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Published: 10 March 2023

Last updated: 11 March 2023

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1

MAO, WEI, JIE CHEN, TIE-LI PENG, XIAO-FEI YIN, LIAN-ZHOU CHEN, and MIN-HU CHEN. "Role of trefoil factor 1 in gastric cancer and relationship between trefoil factor 1 and gastrokine 1." Oncology Reports 28, no. 4 (July 27, 2012): 1257–62. http://dx.doi.org/10.3892/or.2012.1939.

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2

Tan, X. D., Y. H. Chen, Q. P. Liu, F. Gonzalez-Crussi, and X. L. Liu. "Prostanoids mediate the protective effect of trefoil factor 3 in oxidant-induced intestinal epithelial cell injury: role of cyclooxygenase-2." Journal of Cell Science 113, no. 12 (June 15, 2000): 2149–55. http://dx.doi.org/10.1242/jcs.113.12.2149.

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Trefoil factors are small peptides found in several mammalian tissues including gut, respiratory tract and brain. Their physiological function is not well understood. Among them, trefoil factor 3 (intestinal trefoil factor) is known to be cytoprotective in the gut. However, the molecular mechanism and secondary mediators of trefoil factor 3 action are not known. In the present study, we examined whether the cyclooxygenase pathway is involved in trefoil factor 3 action. We showed that trefoil factor 3 significantly induces the production of prostaglandin E(2) and prostaglandin I(2) in IEC-18 cells (an intestinal epithelial cell line) in a dose dependent manner. Western blot and immunohistochemistry revealed that trefoil factor 3 (2.5 microM) up-regulates the expression of cyclooxygenase-2 but not cyclooxygenase-1 in IEC-18 cells. Treating cells with trefoil factor 3 (10 microM) significantly attenuated reactive oxygen species-induced IEC-18 cell injury. This effect is blocked by NS-398 (10 microM), a selective cyclooxygenase-2 inhibitor. Moreover, we demonstrated that exogenously administered carbacyclin (1 microM, a stable analogue of prostaglandin I(2)) and/or prostaglandin E(2) (1 microM) caused a significant reduction of reactive oxygen species-induced cell injury, mimicking the effect of trefoil factor 3. In summary, our results indicate that trefoil factor 3 activates cyclooxygenase-2 in intestinal epithelium to produce prostaglandin I(2) and prostaglandin E(2), which function as survival factors and mediate the cytoprotective action of trefoil factor 3 against oxidant injury.

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3

Doghmi, S., N. Etique, C. Wendling, L. Thim, C. Tomasetto, and M. C. Rio. "Trefoil Factor 1 (TFF1) function in cancer." European Journal of Cancer Supplements 6, no. 9 (July 2008): 151. http://dx.doi.org/10.1016/s1359-6349(08)71757-9.

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4

Chinery, Rebecca, and Raymond J. Playford. "Combined Intestinal Trefoil Factor and Epidermal Growth Factor is Prophylactic against Indomethacin-Induced Gastric Damage in the Rat." Clinical Science 88, no. 4 (April 1, 1995): 401–3. http://dx.doi.org/10.1042/cs0880401.

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1. The availability of recombinant epidermal growth factor provides a potentially exciting development for the treatment of gastrointestinal ulceration. However, because of its potent mitogenic activity, there is a need for strategies which reduce the dose required. Intestinal trefoil factor stimulates mucosal healing without increasing proliferation. Studies were undertaken to examine the biological effects of rat intestinal trefoil factor and/or human epidermal growth factor upon gastrointestinal epithelial cell functions pertinent to mucosal protection, using two wounding models. 2. The study of epithelial restitution in vitro demonstrated a marked synergistic effect on the rate of migration of the wound edge when intestinal trefoil factor was used in combination with epidermal growth factor. There was no increased cellular proliferation due to the addition of intestinal trefoil factor to the cells when given alone, or to the stimulatory effect of cells treated with epidermal growth factor. In the rat model of gastric ulceration, the presence of both epidermal growth factor and intestinal trefoil factor protected against the development of indomethacin-induced gastric lesions. 3. We conclude that combination therapy of epidermal growth factor with intestinal trefoil factor could provide a more potent, safer approach to the treatment of human gastrointestinal ulceration.

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5

Zhu, Ya-Qin, and Xiao-Di Tan. "TFF3 modulates NF-κB and a novel negative regulatory molecule of NF-κB in intestinal epithelial cells via a mechanism distinct from TNF-α." American Journal of Physiology-Cell Physiology 289, no. 5 (November 2005): C1085—C1093. http://dx.doi.org/10.1152/ajpcell.00185.2005.

