Characterization of the Molecular Interaction between Tropoelastin and DANCE/Fibulin-5

Fibulin-5 is believed to play an important role in the elastic fiber formation. The present experiments were carried out to characterize the molecular interaction between fibulin-5 and tropoelastin. Our data showed that the divalent cations of Ca²⁺, Ba²⁺ and Mg²⁺ significantly enhanced the binding o...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of biochemistry (Tokyo) Vol. 143; no. 5; pp. 633 - 639
Main Authors:	Wachi, Hiroshi, Nonaka, Risa, Sato, Fumiaki, Shibata-Sato, Kayoko, Ishida, Marie, Iketani, Saori, Maeda, Iori, Okamoto, Koji, Urban, Zsolt, Onoue, Satoshi, Seyama, Yoshiyuki
Format:	Journal Article
Language:	English
Published:	England Japanese Biochemical Society 01-05-2008 Oxford University Press
Subjects:	Animals Binding Sites Cattle coacervation DANCE/fibulin-5 extracellular matrix Extracellular Matrix Proteins - chemistry Extracellular Matrix Proteins - metabolism Glycosylation Humans molecular interaction Protein Binding Protein Processing, Post-Translational Protein Structure, Tertiary tropoelastin Tropoelastin - chemistry Tropoelastin - metabolism DANCE/fibulin-5 molecular interaction extracellular matrix coacervation tropoelastin
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Fibulin-5 is believed to play an important role in the elastic fiber formation. The present experiments were carried out to characterize the molecular interaction between fibulin-5 and tropoelastin. Our data showed that the divalent cations of Ca²⁺, Ba²⁺ and Mg²⁺ significantly enhanced the binding of fibulin-5 to tropoelastin. In addition, N-linked glycosylation of fibulin-5 does not require for the binding to tropoelastin. To address the fibulin-5 binding site on tropoelastin constructs containing, exons 2-15 and exons 16-36, of tropoelastin were used. Fibulin-5 binding was significantly reduced to either fragment and also to a mixture of the two fragments. These results suggested that the whole molecule of tropoelastin was required for the interaction with fibulin-5. In co-immunoprecipitation experiments, tropoelastin binding to fibulin-5 was enhanced by an increase of temperature and sodium chloride concentration, conditions that enhance the coacervation of tropoelastin. The binding of tropoelastin fragments to fibulin-5 was directly proportional to their propensity to coacervate. Furthermore, the addition of fibulin-5 to tropoelastin facilitated coacervation. Taken together, the present study shows that fibulin-5 enhances elastic fiber formation in part by improving the self-association properties of tropoelastin.
Bibliography:	ArticleID:mvn014 ark:/67375/HXZ-8XZ6VT7C-2 istex:5DDB24750EB81B5D6B016D1DCFE46EB3267B92DA ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-924X 1756-2651
DOI:	10.1093/jb/mvn014