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Lookup NU author(s): Professor Bruce Westley, Professor Michael Griffin, Dr Felicity May
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TFF1 is a gastric tumor suppressor that protects gastric epithelial cells from damage but can promote invasive properties of tumor cells. Antibodies were raised against correctly folded TFF1 protein. These showed that the 6.67 kDa secreted trefoil protein is present as an ∼25 kDa complex in normal human gastric mucosa. The TFF1 complex was immunopurified from human gastric mucosa and shown to comprise two proteins joined by a disulfide bond. Both were identified by amino-terminal sequencing and MALDI TOF mass spectrometry. The TFF1 protein partner is a previously unknown protein that we have called TFIZ1 for trefoil factor interactions(z) 1. TFIZ1 is expressed and secreted in normal gastric mucosa. TFIZ1 mRNA was cloned from gastric mucosa and sequenced. TFIZ1 is an 18.31 kDa protein and contains an ∼100 amino acid brichos domain and homology with smart000 19.10, SF_P. This is the first demonstration that a member of the trefoil factor family of proteins is bound covalently to a brichos domain-containing protein. The apparent molecular mass of the TFF1:TFIZ1 heterodimer is remarkably close to the theoretical molecular mass of 24.98 kDa. In conclusion, the heterodimer comprises one molecule each of TFF1 and TFIZ1, and the disulfide bond between TFF1 and TFIZ1 is the most important factor stabilizing the heterodimer. © 2005 American Chemical Society.
Author(s): Westley BR, Griffin S, May FEB
Publication type: Article
Publication status: Published
Journal: Biochemistry
Year: 2005
Volume: 44
Issue: 22
Pages: 7967-7975
ISSN (print): 0006-2960
ISSN (electronic): 1943-295X
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/bi047287n
DOI: 10.1021/bi047287n
PubMed id: 15924415
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