Dermal collagen fibrils are hybrids of type I and type III collagen molecules

Fleischmajer, Raúl; MacDonald, Ewan; Perlish, Jerome S.; Burgeson, Robert E.; Fisher, Larry W.

doi:10.1016/1047-8477(90)90110-x

Cited by 131 publications

(85 citation statements)

References 20 publications

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“…Type-III collagen is frequently found on the periphery of type-I fibers in the skin and elsewhere (47). To determine whether a negative MRE signal is specifically diagnostic of interactions in type-I collagen fibrils, we monitored the MRE of type-III collagen in acidic and physiological buffers upon heating from 4 C to 60 C. Type-III, like type-I, was triple-helical at 4 C (Fig.…”

Section: Signal Unique To Type-i Collagenmentioning

confidence: 99%

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Drzewiecki

Grisham

Parmar

et al. 2016

Biophysical Journal

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Type-I collagen assembles in a stepwise, hierarchic fashion from the folding of the triple helix to the assembly of fibrils into fibers. The mature assembled fibers are crucial for tissue structure and mechanics, cell interactions, and other functions in vivo. Although triple helix folding can be followed with the use of optical methods such as circular dichroism (CD) spectroscopy, fibrillogenesis is typically measured by alternative methods such as turbidity, rheology, and microscopy. Together, these approaches allow for investigation of the mechanical properties and architectures of collagen-based scaffolds and excised tissues. Herein, we demonstrate that CD spectroscopy, a technique that is used primarily to evaluate the secondary structure of proteins, can also be employed to monitor collagen fibrillogenesis. Type-I collagen suspensions demonstrated a strong, negative ellipticity band between 204 and 210 nm under conditions consistent with fibrillogenesis. Deconvolution of CD spectra before, during, and after fibrillogenesis identified a unique fibril spectrum distinct from triple helix and random coil conformations. The ability to monitor multiple states of collagen simultaneously in one experiment using one modality provides a powerful platform for studying this complex assembly process and the effects of other factors, such as collagenases, on fibrillogenesis and degradation.

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Section: Signal Unique To Type-i Collagenmentioning

confidence: 99%

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Drzewiecki

Grisham

Parmar

et al. 2016

Biophysical Journal

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“…Type I collagen is the most abundant in the human body: it forms more than 90% of bone organic mass and it is the major collagen of tendons, ligaments, cornea and many interstitial connective tissues. It is also the main component of human skin (80%) with collagen type III making up the remainder of skin collagen (15%) [5,9].…”

Section: Collagenmentioning

confidence: 99%

An Overview of the Beneficial Effects of Hydrolysed Collagen as a Nutraceutical on Skin Properties: Scientific Background and Clinical Studies

Sibilla¹,

Godfrey²,

Brewer³

et al. 2015

TONUTRAJ

105

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Skin, the main barrier to the external environment, is subject to deterioration caused by dermatological disorders, environmental conditions and the intrinsic ageing process. This damage to both structure and function may be accelerated by smoking, alcohol consumption and chronic sun exposure (extrinsic components). All these factors may lead to the formation of wrinkles, the appearance of brown spots and skin thickening. One effective strategy to managing the skin ageing process is adopting a healthy nutritional approach to life, maintaining a balanced diet and a good supply of food supplements. This can restore the homeostasis of macro and micronutrients and support the physiology of cells and tissues in the skin. Hydrolysed collagen, an increasingly popular nutraceutical, is composed of low molecular weight small peptides, which are easily digestible, absorbed and distributed in the human body. Numerous clinical trials have now been performed showing the efficacy and benefits of collagen peptides on skin properties, such as hydration, elasticity and reduction of wrinkles. As a result, hydrolysed collagen can be considered an important weapon in the everyday fight against skin ageing.

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“…Immunoelectron microscopic analysis with a monoclonal antibody against the triple helical domain suggested that type III collagen can be present on banded collagen fibrils regardless of fibril diameter (12). The type III collagen molecules interact with the cartilage collagen fibril surface (9), and also with type I collagen fibrils in many tissues (13). Type III collagen has a slightly longer major triple helical domain (1,029 residues) compared with type I collagen (1,014 residues).…”

mentioning

confidence: 99%

Vascular Ehlers-Danlos Syndrome Mutations in Type III Collagen Differently Stall the Triple Helical Folding

Mizuno

Boudko

Engel

et al. 2013

Journal of Biological Chemistry

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Dermal collagen fibrils are hybrids of type I and type III collagen molecules

Cited by 131 publications

References 20 publications

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

An Overview of the Beneficial Effects of Hydrolysed Collagen as a Nutraceutical on Skin Properties: Scientific Background and Clinical Studies

Vascular Ehlers-Danlos Syndrome Mutations in Type III Collagen Differently Stall the Triple Helical Folding

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