STRUCTURE AND COMPOSITION OF THE ELASTIN FIBER IN NORMAL AND PATHOLOGICAL CONDITIONS

Elastin fibres are present in all connective tissues of vertebrates, and are particularly abundant in those undergoing physiological mechanical stress. Elastin, the main component of the fibres, is secreted as soluble tropoelastin molecules, that are crosslinked into insoluble aggregates in the extracellular space. Tropoelastin is highly hydrophobic and is encoded by a single copy gene, localized on chromosome 7 in humans; the primary transcript undergoes alternate splicing giving rise to different tropoelastin molecules, whose distribution and physiological significance are still under investigation. Elastin shows a transient developmental expression, with barely detectable turnover during adult life. In thin sections, elastin fibres appear rather compact and consist of an amorphous material (true elastin) and of longitudinal strips, probably made of various components. By freeze-fracture and negative staining, the elastin fibre has been shown to be made of a loose irregular network of beaded filaments, which can be oriented by stretching. Cytochemical and immunocytochemical approaches have shown that elastin fibres contain proteoglycans as well as sites recognized by antibodies to lysyl oxidase and microfibrillar components. It has been suggested that microfibrils and proteoglycans might have a role in elastin fibrogenesis. Elastin fibres undergo irreversible alterations during aging and in pathological conditions. These alterations consist mainly of accumulation of ions and of abnormal matrix constituents, and/or swelling and disaggregation of the fibre itself.