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Trefoil factor 3 (intestinal trefoil factor) is a cytoprotective factor in the gut. Herein we compared the effect of trefoil factor 3 with tumor necrosis factor-α on 1) activation of NF-κB in intestinal epithelial cells; 2) expression of Twist protein (a molecule essential for downregulation of nuclear factor-κB activity in vivo); and 3) production of interleukin-8. We showed that Twist protein is constitutively expressed in intestinal epithelial cells. Tumor necrosis factor-α induced persistent degradation of Twist protein in intestinal epithelial cells via a signaling pathway linked to proteasome, which was associated with prolonged activation of NF-κB. In contrast to tumor necrosis factor, trefoil factor 3 triggered transient activation of NF-κB and prolonged upregulation of Twist protein in intestinal epithelial cells via an ERK kinase-mediated pathway. Unlike tumor necrosis factor-α, transient activation of NF-κB by trefoil factor 3 is not associated with induction of IL-8 in cells. To examine the role of Twist protein in intestinal epithelial cells, we silenced the Twist expression by siRNA. Our data showed that trefoil factor 3 induced interleukin-8 production after silencing Twist in intestinal epithelial cells. Together, these observations indicated that 1) trefoil factor 3 triggers a diverse signal from tumor necrosis factor-α on the activation of NF-κB and its associated molecules in intestinal epithelial cells; and 2) trefoil factor 3-induced Twist protein plays an important role in the modulation of inflammatory cytokine production in intestinal epithelial cells.

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6

Matsubara, Daisuke, Taichiro Yoshimoto, Manabu Soda, Yusuke Amano, Atsushi Kihara, Toko Funaki, Takeshi Ito, et al. "Reciprocal expression of trefoil factor‐1 and thyroid transcription factor‐1 in lung adenocarcinomas." Cancer Science 111, no. 6 (April 30, 2020): 2183–95. http://dx.doi.org/10.1111/cas.14403.

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7

Huang, You-Guang, Yun-Feng Li, Bao-Long Pan, Li-Ping Wang, Yong Zhang, Wen-Hui Lee, and Yun Zhang. "Trefoil factor 1 gene alternations and expression in colorectal carcinomas." Tumori Journal 99, no. 6 (November 2013): 702–7. http://dx.doi.org/10.1177/030089161309900610.

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8

Esposito, Roberta, Sandro Montefusco, Piera Ferro, Maria Chiara Monti, Daniela Baldantoni, Alessandra Tosco, and Liberato Marzullo. "Trefoil Factor 1 is involved in gastric cell copper homeostasis." International Journal of Biochemistry & Cell Biology 59 (February 2015): 30–40. http://dx.doi.org/10.1016/j.biocel.2014.11.014.

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9

Amiry, Naeem, Xiangjun Kong, Nethaji Muniraj, Nagarajan Kannan, Prudence M. Grandison, Juan Lin, Yulu Yang, et al. "Trefoil Factor-1 (TFF1) Enhances Oncogenicity of Mammary Carcinoma Cells." Endocrinology 150, no. 10 (July 9, 2009): 4473–83. http://dx.doi.org/10.1210/en.2009-0066.

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Abstract The functional role of autocrine trefoil factor-1 (TFF1) in mammary carcinoma has not been previously elucidated. Herein, we demonstrate that forced expression of TFF1 in mammary carcinoma cells resulted in increased total cell number as a consequence of increased cell proliferation and survival. Forced expression of TFF1 enhanced anchorage-independent growth and promoted scattered cell morphology with increased cell migration and invasion. Moreover, forced expression of TFF1 increased tumor size in xenograft models. Conversely, RNA interference-mediated depletion of TFF1 in mammary carcinoma cells significantly reduced anchorage-independent growth and migration. Furthermore, neutralization of secreted TFF1 protein by polyclonal antibody decreased mammary carcinoma cell viability in vitro and resulted in regression of mammary carcinoma xenografts. We have therefore demonstrated that TFF1 possesses oncogenic functions in mammary carcinoma cells. Functional antagonism of TFF1 can therefore be considered as a novel therapeutic strategy for mammary carcinoma.

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10

Mercatali, Laura, Yibin Kang, Michele Zanoni, Chiara Liverani, Elisa Carretta, Marianna Ricci, Nada Riva, et al. "Trefoil factor 1 as a predictive factor of bone metastases in breast cancer." Journal of Clinical Oncology 31, no. 15_suppl (May 20, 2013): 11022. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.11022.

