ArticleCellular and molecular life sciences : CMLS2010
Copper binds the carboxy-terminus of trefoil protein 1 (TFF1), favoring its homodimerization and motogenic activity.
Article in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- IFNγ-dependent silencing of TFF1 duringOpen biology · 2022Article
- TFF1 Induces Aggregation and Reduces Motility ofInternational journal of molecular sciences · 2021Article
- Trefoil Factor Family (TFF) Peptides and Their Diverse Molecular Functions in Mucus Barrier Protection and More: Changing the Paradigm.International journal of molecular sciences · 2020Review
- The Tumor Suppressor TFF1 Occurs in Different Forms and Interacts with Multiple Partners in the Human Gastric Mucus Barrier: Indications for Diverse Protective Functions.International journal of molecular sciences · 2020Article
- Molecular Alterations in the Stomach ofInternational journal of molecular sciences · 2020Article
- TFF1 Promotes EMT-Like Changes through an Auto-Induction Mechanism.International journal of molecular sciences · 2018Article
- Gastric TFF1 Expression from Acute to ChronicFrontiers in cellular and infection microbiology · 2017Article
- Nutritional Aspects of Gastrointestinal Wound Healing.Advances in wound care · 2016Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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