Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 62, Issue 24, Pages 2939-2946Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-005-5482-8
Keywords
trefoil peptides; binding protein; receptor; mucin; vWF domain C; CRP-ductin; TFIZ1; blottin; Brichos domain
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Trefoil factor family (TFF) peptides have many in vivo and in vitro effects on restitution, wound healing, apoptosis, cell motility, adhesion and vectorial ion pumping, amongst others. I-125-TFF peptides bind to cell membranes with classical saturable ability. It would be surprising if there were not TFF-protein interactions that would explain these actions, but to date no convincing TFF-binding partner has been shown which unambiguously takes part in any of these functions. Nevertheless, several TFF-binding proteins exist, including the small intestinal CRP-ductin (muclin), which binds TFF2, and the recently described gastric foveolar proteins TFIZ1 (TFF1-binding) and blottin (TFF2-binding), any of which may yet interact in novel ways to elicit TFF-mediated events. This review describes the expression and, where known, the functions of such proteins.
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