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11022 Background: Patients with breast cancer frequently develop bone metastases, which are responsible for high morbidity and reduced quality of life. The early identification of patients with a high probability of relapsing in this site could be used to select candidates for tailored therapy with bone-specific drugs such as bisphosphonates or RANK-L inhibitors. We aimed to identify a pattern of tissue markers in primary breast cancer that could predict bone metastatization. Methods: Expression of different markers was retrospectively analyzed in frozen breast cancer tissue samples from 90 patients comprising 30 cases with no evidence of disease (NEDP), 30 with bone metastases (BMP) and 30 with visceral metastases (VMP). Eight transcripts were analyzed by Quantitative Real time PCR: trefoil factor 1(TFF1), bone sialoprotein (IBSP), heparanase (HPSE), secreted protein acidic and rich in cysteine (SPARC), connective tissue growth factoe (CTGF), B2 microglobulin (B2M) and receptor activator of Nf-kB (RANK). Immunohistochemistry of TFF1 was performed on a part of the case series. Results: Marker expression analysis in the 3 different subgroups showed at least twofold higher median values of all markers in NEDP and VMP subgroups than in BMP. In particular, TFF1, B2M and CXCR4 levels showed statistically significant values. Median TFF1 value in BMP patients was 430.64 compared to 115.83 and 32.79 in VMP and NEDP, respectively (p=0.0043). Considering markers as dichotomous variables, TFF1 expression in BMP reached 59% compared to 21% and 23 % in NEDP and VMP, respectively (p=0.0022). Univariate analysis confirmed that TFF1 predicted the relapse and also the site of relapse. Immunohistochemistry data on TFF1 revealed that this protein was expressed only by cancer cells. Furthermore, the accuracy of the marker did not change at RNA or protein level, thus excluding a post transcriptional control of the RNA. Conclusions: In this preliminary study we identified a gene expression pattern in primary breast cancer that can identify patients destined to relapse to the bone. In particular, TFF1 would seem to be a suitable marker for bone metastatization and a possible target for the development of new drugs.

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11

Wunsch, Michael J., Alexandra H. Baker, David W. Kalb, and Gary C. Bergstrom. "Characterization of Fusarium oxysporum f. sp. loti Forma Specialis nov., a Monophyletic Pathogen Causing Vascular Wilt of Birdsfoot Trefoil." Plant Disease 93, no. 1 (January 2009): 58–66. http://dx.doi.org/10.1094/pdis-93-1-0058.

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Fusarium wilt, a vascular wilt caused by Fusarium oxysporum, has been a serious problem for birdsfoot trefoil (Lotus corniculatus) production in parts of New York and Vermont since the 1970s, causing wilt, severe root necrosis, and rapid plant death. Analysis of F. oxysporum isolates causing this disease indicated that the pathogen has a unique host range relative to previously designated F. oxysporum formae speciales and is monophyletic. Pathogenic isolates from New York and Vermont caused severe vascular wilt of trefoil and moderate vascular wilt of pea but no disease on alfalfa, red clover, soybean, or dry bean. The host range of trefoil isolates was distinct from F. oxysporum isolates pathogenic to other legumes. F. oxysporum isolates pathogenic to trefoil belonged to a single vegetative compatibility group separate from nonpathogenic isolates and shared identical mitochondrial small subunit rDNA, translation elongation factor 1-alpha, and nuclear rDNA intergenic spacer haplotypes. Phylogenetic analysis of the concatenated sequence data assigned isolates pathogenic to trefoil to a single, well-supported clade distinct from other pathogenic F. oxysporum. We propose designating the fungus Fusarium oxysporum Schlechtendahl emend. Snyder & Hansen f. sp. loti forma specialis nova.

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12

McBerry, Cortez, Charlotte E. Egan, Reena Rani, Yanfen Yang, David Wu, Nicholas Boespflug, Louis Boon, et al. "Trefoil Factor 2 Negatively Regulates Type 1 Immunity against Toxoplasma gondii." Journal of Immunology 189, no. 6 (August 15, 2012): 3078–84. http://dx.doi.org/10.4049/jimmunol.1103374.

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13

Yamaguchi, Junpei, Yukihiro Yokoyama, Toshio Kokuryo, Tomoki Ebata, Atsushi Enomoto, and Masato Nagino. "Trefoil factor 1 inhibits epithelial-mesenchymal transition of pancreatic intraepithelial neoplasm." Journal of Clinical Investigation 128, no. 8 (July 23, 2018): 3619–29. http://dx.doi.org/10.1172/jci97755.

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14

Kannan, Rama, Catherine Tomasetto, Adrien Staub, Carine Bossenmeyer-Pourié, Lars Thim, Per F. Nielsen, and Marie-Christine Rio. "Human pS2/Trefoil Factor 1: Production and Characterization in Pichia pastoris." Protein Expression and Purification 21, no. 1 (February 2001): 92–98. http://dx.doi.org/10.1006/prep.2000.1352.

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15

Torres, Luis-Fernando, Sherif M. Karam, Corinne Wendling, Marie-Pierre Chenard, David Kershenobich, Catherine Tomasetto, and Marie-Christine Rio. "TreFoil Factor 1 (TFF1/pS2) Deficiency Activates the Unfolded Protein Response." Molecular Medicine 8, no. 5 (May 2002): 273–82. http://dx.doi.org/10.1007/bf03402153.

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16

Soutto, Mohammed, Zheng Chen, Ahmed M. Katsha, Judith Romero-Gallo, Uma S. Krishna, M. Blanca Piazuelo, M. Kay Washington, Richard M. Peek, Abbes Belkhiri, and Wael M. El-Rifai. "Trefoil factor 1 expression suppressesHelicobacter pylori-induced inflammation in gastric carcinogenesis." Cancer 121, no. 24 (September 15, 2015): 4348–58. http://dx.doi.org/10.1002/cncr.29644.

