The TRefOIl PePTIde fAmIlY: smAll BUT veRsATIle – fROm ANTI-APOPTOsIs TO NeOPlAsIA IN The dIGesTIve TRAcT

Years ago, during isolation of pancreatic proteins Jorgensen et al. (1) noted a side fraction and thus discovered the pancreatic spasmolytic peptide. Further studies revealed that this peptide, along with two additional ones, formed a small family of cytoprotective peptides, later termed TFF (trefoil factor) family (2) to standarize the previous, somewhat confusing terminology. TFF1, TFF2 and TFF3 share a clover-like folding motif (the trefoil domain) as a hallmark of these peptides in vertebrates (3) but the evolutionary origin goes back to invertebrates (4). While at first, trefoils’ activity was assigned to epithelial cells of the digestive tract and some carcinomas (for a most recent review, see 5) contributions from many research groups extended this setting and actually rather confused than clarified the picture. Several attempts to bring some order to this situation were made and a series of reviews present the current knowledge (e.g. 5-9). Next to their cytoprotective function the TFFs exhibit motogenic, anti-apoptotic, chemotaxic and neoplastic properties, and they participate in immune response, neural development and neusosensory activity. Therefore in this overview, several questions and some possible answers will be approached: a) what is the relation of the 3 family members? b) which expression patterns do they exhibit in normal and pathologic conditions? c) which functional properties are known for the TFFs? d) are cooperating factors known for the TFFs (receptors, binding proteins)? POLSKI PRZEGLĄD CHIRURGICZNY 10.2478/v10035-009-0079-9 2009, 81, 10, 486–490