Please use this identifier to cite or link to this item: 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
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
Appears in Collections:Aurora harvest 6
Pathology publications

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