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17

Ogata, H., and D. K. Podolsky. "Trefoil peptide expression and secretion is regulated by neuropeptides and acetylcholine." American Journal of Physiology-Gastrointestinal and Liver Physiology 273, no. 2 (August 1, 1997): G348—G354. http://dx.doi.org/10.1152/ajpgi.1997.273.2.g348.

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Trefoil peptides are a family of small proteins expressed by goblet cells that are secreted onto the apical gastrointestinal mucosal surface, where they are present in high concentrations. These peptides appear to both protect the epithelium and promote healing after injury. However, the factors regulating the expression and secretion of these proteins contributing to mucosal defense have not been characterized. To determine the mechanisms controlling production of trefoil peptides, the human colon cancer-derived model cell line HT-29 was exposed to a variety of potential secretagogues. Expression and secretion of human intestinal trefoil factor (hITF) as well as the intestinal apomucin MUC2 were assessed by Northern and Western blot analysis. Carbachol, an analog of acetylcholine, and the neuroendocrine peptides somatostatin and vasoactive intestinal polypeptide (VIP) stimulated increased expression of hITF mRNA within 5 min. These same factors stimulated parallel secretion of the hITF peptide, with maximal stimulation observed at concentrations ranging from 10(-6) M (carbachol and somatostatin) to 10(-7) M (VIP). Expression and secretion of hITF in response to carbachol, VIP, and somatostatin was independent of production of apomucin. hITF was not regulated by other neuroendocrine transmitters including histamine and substance P. Similarly, hITF expression and secretion was not modulated by peptide growth factors (epidermal growth factor, transforming growth factor-beta, and keratinocyte growth factor), cytokines [interleukin (IL)-1 beta, IL-2, IL-7, and IL-11], or arachidonic acid metabolites (prostaglandin E1/E2 and leukotriene B4). In conclusion, trefoil peptides appear to be integrated into mechanisms of mucosal defense and repair through the enteric neuroendocrine system and independent of the classical mucosal immune cytokine network.

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18

Lien, Gi-Shih, Anatoly Leytin, Anli Chen, Noam Harpaz, Mark W. Babyatsky, and Steven h. Itzkowitz. "Ubiquitous expression of intestinal trefoil factor (ITF) in Barrett's esophagus." Gastroenterology 118, no. 4 (April 2000): A36. http://dx.doi.org/10.1016/s0016-5085(00)82213-1.

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19

Furuta, Glenn T., Jerrold R. Turner, Cormac T. Taylor, Robert M. Hershberg, Katrina Comerford, Sailaja Narravula, Daniel K. Podolsky, and Sean P. Colgan. "Hypoxia-Inducible Factor 1–Dependent Induction of Intestinal Trefoil Factor Protects Barrier Function during Hypoxia." Journal of Experimental Medicine 193, no. 9 (April 30, 2001): 1027–34. http://dx.doi.org/10.1084/jem.193.9.1027.

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Mucosal organs such as the intestine are supported by a rich and complex underlying vasculature. For this reason, the intestine, and particularly barrier-protective epithelial cells, are susceptible to damage related to diminished blood flow and concomitant tissue hypoxia. We sought to identify compensatory mechanisms that protect epithelial barrier during episodes of intestinal hypoxia. Initial studies examining T84 colonic epithelial cells revealed that barrier function is uniquely resistant to changes elicited by hypoxia. A search for intestinal-specific, barrier-protective factors revealed that the human intestinal trefoil factor (ITF) gene promoter bears a previously unappreciated binding site for hypoxia-inducible factor (HIF)-1. Hypoxia resulted in parallel induction of ITF mRNA and protein. Electrophoretic mobility shift assay analysis using ITF-specific, HIF-1 consensus motifs resulted in a hypoxia-inducible DNA binding activity, and loading cells with antisense oligonucleotides directed against the α chain of HIF-1 resulted in a loss of ITF hypoxia inducibility. Moreover, addition of anti-ITF antibody resulted in a loss of barrier function in epithelial cells exposed to hypoxia, and the addition of recombinant human ITF to vascular endothelial cells partially protected endothelial cells from hypoxia-elicited barrier disruption. Extensions of these studies in vivo revealed prominent hypoxia-elicited increases in intestinal permeability in ITF null mice. HIF-1–dependent induction of ITF may provide an adaptive link for maintenance of barrier function during hypoxia.

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20

Braga Emidio, Nayara, Hayeon Baik, David Lee, René Stürmer, Jörn Heuer, Alysha G. Elliott, Mark A. T. Blaskovich, et al. "Correction: Chemical synthesis of human trefoil factor 1 (TFF1) and its homodimer provides novel insights into their mechanisms of action." Chemical Communications 56, no. 51 (2020): 7049. http://dx.doi.org/10.1039/d0cc90250k.

