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[9] Elastin: An overview

1987; Academic Press; Linguagem: Inglês

10.1016/0076-6879(87)44178-5

1557-7988

Joel Rosenbloom,

Elasticity and Material Modeling

The elastic properties of many tissues such as the lung, dermis, and large blood vessels are because of the presence of elastic fibers in the extracellular space. These fibers have been shown by biochemical and ultrastructural analysis to be composed of two distinct components, a more abundant amorphous component and the microfibrillar component. Elastin is composed largely of glycine, proline, and other hydrophobic residues and contains multiple lysine-derived cross-links, such as the desmosines, which link the individual polypeptide chains into a rubber-like network. Recent application of recombinant DNA techniques has led to further understanding of the structure of elastin. Analyses of the bovine and human elastin genes have demonstrated that the hydrophobic and crosslinking domains are encoded in separate exons. Elastin can be solubilized only by proteases which have consequently been designated elastases, although these are general, powerful proteases which can hydrolyze numerous proteins.