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Design and Construction of Artificial Extracellular Matrix (aECM) Proteins from Escherichia coli for Skin Tissue Engineering
Published on: June 11, 2015
EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth
S Harumiya1, A Omori, T Sugiura
1Laboratory of Biological Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology.
Abstract:
In order to study the elastin-binding factors in blood, human plasma was applied to an alpha-elastin-Sepharose column. The column-binding fraction contained a 37-kDa protein, which was tentatively named EBP-37. Partial amino acid sequences of EBP-37 were determined. It had collagenous and non-collagenous domains. Homology searches of the sequences revealed that the protein is very similar but not identical to ficolins, transforming growth factor-beta 1 (TGF-beta 1)-binding proteins from porcine uterus membranes. Direct interaction of EBP-37 with elastin was confirmed by demonstrating the binding of the isolated EBP-37 to alpha-elastin on a nitrocellulose membrane using the EBP-37-specific antiserum. The existence of oligomers and multimers crosslinked by disulfide bonds was demonstrated by immunoblot analysis. Possible functions of EBP-37 are discussed.
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