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Correction for ‘Chemical synthesis of human trefoil factor 1 (TFF1) and its homodimer provides novel insights into their mechanisms of action’ by Nayara Braga Emidio et al., Chem. Commun., 2020, DOI: 10.1039/D0CC02321C.

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21

Park, Won Sang, Ro Ra Oh, Jik Young Park, Jong Heun Lee, Min Sun Shin, Hong Sug Kim, Hun Kyung Lee, et al. "Somatic mutations of the trefoil factor family 1 gene in gastric cancer." Gastroenterology 119, no. 3 (September 2000): 691–98. http://dx.doi.org/10.1053/gast.2000.16483.

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22

Chourkova, B. "Morphological composition and rate of growth of the sward from birdsfoot trefoil (Lotus corniculatus L.) treated with organic fertilizer alfalfa blend." Biotehnologija u stocarstvu 27, no. 3 (2011): 1287–93. http://dx.doi.org/10.2298/bah1103287c.

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The study was conducted during the 2007-2009 period in the experimental field of IMSA-Troyan. The aim was to determine the influence of the organic product alfalfa blend on the rate of growth of the sward from the birdsfoot trefoil. The organic preparation alfalfa blend was tested on a candidate variety of birdsfoot trefoil with the following factors and fertilizing rates: Factor A - dates of harvesting: ?1 - budding stage, ?2 - early flowering stage, Factor ? - rates of fertilizing with leaf fertilizers: ?0 - no fertilizing, ?1 - leaf fertilizing at the dose of 1 l/ha, ?2 - leaf fertilizing at the dose of 2 l/ha, ?3 - leaf fertilizing at the dose of 3 l/ha. The birdsfoot trefoil treatment with an organic fertilizer as a cultivar factor exerted an effect on the height and morphological composition of the sward. As in the three years of study and on average over a significant influence on plant height was the stage of harvest than the dose of organic fertilizer. In flowering stage and during the three experimental years and three doses of the plants are higher than those harvested in the phase budding treated with the same doses. The strong positive correlation established between the height and the leaves (r = 0.5734) and low positive correlation between the leaves and the generative organs (r = 0.3370); between dry mass yield and the height (r = 0.2740) and the stems.

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23

Barrera Roa, Jose, Gabiela Sanchez Tortolero, and Emanuele Gonzalez. "Trefoil factor 3 (TFF3) expression is regulated by insulin and glucose." Journal of Health Sciences 3, no. 1 (April 15, 2013): 1–12. http://dx.doi.org/10.17532/jhsci.2013.26.

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Introduction: Trefoil factors are effector molecules in gastrointestinal tract physiology. They are classified into three groups: the gastric peptides (TFF1), spasmolytic peptide (TFF2) and intestinal trefoil factor (TFF3). Previous studies have shown that trefoil factors are located and expressed in human endocrine pancreas suggesting that TFF3 play a role in: a) pancreatic cells migration, b) β-cell mitosis, and c) pancreatic cells regeneration. We speculated that the presence of TFF3 in pancreas, could be associated to a possible regulation mechanism by insulin and glucose. To date, there are not reports whether the unbalance in carbohydrate metabolism observed in diabetes could affect the production or expression of TFF3.Methods: We determined the TFF3 levels and expression by immunoassay (ELISA) and semi-quantitative RT-PCR technique respectively, of intestinal epithelial cells (HT-29) treated with glucose and insulin. Also,Real Time-PCR (RTq-PCR) was done.Results: Increasing concentrations of glucose improved TFF3 expression and these levels were further elevated after insulin treatment. Insulin treatment also led to the up-regulation of human sodium/glucose transporter 1 (hSGLT1), which further increases intracellular glucose levels. Finally, we investigated theTFF3 levels in serum of diabetes mellitus type 1 (T1DM) and healthy patients. Here we shown that serum TFF3 levels were down-regulated in T1DM and this levels were up-regulated after insulin treatment. Also, the TFF3 levels of healthy donors were up-regulated 2 h after breakfast.Conclusion: Our fi ndings suggest for the fi rst time that insulin signaling is important for TFF3 optimal expression in serum and intestinal epithelial cells.

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24

Estívariz, C. F., L. H. Gu, C. R. Jonas, C. L. Farrell, and T. R. Ziegler. "O.01 Regulation of intestinal trefoil factor mRNA by nutritional status and keratinocyte growth factor." Clinical Nutrition 17 (August 1998): 1. http://dx.doi.org/10.1016/s0261-5614(98)80069-1.

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25

Ren, Jian-Lin. "Relationship between trefoil factor 1 expression and gastric mucosa injuries and gastric cancer." World Journal of Gastroenterology 11, no. 17 (2005): 2674. http://dx.doi.org/10.3748/wjg.v11.i17.2674.

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26

Flores, Ana R., Marisa Castro, Alexandra Rêma, João R. Mesquita, Marian Taulescu, Fátima Gärtner, Fernanda Seixas, and Irina Amorim. "Immunoexpression of Trefoil Factor 1 in Non-Neoplastic and Neoplastic Canine Gastric Tissues." Animals 11, no. 10 (September 29, 2021): 2855. http://dx.doi.org/10.3390/ani11102855.

