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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

28.9K
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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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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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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The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

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Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
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Bone Disorders01:29

Bone Disorders

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Aging and its effect on bone remodeling is the most common cause of bone disorders. In young and healthy people, bone deposition and resorption happen at an equal rate to maintain optimal bone health.
Bone deposition is also affected by the levels of sex hormones like estrogen and testosterone that promote osteoblast activity and bone matrix synthesis. When the level of these hormones decreases due to aging, it causes a reduction in bone deposition. As a result, bone resorption by osteoclasts...
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Related Experiment Video

Updated: May 5, 2026

Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates
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Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates

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Collagen genes and brittle bones.

J R Shapiro, D W Rowe

    Annals of Internal Medicine
    |November 1, 1983
    PubMed
    Summary

    Heritable connective tissue diseases stem from extracellular matrix defects. Osteogenesis imperfecta variants show diverse molecular defects in type I collagen synthesis, aiding precise classification.

    Area of Science:

    • Biochemistry
    • Genetics
    • Molecular Biology

    Background:

    • Heritable connective tissue diseases involve defects in extracellular matrix components like collagen.
    • Osteogenesis imperfecta (OI) is a heritable connective tissue disease linked to type I collagen synthesis abnormalities.
    • Clinical OI classification is challenged by genetic heterogeneity and variable expression, necessitating biochemical criteria.

    Purpose of the Study:

    • To define osteogenesis imperfecta variants using precise biochemical criteria.
    • To identify molecular defects in type I collagen synthesis and processing in OI.
    • To correlate specific molecular lesions with clinical OI phenotypes.

    Main Methods:

    • Analysis of type I collagen synthesis and assembly.

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    Laser Capture Microdissection of Mouse Embryonic Cartilage and Bone for Gene Expression Analysis

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  • Quantification of alpha-1(I) and alpha-2(I) collagen chains and their messenger RNA.
  • Investigation of collagen secretion and post-translational modifications.
  • Genetic analysis to identify mutations in collagen genes.

    • Main Results:

    • Identified molecular defects include diminished type I collagen and mRNA formation, abnormal alpha-2(I) synthesis, gene mutations (deletions/insertions), and impaired procollagen secretion.
    • Specific defects like cysteine for glycine substitution in the collagen triple helix were noted.
    • In severe OI, normal type I collagen synthesis and chain ratios suggest unidentified molecular lesions, possibly alpha-1 trimer production.

    Conclusions:

    • Biochemical characterization of type I collagen defects provides precise classification for OI variants.
    • Molecular defects identified offer insights into the pathogenesis of different OI subtypes.
    • Further research is needed to elucidate the molecular basis of severe OI cases with seemingly normal collagen synthesis.