Ulfrastructure of Elastin

Fornieri, C.; Baccarani-Contri, M.; Quaglino, Daniela

doi:10.1002/9780470514771.ch3

Cited by 13 publications

(15 citation statements)

References 51 publications

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“…The resulting coacervate, consisting approximately of 60% water and 40% protein material, is presumed to be the preliminary step in the process of aggregation of tropoelastin before cross-linking to give rise to mature elastin. Transmission electron microscopy confirmed that full length tropoelastin molecules at relatively high concentration (more than 1 mg/ml), in physiological solution and at physiological temperatures, form long 5 nm thick filaments with a tendency to aggregate into huge and branched bundles exhibiting structural organization similar to that of natural elastic fibers observed by conventional TEM in thin sections of tissues (Bressan et al, 1983;Pasquali Ronchetti and Fornieri, 1985;Pasquali Ronchetti et al, 1995). Furthermore, rather similar structures have also been observed by applying the same techniques to the repeated hydrophobic tetrapeptide (VPGG)n and pentapeptide (VPGVG)n present in native elastin (Long et al, 1980;Volpin et al, 1976b).…”

Section: Introductionsupporting

confidence: 55%

Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons

et al. 2005

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Section: Introductionsupporting

confidence: 55%

Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons

et al. 2005

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“…The measurement of the specific surface of dried, micronised elastic fibers by radioactive Krypton-gas adsorption (Robert et al 1970) pleaded also in favour of this contention, as well as the flow-calorimetric (Robert et al 1971c) and differential scanning-calorimetric measurements (Bihari-Varga et al 1983. The ultrastructural observations of Pasquali-Ronchetti et al (1995), showing the close proximity of glycosaminglycans to elastin fibers in the aorta, might well be part of the explanation.…”

Section: Physicochemical Properties Of Elastinmentioning

confidence: 89%

Rapid increase in human life expectancy: will it soon be limited by the aging of elastin?

Robert

Fülöp

2008

Biogerontology

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The postponement of the most frequent age-related diseases stimulated speculations of the possibility of "dying of old age". The selective decline of individual physiological functions-aging in spare-parts-indicates however the potential limitation of the life-span by the rapid decline of some of the vital parameters. We explored a possibility of such a limitation of maximal life-span by the age-related alteration of elastin, consisting in Ca-accumulation, lipid deposition and elastolytic degradation. The quantitative evaluation of these processes suggests an approximative upper limit for the elastic properties of the cardio-respiratory system of about 100-120 years, at least, as far as elastin is involved. This process, age-related alterations of elastic fibers, is however not the only one limiting the functional value of the cardiovascular system. Crosslinking of collagen fibers by advanced glycation end-products certainly contributes also to the age-dependent rigidification of the cardiovascular system. Therefore the answer to the initial question, can age-dependent alterations of a single matrix macromolecule be limiting such vital functions as the cardio-respiratory system-is a cautious yes, with however the caveat that other, independent mechanisms, such as the Maillard reaction, can also interfere with and limit further the functional value of such vital physiological functions.

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“…The natural moisturizing factor (NMF), for example, decreases, and a higher water loss of the stratum corneum could be observed in old skin in vivo (48). The NMF is produced via breakdown of filaggrin, which is essential for the regulation of epidermal homeostasis and the barrier function (21). In aged skin in vivo, the filaggrin amount is decreased (49) and in in vitro aged skin equivalents, too ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Elastin is a connective tissue protein that allows many tissues to resume their shape after stretching or contracting (20). An accumulation of amorphous elastin material has been associated with skin ageing (21)(22)(23). In young skin in vivo, a very high density of elastin fibres is shown, which are obviously disrupted in old skin in vivo and in vitro resulting in a loose structure ( Fig.…”

Section: Histological Changes In Aged Skin In Vivo and In Vitromentioning

confidence: 99%

A three‐dimensional skin equivalent reflecting some aspects of in vivo aged skin

Diekmann

Alili

Scholz

et al. 2015

Experimental Dermatology

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Human skin undergoes morphological, biochemical and functional modifications during the ageing process. This study was designed to produce a 3-dimensional (3D) skin equivalent in vitro reflecting some aspects of in vivo aged skin. Reconstructed skin was generated by co-culturing skin fibroblasts and keratinocytes on a collagen-glycosaminoglycan-chitosan scaffold, and ageing was induced by the exposition of fibroblasts to Mitomycin-C (MMC). Recently published data showed that MMC treatment resulted in a drug-induced accelerated senescence (DIAS) in human dermal fibroblast cultures. Next to established ageing markers, histological changes were analysed in comparison with in vivo aged skin. In aged epidermis, the filaggrin expression is reduced in vivo and in vitro. Furthermore, in dermal tissue, the amount of elastin and collagen is lowered in aged skin in vivo as well as after the treatment of 3D skin equivalents with MMC in vitro. Our results show histological signs and some aspects of ageing in a 3D skin equivalent in vitro, which mimics aged skin in vivo.

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Ulfrastructure of Elastin

Cited by 13 publications

References 51 publications

Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons

Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons

Rapid increase in human life expectancy: will it soon be limited by the aging of elastin?

A three‐dimensional skin equivalent reflecting some aspects of in vivo aged skin

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