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TFF1 expression is markedly reduced in human GCs, suggesting that TFF1 is a tumor suppressor for human gastric cancer. The present study evaluated the expression and distribution pattern of TFF1 in paraffin-embedded canine gastric tissue samples, including normal mucosa (n = 3), polyps (n = 8), carcinomas (n = 31) and their adjacent non-neoplastic mucosa (n = 30), neoplastic emboli (n = 14), and metastatic lesions (n = 9), by immunohistochemistry (IHC). All normal gastric tissues expressed TFF1 in the superficial foveolar epithelium and mucopeptic cells of the neck region. Most gastric polyps (GPs) displayed immunoreactivity for TFF1 in >75% of the epithelial component. In GCs, the expression of TFF1 was found reduced in 74.2% of the cases. The level of TFF1 expression had a decreased tendency from normal gastric mucosa to GPs and GCs (p < 0.05). No significant differences in the expression of TFF1 were found in GCs, according to age, sex, histological type based on World Health Organization (WHO) and Lauren classification, tumor location, depth of tumor invasion, presence of neoplastic emboli or metastatic lesions. The median survival time of GC patients with preserved and reduced TFF1 immunoexpression were 30 and 12 days, respectively. Kaplan–Meier analysis revealed no significant survival differences between the two groups (p > 0.05). These findings suggest that TFF1 protein may play a role in canine gastric carcinogenesis, and further studies are necessary to define its usefulness as a prognostic indicator in canine gastric carcinoma.

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27

Park, Won Sang, Young Sil Kim, Nam Jin Yoo, Cho Hyun Park, Jin Young Yoo, Youn Soo Lee, and Jung Young Lee. "Expression Pattern of the Trefoil Factor Family 1 in Gastric Adenoma and Carcinoma." Journal of the Korean Gastric Cancer Association 1, no. 1 (2001): 4. http://dx.doi.org/10.5230/jkgca.2001.1.1.4.

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28

Lebherz-Eichinger, Diana, Bianca Tudor, Hendrik J. Ankersmit, Thomas Reiter, Martin Haas, Franziska Roth-Walter, Claus G. Krenn, and Georg A. Roth. "Trefoil Factor 1 Excretion Is Increased in Early Stages of Chronic Kidney Disease." PLOS ONE 10, no. 9 (September 21, 2015): e0138312. http://dx.doi.org/10.1371/journal.pone.0138312.

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29

Lai, Ming-Yu, Xiao-Xia Liao, Yao-Guang Lin, Zhi-Hai Liang, Hui Chen, Su-Yan Li, Dun-Ke Jiang, and Ying Liu. "Expression of trefoil factor 1 in gastric cancer and its correlation with neovascularization." World Chinese Journal of Digestology 17, no. 9 (2009): 931. http://dx.doi.org/10.11569/wcjd.v17.i9.931.

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30

Jensen, Pia, Michel Heimberg, Angelique D. Ducray, Hans R. Widmer, and Morten Meyer. "Expression of Trefoil Factor 1 in the Developing and Adult Rat Ventral Mesencephalon." PLoS ONE 8, no. 10 (October 7, 2013): e76592. http://dx.doi.org/10.1371/journal.pone.0076592.

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31

Arumugam, Thiruvengadam, Will Brandt, Vijaya Ramachandran, Tood T. Moore, Huamin Wang, Felicity E. May, Bruce R. Westley, Rosa F. Hwang, and Craig D. Logsdon. "Trefoil Factor 1 Stimulates Both Pancreatic Cancer and Stellate Cells and Increases Metastasis." Pancreas 40, no. 6 (August 2011): 815–22. http://dx.doi.org/10.1097/mpa.0b013e31821f6927.

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32

Masui, Fujiko, Keiko Kurosaki, Takao Mori, and Manabu Matsuda. "Persistent trefoil factor 1 expression imprinted on mouse vaginal epithelium by neonatal estrogenization." Cell and Tissue Research 323, no. 1 (August 30, 2005): 167–75. http://dx.doi.org/10.1007/s00441-005-0049-4.

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33

Beckler, Andrew D., James K. Roche, Jeffrey C. Harper, Gina Petroni, Henry F. Frierson, Christopher A. Moskaluk, Wa'el El-Rifai, and Steven M. Powell. "Decreased abundance of trefoil factor 1 transcript in the majority of gastric carcinomas." Cancer 98, no. 10 (October 30, 2003): 2184–91. http://dx.doi.org/10.1002/cncr.11789.

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34

Wu, Ping, Hai-Shui Shi, Yi-Xiao Luo, Ruo-Xi Zhang, Jia-Li Li, Jie Shi, Lin Lu, and Wei-Li Zhu. "Neuropeptide trefoil factor 3 attenuates naloxone-precipitated withdrawal in morphine-dependent mice." Psychopharmacology 231, no. 24 (May 14, 2014): 4659–68. http://dx.doi.org/10.1007/s00213-014-3615-1.

