Trefoil factor family-interacting proteins

被引:35
作者
Otto, W
Thim, L [1 ]
机构
[1] Novo Nordisk AS, Prot Engn, Malov, Denmark
[2] Canc Res UK, Histopathol Unit, London WC2A 3PX, England
关键词
trefoil peptides; binding protein; receptor; mucin; vWF domain C; CRP-ductin; TFIZ1; blottin; Brichos domain;
D O I
10.1007/s00018-005-5482-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2939 / 2946
页数:8
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