TREFOIL PEPTIDES - FROM STRUCTURE TO FUNCTION

Authors
Citation
L. Thim, TREFOIL PEPTIDES - FROM STRUCTURE TO FUNCTION, Cellular and molecular life sciences, 53(11-12), 1997, pp. 888-903
Citations number
171
ISSN journal
1420682X
Volume
53
Issue
11-12
Year of publication
1997
Pages
888 - 903
Database
ISI
SICI code
1420-682X(1997)53:11-12<888:TP-FST>2.0.ZU;2-5
Abstract
The unique structure in which six cysteine residues in a sequence of 3 8 or 39 amino acid residues form three disulphide bonds in a 1-5, 2-4 and 3-6 configuration constitutes the basic elements of a trefoil doma in. Today three mammalian trefoil factors (TFF1. TFF2 and TFF3) contai ning one or two trefoil domains are known. Trefoil factors are usually associated with the mucin layer of the gastrointestinal tract. Early studies on trefoil factors concentrated on structure elucidation and s ites of expression in health and disease. whereas studies over the las t 3-5 years have focused on the mechanism of action and the search for specific receptors. This review summarises our present knowledge of t refoil peptide structures, their sites of expression, and their protec tion and repair functions, with a focus on the mechanism by which thes e peptides exert their biological function.