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35

Yeo, Dahee, Su-Jung Hwang, Ye-Seul Song, and Hyo-Jong Lee. "Humulene Inhibits Acute Gastric Mucosal Injury by Enhancing Mucosal Integrity." Antioxidants 10, no. 5 (May 11, 2021): 761. http://dx.doi.org/10.3390/antiox10050761.

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This study was designed to determine whether α-humulene, a major constituent in many plants used in fragrances, has a protective role against gastric injury in vivo and in vitro. A rat model of hydrochloric acid (HCl)/ethanol-induced gastritis and human mast cells (HMC-1) were used to investigate the mucosal protective effect of α-humulene. α-Humulene significantly inhibited gastric lesions in HCl/ethanol-induced acute gastritis and decreased gastric acid secretion pyloric ligation-induced gastric ulcers in vivo. In addition, α-humulene reduced the amount of reactive oxygen species and malondialdehyde through upregulation of prostaglandin E2 (PGE2) and superoxide dismutase (SOD). In HMC-1 cells, α-humulene decreased intracellular calcium and increased intracellular cyclic adenosine monophosphate (cAMP) levels, resulting in low histamine levels. α-Humulene also reduced the expression levels of cytokine genes such as interleukin (IL)-1β, IL-6, tumor necrosis factor (TNF) by downregulating nuclear factor-κB (NF-κB) nuclear translocation. Finally, α-humulene upregulated the expression levels of mucin 5AC (Muc5ac), Muc6, trefoil factor 1 (Tff1), trefoil factor 2 (Tff2), and polymeric immunoglobulin receptor (pigr). α-Humulene may attenuate HCl/ethanol-induced gastritis by inhibiting histamine release and NF-κB activation and stimulating antioxidants and mucosal protective factors, particularly Muc5ac and Muc6. Therefore, these data suggest that α-humulene is a potential drug candidate for the treatment of stress-induced or alcoholic gastritis.

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Karam, S. M. "Trefoil factor 1 is required for the commitment programme of mouse oxyntic epithelial progenitors." Gut 53, no. 10 (October 1, 2004): 1408–15. http://dx.doi.org/10.1136/gut.2003.031963.

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Sun, Jian-Min, Virginia A. Spencer, Lin Li, Hou Yu Chen, Jenny Yu, and James R. Davie. "Estrogen regulation of trefoil factor 1 expression by estrogen receptor α and Sp proteins." Experimental Cell Research 302, no. 1 (January 2005): 96–107. http://dx.doi.org/10.1016/j.yexcr.2004.08.015.

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Sasaki, Motoko, Hiroko Ikeda, Shusaku Ohira, Akira Ishikawa, and Yasuni Nakanuma. "Expression of trefoil factor family 1, 2, and 3 peptide is augmented in hepatolithiasis." Peptides 25, no. 5 (May 2004): 763–70. http://dx.doi.org/10.1016/j.peptides.2003.12.023.

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Jensen, P., A. D. Ducray, H. R. Widmer, and M. Meyer. "Effects of Forskolin on Trefoil factor 1 expression in cultured ventral mesencephalic dopaminergic neurons." Neuroscience 310 (December 2015): 699–708. http://dx.doi.org/10.1016/j.neuroscience.2015.10.010.

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Bougen, N. M., N. Amiry, Y. Yuan, X. J. Kong, V. Pandey, L. J. P. Vidal, J. K. Perry, T. Zhu, and P. E. Lobie. "Trefoil factor 1 suppression of E-CADHERIN enhances prostate carcinoma cell invasiveness and metastasis." Cancer Letters 332, no. 1 (May 2013): 19–29. http://dx.doi.org/10.1016/j.canlet.2012.12.012.

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Yio, Xianyang, Matthew Diamond, Jie–Yu Zhang, Harel Weinstein, Lu–Hai Wang, Lawrence Werther, and Steven Itzkowitz. "Trefoil Factor Family-1 Mutations Enhance Gastric Cancer Cell Invasion Through Distinct Signaling Pathways." Gastroenterology 130, no. 6 (May 2006): 1696–706. http://dx.doi.org/10.1053/j.gastro.2006.01.040.

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Sasaki, Motoko, Koichi Tsuneyama, and Yasuni Nakanuma. "Aberrant Expression of Trefoil Factor Family 1 in Biliary Epithelium in Hepatolithiasis and Cholangiocarcinoma." Laboratory Investigation 83, no. 10 (October 2003): 1403–13. http://dx.doi.org/10.1097/01.lab.0000092230.59485.9e.

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Khan, Protiti, Bojan Drobic, Beatriz Pérez-Cadahía, Shannon Healy, Shihua He, and James R. Davie. "Mitogen- and Stress-Activated Protein Kinases 1 and 2 Are Required for Maximal Trefoil Factor 1 Induction." PLoS ONE 8, no. 5 (May 13, 2013): e63189. http://dx.doi.org/10.1371/journal.pone.0063189.

