Human Intestinal TFF3 Forms Disulfide-Linked Heteromers with the Mucus-Associated FCGBP Protein and Is Released by Hydrogen Sulfide
Proteome
DOI:
10.1021/pr100020c
Publication Date:
2010-04-28T10:08:14Z
AUTHORS (7)
ABSTRACT
TFF3 is a secretory peptide belonging to the trefoil factor family with predicted size of 59 amino acid residues containing seven cysteine residues. It predominantly expressed in intestinal goblet cells where it plays key role mucosal regeneration and repair processes. In course these studies, human colonic was shown exist mainly as high molecular weight heteromer. Purification this heteromer characterization by LC-ESI-MS/MS analysis identified IgG Fc binding protein (FCGBP) disulfide-linked partner TFF3. FCGBP constituent mucus secreted cells. Furthermore, low amounts TFF3/monomer only little TFF3/dimer were detected extracts. Here, we show that forms can be released from purified TFF3-FCGBP complex vitro reduction hydrogen sulfide (H(2)S). Such mechanism would line H(2)S concentrations reported occur lumen colon. Of special note, points reservoir for biologically active peptide. Also proteolytic processing observed which multiple autocatalytic cleavages proposed earlier Johansson et al. (J. Proteome Res. 2009 , 8 3549 - 3557).
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