ArticleGut2000
The human trefoil peptide, TFF1, is present in different molecular forms that are intimately associated with mucus in normal stomach.
Article in Gut, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 99 citations in OpenAlex.
- Mechanisms of cellular crosstalk in the gastric tumor microenvironment are mediated by YAP1 and STAT3.Life science alliance · 2024Article
- Gut homeostasis, injury, and healing: New therapeutic targets.World journal of gastroenterology · 2022Review
- Prediction of Anti-COVID 19 Therapeutic Power of Medicinal Moroccan Plants Using Molecular Docking.Bioinformatics and biology insights · 2021Article
- Structure, Function, and Therapeutic Potential of the Trefoil Factor Family in the Gastrointestinal Tract.ACS pharmacology & translational science · 2020Review
- Trefoil Factor Family (TFF) Peptides and Their Diverse Molecular Functions in Mucus Barrier Protection and More: Changing the Paradigm.International journal of molecular sciences · 2020Review
- Chemical synthesis of human trefoil factor 1 (TFF1) and its homodimer provides novel insights into their mechanisms of action.Chemical communications (Cambridge, England) · 2020Article
- The Tumor Suppressor TFF1 Occurs in Different Forms and Interacts with Multiple Partners in the Human Gastric Mucus Barrier: Indications for Diverse Protective Functions.International journal of molecular sciences · 2020Article
- Molecular Alterations in the Stomach ofInternational journal of molecular sciences · 2020Article
- The Interaction ofInternational journal of molecular sciences · 2019Review
- Binding ofMicroorganisms · 2018Article
- Heterodimeric interaction between GKN2 and TFF1 entails synergistic antiproliferative and pro-apoptotic effects on gastric cancer cells.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2017Article
- Trefoil Factor Peptides and Gastrointestinal Function.Annual review of physiology · 2017Review
- Functional expression of recombinant human trefoil factor 1 by Escherichia coli and Brevibacillus choshinensis.BMC biotechnology · 2015Article
- Activation of the NF-kB pathway downregulates TFF-1 in gastric carcinogenesis.Virchows Archiv : an international journal of pathology · 2013Article
- Virulent Shigella flexneri affects secretion, expression, and glycosylation of gel-forming mucins in mucus-producing cells.Infection and immunity · 2013Article
- Optimising the quantification of cytokines present at low concentrations in small human mucosal tissue samples using Luminex assays.Journal of immunological methods · 2013Article
- The interaction of Helicobacter pylori with the adherent mucus gel layer secreted by polarized HT29-MTX-E12 cells.PloS one · 2012Article
- Mucin dynamics and enteric pathogens.Nature reviews. Microbiology · 2011Review
- Selective gene expression by rat gastric corpus epithelium.Physiological genomics · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTFF1 is a 6.5 kDa secreted protein that is expressed predominantly in normal gastric mucosa. It is coexpressed with mucins and it can form dimers via a free carboxy terminal cysteine residue.
aimsTo investigate the molecular forms of TFF1 that are present in normal human stomach and the association of the different molecular forms with mucus. SUBJECTS: All subjects had macroscopically normal stomachs at gastroscopy. None had a significant past medical history.
methodsTFF1 was detected in normal gastric mucosa and adherent mucus by western transfer analysis after electrophoresis on reducing and non-reducing polyacrylamide gels. In some instances, proteins were fractionated by caesium chloride density gradient centrifugation prior to detection of TFF1. The location of TFF1 in gastric mucosa with an intact adherent mucus layer was assessed by immunohistochemistry.
resultsThree different molecular forms of TFF1 were detected: TFF1 monomer, TFF1 dimer, and a TFF1 complex with an apparent molecular mass of about 25 kDa. TFF1 was present at higher concentrations than realised previously. The TFF1 complex was present in the adherent mucus gel layer but while its interaction with mucin was destabilised by caesium chloride, the interaction between mucin and the TFF1 dimer was resistant to caesium chloride.
conclusionsMost of TFF1 in normal human gastric mucosa is present in a complex that is stabilised by a disulphide bond. TFF1 is intimately associated with mucus. The high concentration, colocalisation, and binding of TFF1 to gastric mucus strongly implicate TFF1 in gastric mucus function.
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