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Christine, Rivat, Rodrigues Sylvie, Bruyneel Erik, Piétu Geneviève, Robert Amélie, Redeuilh Gérard, Bracke Marc, Gespach Christian, and Attoub Samir. "Implication of STAT3 Signaling in Human Colonic Cancer Cells during Intestinal Trefoil Factor 3 (TFF3) – and Vascular Endothelial Growth Factor–Mediated Cellular Invasion and Tumor Growth." Cancer Research 65, no. 1 (January 1, 2005): 195–202. http://dx.doi.org/10.1158/0008-5472.195.65.1.

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Abstract Signal transducer and activator of transcription (STAT) 3 is overexpressed or activated in most types of human tumors and has been classified as an oncogene. In the present study, we investigated the contribution of the STAT3s to the proinvasive activity of trefoil factors (TFF) and vascular endothelial growth factor (VEGF) in human colorectal cancer cells HCT8/S11 expressing VEGF receptors. Both intestinal trefoil peptide (TFF3) and VEGF, but not pS2 (TFF1), activate STAT3 signaling through Tyr705 phosphorylation of both STAT3α and STAT3β isoforms. Blockade of STAT3 signaling by STAT3β, depletion of the STAT3α/β isoforms by RNA interference, and pharmacologic inhibition of STAT3α/β phosphorylation by cucurbitacin or STAT3 inhibitory peptide abrogates TFF- and VEGF-induced cellular invasion and reduces the growth of HCT8/S11 tumor xenografts in athymic mice. Differential gene expression analysis using DNA microarrays revealed that overexpression of STAT3β down-regulates the VEGF receptors Flt-1, neuropilins 1 and 2, and the inhibitor of DNA binding/differentiation (Id-2) gene product involved in the neoplastic transformation. Taken together, our data suggest that TFF3 and the essential tumor angiogenesis regulator VEGF165 exert potent proinvasive activity through STAT3 signaling in human colorectal cancer cells. We also validate new therapeutic strategies targeting STAT3 signaling by pharmacologic inhibitors and RNA interference for the treatment of colorectal cancer patients.

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Moro, F., F. Levenez, H. Guignard, J. A. Chayvialle, A. S. Giraud, and J. C. Cuber. "Secretion of the intestinal trefoil factor from the isolated vascularly perfused rat colon." Gastroenterology 114 (April 1998): A400—A401. http://dx.doi.org/10.1016/s0016-5085(98)81621-1.

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Menheniott, Trevelyan R., Bayzar Kurklu, and Andrew S. Giraud. "Gastrokines: stomach-specific proteins with putative homeostatic and tumor suppressor roles." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 2 (January 15, 2013): G109—G121. http://dx.doi.org/10.1152/ajpgi.00374.2012.

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During the past decade, a new family of stomach-specific proteins has been recognized. Known as “gastrokines” (GKNs), these secreted proteins are products of gastric mucus-producing cell lineages. GKNs are highly conserved in physical structure, and emerging data point to convergent functions in the modulation of gastric mucosal homeostasis and inflammation. While GKNs are highly prevalent in the normal stomach, frequent loss of GKN expression in gastric cancers, coupled with established antiproliferative activity, suggests putative tumor suppressor roles. Conversely, ectopic expression of GKNs in reparative lesions of Crohn's disease alludes to additional activity in epithelial wound healing and/or repair. Modes of action remain unsolved, but the recent demonstration of a GKN2-trefoil factor 1 heterodimer implicates functional interplay with trefoil factors. This review aims to provide a historical account of GKN biology and encapsulate the rapidly accumulating evidence supporting roles in gastric epithelial homeostasis and tumor suppression.

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FENG, GUOXUN, YAN ZHANG, HUISHENG YUAN, RIXING BAI, JIANWEI ZHENG, JINQIAN ZHANG, and MAOMIN SONG. "DNA methylation of trefoil factor 1 (TFF1) is associated with the tumorigenesis of gastric carcinoma." Molecular Medicine Reports 9, no. 1 (November 4, 2013): 109–17. http://dx.doi.org/10.3892/mmr.2013.1772.

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Chutipongtanate, S. "Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor." Journal of Clinical Investigation 115, no. 12 (December 1, 2005): 3613–22. http://dx.doi.org/10.1172/jci25342.

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Karam, S. M., C. Tomasetto, and M. ‐C Rio. "Amplification and invasiveness of epithelial progenitors during gastric carcinogenesis in trefoil factor 1 knockout mice." Cell Proliferation 41, no. 6 (November 18, 2008): 923–35. http://dx.doi.org/10.1111/j.1365-2184.2008.00562.x.

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Atala, Anthony. "Re: Trefoil Factor 1 Suppression of E-CADHERIN Enhances Prostate Carcinoma Cell Invasiveness and Metastasis." Journal of Urology 191, no. 1 (January 2014): 270–71. http://dx.doi.org/10.1016/j.juro.2013.10.006.

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