Correspondence to A. S. Weiss, Department of Biochemistry, University of Sydney, NSW 2006, Australia
Biochemistry of tropoelastin
Article first published online: 25 DEC 2001
European Journal of Biochemistry
Volume 258, Issue 1, pages 1–18, November (II) 1998
How to Cite
Vrhovski, B. and Weiss, A. S. (1998), Biochemistry of tropoelastin. European Journal of Biochemistry, 258: 1–18. doi: 10.1046/j.1432-1327.1998.2580001.x
Fax: +61 2 93514726.
Abbreviations. CNBr, cyanogen bromide; EBP, elastin-binding protein; MAGP, microfibril-associated glycoprotein; RER, rough endoplasmic reticulum; SVAS, supravalvular aortic stenosis.
- Issue published online: 25 DEC 2001
- Article first published online: 25 DEC 2001
- (Received 22 June/25 August 1998)
- Cited By
- extracellular matrix;
- lysyl oxidase;
- microfibril-associated glycoprotein;
Elastic fibres are an important component of the extracellular matrix and are made of two major components : the more abundant cross-linked elastic protein elastin and the multi-component microfibrils. The biosynthesis of elastic fibres is a complex process involving the interplay of many diverse proteins and genes with elastin as the major component. Tropoelastin is the soluble precursor of elastin and as such it plays a dominant role in elastogenesis. The expression of tropoelastin is under a complex control mechanism, with many isoforms existing. Numerous other components, including the microfibrillar proteins, the elastin-binding protein and lysyl oxidase, the enzyme which initiates elastin cross-linking, are involved in elastogenesis. Tropoelastin undergoes self-association under physiological conditions in a process referred to as coacervation, and this is thought to be a vital process during elastic fibre formation and in providing elasticity. Although various models explaining the elasticity of elastin have been put forward, only the fibrillar model is based on the coacervation ability of tropoelastin. With the molecular cloning of a number of components of the elastic fibre, the availability of these components is increasing and paves the way for in vitro modelling of complex interactions of the elastic fibre. This review emphasises the biochemistry of tropoelastin and its role in elastic fibre structure and assembly.