The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Biochemistry of tropoelastin
Open accessAbstract
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.
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Indik, Z., Yeh, H., Ornstein-Goldstein, N., Sheppard, P., Anderson, N., Rosenbloom, J. C., Peltonen, L., & Rosenbloom, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5680 · Cited by 334
Davidson, J. M., LuValle, P. A., Zoia, O., Quaglino, D., & Giro, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.345 · Cited by 177 · cited 1×
“It has been proposed that the effect of ascorbate may be due to transcriptional regulation of elastin mRNA levels, although the mechanism is not known [109].”
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Cited by
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Elastic fiber homeostasis requires lysyl oxidase–like 1 protein
Liu, X., Zhao, Y., Gao, J., Pawlyk, B., Starcher, B., Spencer, J. A., Yanagisawa, H., Zuo, J., & Li, T. (2004) · Nature Genetics · doi:10.1038/ng1297 · Cited by 663
Mäki, J. M., Räsänen, J., Tikkanen, H., Sormunen, R., Mäkikallio, K., Kivirikko, K. I., & Soininen, R. (2002) · Circulation · doi:10.1161/01.cir.0000038109.84500.1e · Cited by 482
Elastin, arterial mechanics, and cardiovascular disease
Cocciolone, A. J., Hawes, J. Z., Staiculescu, M. C., Johnson, E. O., Murshed, M., & Wagenseil, J. E. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00087.2018 · Cited by 341
Martin, E. W., & Holehouse, A. S. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20190164 · Cited by 281
Metadata
- Authors
- Vrhovski, B., & Weiss, A. S.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1998-11-15
- Volume
- 258
- Issue
- 1
- Pages
- 1-18
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1969749903
- Cited by
- 544
- References
- 2
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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