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https://hdl.handle.net/2440/30726
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Type: | Book chapter |
Title: | Elastic fibre assembly: Macromolecular interactions |
Author: | Mecham, R. Broekelmann, T. Davis, E. Gibson, M. Brown-Augsburger, P. |
Citation: | The molecular pathology of elastic tissues, 1995 / Chadwick, D.J., Goode, J.A. (ed./s), vol.192, pp.172-184 |
Publisher: | J. Wiley |
Issue Date: | 1995 |
Series/Report no.: | CIBA FOUNDATION SYMPOSIA |
ISBN: | 0471957186 9780471957188 |
Editor: | Chadwick, D.J. Goode, J.A. |
Abstract: | To investigate the mechanisms behind elastic fibre assembly, we studied the molecular interactions between elastin and microfibrillar components using solid-phase binding assays. Fibrillin 1, purified from tissue using reductive-saline extraction, showed no binding to microfibril-associated glycoprotein (MAGP) or tropoelastin. MAGP, however, was found to bind specifically to tropoelastin in a divalent-cation independent manner. Antibody inhibition studies indicated that the C-terminus of tropoelastin defined the interactive site with MAGP. MAGP and fibrillin were also substrates for transglutaminase, which may provide an important mechanism for stabilizing microfibrillar structure. In other studies we found that a major cross-linking region in elastin is formed through the association of domains encoded by exons 10, 19 and 25 of tropoelastin and that the three chains are joined together by one desmosine and two lysinonorleucine cross-links. |
Keywords: | Elastic Tissue Animals Humans Elastin Microfilament Proteins Protein-Lysine 6-Oxidase Transglutaminases Contractile Proteins Tropoelastin Extracellular Matrix Proteins Binding Sites Amino Acid Sequence Protein Binding Substrate Specificity Molecular Sequence Data Fibrillin-1 Fibrillins RNA Splicing Factors |
DOI: | 10.1002/9780470514771.ch9 |
Published version: | http://dx.doi.org/10.1002/9780470514771.ch9 |
Appears in Collections: | Aurora harvest 6 Pathology publications |
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