scholarly journals Aberrant Expression of Trefoil Factor Family 1 in Biliary Epithelium in Hepatolithiasis and Cholangiocarcinoma

2003 ◽  
Vol 83 (10) ◽  
pp. 1403-1413 ◽  
Author(s):  
Motoko Sasaki ◽  
Koichi Tsuneyama ◽  
Yasuni Nakanuma
Keyword(s):  
Trefoil Factor ◽  
Aberrant Expression ◽  
Biliary Epithelium ◽  
Trefoil Factor Family

Trefoil factor family peptide 2 acts pro-proliferative and pro-apoptotic in the murine retina

2011 ◽  
Vol 135 (5) ◽  
pp. 461-473 ◽  
Author(s):  
Adnana N. Paunel-Görgülü ◽  
Andreas G. Franke ◽  
Friedrich P. Paulsen ◽  
Nicole Dünker
Keyword(s):  
Trefoil Factor ◽  
Trefoil Factor Family

scholarly journals Expression of Trefoil Factor Family Members Correlates with Patient Prognosis and Neoangiogenesis

2005 ◽  
Vol 11 (18) ◽  
pp. 6472-6478 ◽  
Author(s):  
Dipok Kumar Dhar ◽  
Timothy C. Wang ◽  
Hideki Tabara ◽  
Yasuhito Tonomoto ◽  
Riruke Maruyama ◽  
...  
Keyword(s):  
Family Members ◽  
Trefoil Factor ◽  
Trefoil Factor Family ◽  
Patient Prognosis

Expression and localization of trefoil factor family genes in rat submandibular glands

2014 ◽  
Vol 89 (6) ◽  
pp. 424-432 ◽  
Author(s):  
JF Wu ◽  
J Zhang ◽  
G Xue ◽  
HQ Zhang
Keyword(s):  
Trefoil Factor ◽  
Submandibular Glands ◽  
Trefoil Factor Family

scholarly journals Trefoil Factor Family (TFF) Modules Are Characteristic Constituents of Separate Mucin Complexes in the Xenopus laevis Integumentary Mucus: In Vitro Binding Studies with FIM-A.1

2020 ◽  
Vol 21 (7) ◽  
pp. 2400 ◽  
Author(s):  
René Stürmer ◽  
Jana Reising ◽  
Werner Hoffmann
Keyword(s):  
Molecular Mass ◽  
Complex I ◽  
Size Exclusion ◽  
Trefoil Factor ◽  
Binding Studies ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Exclusion Chromatography ◽  
Trefoil Factor Family

The skin of the frog Xenopus laeevis is protected from microbial infections by a mucus barrier that contains frog integumentary mucins (FIM)-A.1, FIM-B.1, and FIM-C.1. These gel-forming mucins are synthesized in mucous glands consisting of ordinary mucous cells and one or more cone cells at the gland base. FIM-A.1 and FIM-C.1 are unique because their cysteine-rich domains belong to the trefoil factor family (TFF). Furthermore, FIM-A.1 is unusually short (about 400 amino acid residues). In contrast, FIM-B.1 contains cysteine-rich von Willebrand D (vWD) domains. Here, we separate skin extracts by the use of size exclusion chromatography and analyze the distribution of FIM-A.1 and FIM-C.1. Two mucin complexes were detected, i.e., a high-molecular-mass Complex I, which contains FIM-C.1 and little FIM-A.1, whereas Complex II is of lower molecular mass and contains the bulk of FIM-A.1. We purified FIM-A.1 by a combination of size-exclusion chromatography (SEC) and anion-exchange chromatography and performed first in vitro binding studies with radioactively labeled FIM-A.1. Binding of 125I-labeled FIM-A.1 to the high-molecular-mass Complex I was observed. We hypothesize that the presence of FIM-A.1 in Complex I is likely due to lectin interactions, e.g., with FIM-C.1, creating a complex mucus network.

scholarly journals Trefoil Factor Family (TFF) Peptides and Their Diverse Molecular Functions in Mucus Barrier Protection and More: Changing the Paradigm

