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Related Concept Videos

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...
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...
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...
Pleiotropy01:33

Pleiotropy

Pleiotropy is the phenomenon in which a single gene impacts multiple, seemingly unrelated phenotypic traits. For example, defects in the SOX10 gene cause Waardenburg Syndrome Type 4, or WS4, which can cause defects in pigmentation, hearing impairments, and an absence of intestinal contractions necessary for elimination. This diversity of phenotypes results from the expression pattern of SOX10 in early embryonic and fetal development. SOX10 is found in neural crest cells that form melanocytes,...
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...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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: Jun 13, 2026

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

Polygene network in collagen disease.

Masato Nose1

  • 1Department of Pathogenomics, Ehime University Graduate School of Medicine, and Proteo-Medicine Research Center, Ehime University.

Nihon Rinsho Men'Eki Gakkai Kaishi = Japanese Journal of Clinical Immunology
|May 11, 2010
PubMed
Summary
This summary is machine-generated.

Collagen diseases involve complex lesions resulting from a polygenic system. Multiple gene loci cumulatively influence lesion development, indicating a polygene network contributes to disease variation.

Related Experiment Videos

Last Updated: Jun 13, 2026

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

Area of Science:

  • Rheumatology
  • Genetics
  • Immunology

Background:

  • Collagen diseases, first described in 1942, present with diverse lesions including glomerulonephritis, vasculitis, and arthritis.
  • The underlying causes for the varied presentation of collagen diseases remain debated, with possibilities including diagnostic ambiguity or inherent disease qualities.

Purpose of the Study:

  • To investigate the genetic basis of collagen disease susceptibility using MRL mouse models.
  • To elucidate the role of polygenic inheritance and gene interactions in the development of collagen disease pathology.

Main Methods:

  • Utilized MRL mouse models to study susceptibility loci for collagen disease.
  • Analyzed the cumulative and additive effects of multiple gene loci on lesion development.
  • Examined allelic polymorphism in positional candidate genes.

Main Results:

  • Identified a polygenic system where multiple gene loci contribute cumulatively to lesion development (glomerulonephritis, vasculitis, arthritis, sialoadenitis).
  • Observed an additive and hierarchical effect in lesion development across the mouse models.
  • Found evidence of shared susceptibility loci across different collagen diseases and allelic polymorphisms in candidate genes.

Conclusions:

  • A specific combination of polygenes with allelic polymorphisms forms a network that critically drives lesion development in collagen disease.
  • This polygene network likely explains the regular variations observed in collagen disease presentations.
  • The findings support a polygenic model for collagen disease pathogenesis.