Alimentary TractOverexpression of intestinal trefoil factor in human colon carcinoma cells reduces cellular growth in vitro and in vivo☆,☆☆
Section snippets
Cell culture
All human colon carcinoma cell lines were maintained in a growth medium of a mixture of RPMI 1640 and Ham's F-12 supplemented with 10% heat-inactivated fetal bovine serum. LoVo was obtained from Riken Cell Bank (Tsukuba, Japan). SW837, WiDr, Colo205, and Caco-2 were from Dainihon Seiyaku (Osaka, Japan), and Colo320DM was from Japanese Cancer Research Resources Bank (Osaka, Japan). For 3-dimensional (3-D) collagen gel culture, 0.1% collagen type I gel (Koken, Tokyo, Japan) in the growth medium
Selection of ITF-expressing LoVo clones and effect of ITF overexpression on in vitro culture morphology and growth
An RT-PCR study revealed that 3 (SW837, Colo320DM, and LoVo) of 7 colon carcinoma cell lines examined did not express endogenous ITF (Figure 1A).
Discussion
The current view on the role of trefoil family peptides indicates that these peptides have an important role in promoting repair of damaged mucosa and differentiation of gastrointestinal epithelial cells. Although the precise mechanism by which trefoil peptides promote repair of damaged mucosa remains to be clarified, the migration-stimulatory activities of these peptides are thought to be important because the repair of ulcerated areas involves migration of epithelial cells over the ulcerated
Acknowledgements
The authors thank Drs. H. Maruyama, Nagoya City University, and Y. Nawa, Miyazaki Medical College, for generating anti-ITF antiserum; N. Iwakiri for skillful technical assistance; and Dr. K. Nabeshima for useful discussion and comment.
References (31)
- et al.
Identification of human intestinal trefoil factor. Goblet cell–specific expression of a peptide targeted for apical secretion
J Biol Chem
(1993) - et al.
Oral trefoil peptides protect against ethanol- and indomethacin-induced gastric injury in rats
Gastroenterology
(1996) - et al.
Trefoil peptide gene expression in gastrointestinal epithelial cells in inflammatory bowel disease
Gastroenterology
(1993) - et al.
Growth stimulatory effect of pancreatic spasmolytic polypeptide on cultured colon and breast tumor cells
FEBS Lett
(1989) - et al.
Mitogen-activated protein kinase activation regulates intestinal epithelial differentiation
Gastroenterology
(1999) - et al.
The trefoil peptide family
Annu Rev Physiol
(1996) - et al.
Trefoil factor family domain peptides
Virchows Arch
(1997) - et al.
Identification and characterization of rat intestinal trefoil factor: tissue- and cell-specific member of the trefoil protein family
Proc Natl Acad Sci USA
(1991) - et al.
hP1.B, a human P-domain peptide homologous with rat intestinal trefoil factor, is expressed also in the ulcer-associated cell lineage and the uterus
Proc Natl Acad Sci USA
(1993) - et al.
Molecular cloning of mouse intestinal trefoil factor and its expression during goblet cell changes
Biochem J
(1995)
cDNA cloning of rat pS2 peptide and expression of trefoil peptides in acetic acid-induced colitis
Biochem J
Experimental ulceration leads to sequential expression of spasmolytic polypeptide, intestinal trefoil factor, epidermal growth factor and transforming growth factor alpha mRNAs in rat stomach
J Pathol
Impaired defense of intestinal mucosa in mice lacking intestinal trefoil factor
Science
Trefoil peptides promote epithelial migration through a transforming growth factor β–independent pathway
J Clin Invest
The pS2 gene, mRNA, and protein: a potential marker for human breast cancer
Cancer Cells
Cited by (56)
Odyssey of trefoil factors in cancer: Diagnostic and therapeutic implications
2020, Biochimica et Biophysica Acta - Reviews on CancerCitation Excerpt :Contrary to the above-mentioned studies, a tumor-suppressive function of TFF3 has been reported in CRC and retinoblastoma. Overexpression of TFF3 in CRC and retinoblastoma cells reduced cellular growth in both in vitro and in vivo studies [128] [129]. X-ray structure-based modeling has revealed a high-affinity interaction of TFF3 with the extracellular loop of dimeric forms of CXCR4 and CXCR7.
Growth Factors in the Gastrointestinal Tract
2012, Physiology of the Gastrointestinal Tract, Two Volume SetTFF3 is a normal breast epithelial protein and is associated with differentiated phenotype in early breast cancer but predisposes to invasion and metastasis in advanced disease
2012, American Journal of PathologyCitation Excerpt :These associations are consistent with our finding that TFF3 is a protein of normal breast epithelium and suggest that during the process of carcinogenesis and dedifferentiation TFF3 expression is lost from a subset of tumors. Several functions have been ascribed to TFF3 on the basis of laboratory studies, including inhibition of gastric cancer cell growth,31 stimulation of angiogenesis in human umbilical vein endothelial cell and embryonic chicken cell models,7 and stimulation of invasion of different types of cells.6 Our study was designed to determine whether the profile of expression of TFF3 in vivo supports the hypothesis that TFF3 has these functions in malignant breast tumors.
Growth Factors in the Gastrointestinal Tract
2012, Physiology of the Gastrointestinal TractExpression profiles of MUC mucins and trefoil factor family (TFF) peptides in the intrahepatic biliary system: Physiological distribution and pathological significance
2007, Progress in Histochemistry and Cytochemistry
- ☆
Address requests for reprints to: Masashi Koono, M.D., Second Department of Pathology, Miyazaki Medical College, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan. Fax: (81) 985-85-6003.
- ☆☆
Supported in part by a grant from the Tokyo Biochemical Research Foundation, Japan, a grant from the Kurozumi Medical Foundation, and a grant-in-aid for research project from Miyazaki Medical College.