relevance in human diseases, including cancer.