2020 ◽  
Vol 21 (12) ◽  
pp. 4535 ◽  
Author(s):  
Werner Hoffmann
Keyword(s):  
Thiol Group ◽  
Suppressor Gene ◽  
Immune Defense ◽  
Trefoil Factor ◽  
Gastric Mucus ◽  
Free Thiol Group ◽  
Trefoil Factor Family ◽  
Molecular Functions ◽  
Mucus Barrier ◽  
Tff Peptides

Trefoil factor family peptides (TFF1, TFF2, TFF3) are typically co-secreted together with mucins. Tff1 represents a gastric tumor suppressor gene in mice. TFFs are also synthesized in minute amounts in the immune and central nervous systems. In mucous epithelia, they support rapid repair by enhancing cell migration (“restitution”) via their weak chemotactic and anti-apoptotic effects. For a long time, as a paradigm, this was considered as their major biological function. Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP). Furthermore, lectin activities were recognized as enabling binding to a lipopolysaccharide of Helicobacter pylori (TFF1, TFF3) or to a carbohydrate moiety of the mucin MUC6 (TFF2). Only recently, gastric TFF1 was demonstrated to occur predominantly in monomeric forms with an unusual free thiol group. Thus, a new picture emerged, pointing to diverse molecular functions for TFFs. Monomeric TFF1 might protect the gastric mucosa as a scavenger for extracellular reactive oxygen/nitrogen species. Whereas, the TFF2/MUC6 complex stabilizes the inner layer of the gastric mucus. In contrast, the TFF3–FCGBP heterodimer (and also TFF1–FCGBP) are likely part of the innate immune defense of mucous epithelia, preventing the infiltration of microorganisms.

scholarly journals Obstructive sleep apnea and rhonchopathy are associated with downregulation of trefoil factor family peptide 3 (TFF3)—Implications of changes in oral mucus composition

PLoS ONE ◽  
2017 ◽  
Vol 12 (10) ◽  
pp. e0185200 ◽  
Author(s):  
Regina Siber-Hoogeboom ◽  
Martin Schicht ◽  
Sebastian Hoogeboom ◽  
Friedrich Paulsen ◽  
Maximilian Traxdorf
Keyword(s):  
Obstructive Sleep Apnea ◽  
Sleep Apnea ◽  
Trefoil Factor ◽  
Obstructive Sleep ◽  
Trefoil Factor Family

Trefoil factor family peptides – friends or foes?

2015 ◽  
Vol 6 (5-6) ◽  
pp. 343-359 ◽  
Author(s):  
Maike Busch ◽  
Nicole Dünker
Keyword(s):  
Cancer Research ◽  
Tumor Suppressors ◽  
Current Knowledge ◽  
Tumor Biology ◽  
Epigenetic Mechanisms ◽  
Trefoil Factor ◽  
Protective Function ◽  
Trefoil Factor Family ◽  
Tff Peptides

AbstractTrefoil factor family (TFF) peptides are a group of molecules bearing a characteristic three-loop trefoil domain. They are mainly secreted in mucous epithelia together with mucins but are also synthesized in the nervous system. For many years, TFF peptides were only known for their wound healing and protective function, e.g. in epithelial protection and restitution. However, experimental evidence has emerged supporting a pivotal role of TFF peptides in oncogenic transformation, tumorigenesis and metastasis. Deregulated expression of TFF peptides at the gene and protein level is obviously implicated in numerous cancers, and opposing functions as oncogenes and tumor suppressors have been described. With regard to the regulation of TFF expression, epigenetic mechanisms as well as the involvement of various miRNAs are new, promising aspects in the field of cancer research. This review will summarize current knowledge about the expression and regulation of TFF peptides and the involvement of TFF peptides in tumor biology and cancerogenesis.

scholarly journals Forced Trefoil Factor Family Peptide 3 (TFF3) Expression Reduces Growth, Viability, and Tumorigenicity of Human Retinoblastoma Cell Lines

PLoS ONE ◽  
2016 ◽  
Vol 11 (9) ◽  
pp. e0163025 ◽  
Author(s):  
Jan Große-Kreul ◽  
Maike Busch ◽  
Claudia Winter ◽  
Stefanie Pikos ◽  
Harald Stephan ◽  
...  
Keyword(s):  
Cell Lines ◽  
Trefoil Factor ◽  
Retinoblastoma Cell ◽  
Human Retinoblastoma ◽  
Trefoil Factor Family
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