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Content Provider | Springer Nature Link |
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Author | Tosco, Alessandra Monti, Maria Chiara Fontanella, Bianca Montefusco, Sandro D’Andrea, Luca Ziaco, Barbara Baldantoni, Daniela Rio, Marie Christine Marzullo, Liberato |
Copyright Year | 2010 |
Abstract | Trefoil protein 1 (TFF1) is a small secreted protein belonging to the trefoil factor family of proteins, that are present mainly in the gastrointestinal (GI) tract and play pivotal roles as motogenic factors in epithelial restitution, cell motility, and other incompletely characterized biological processes. We previously reported the up-regulation of TFF1 gene in copper deficient rats and the unexpected property of the peptide to selectively bind copper. Following the previous evidence, here we report the characterization of the copper binding site by fluorescence quenching spectroscopy and mass spectrometric analyses. We demonstrate that Cys58 and at least three Glu surrounding residues surrounding it, are essential to efficiently bind copper. Moreover, copper binding promotes the TFF1 homodimerization, thus increasing its motogenic activity in in vitro wound healing assays. Copper levels could then modulate the TFF1 functions in the GI tract, as well as its postulated role in cancer progression and invasion. |
Starting Page | 1943 |
Ending Page | 1955 |
Page Count | 13 |
File Format | |
ISSN | 1420682X |
Journal | Cellular and Molecular Life Sciences |
Volume Number | 67 |
Issue Number | 11 |
e-ISSN | 14209071 |
Language | English |
Publisher | SP Birkhäuser Verlag Basel |
Publisher Date | 2010-03-07 |
Publisher Place | Basel |
Access Restriction | Subscribed |
Subject Keyword | Trefoil factors TFF1 Copper Cell motility Gastrointestinal peptides Copper binding protein Biochemistry Life Sciences Biomedicine general Cell Biology |
Content Type | Text |
Resource Type | Article |
Subject | Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience |
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