Trefoil factor family (TFF) expression in the mouse brain and pituitary: changes in the developing cerebellum

Hinz, Manfred; Schwegler, Herbert; Chwieralski, Caroline E.; Laube, Gregor; Linke, Rüdiger; Pohle, W. D.; Hoffmann, Werner

doi:10.1016/j.peptides.2004.01.020

Cited by 42 publications

(47 citation statements)

References 27 publications

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“…Stress-induced impairment in the noradrenergic facilitation of g-aminobutyric acid release in the BLA may be the underlying mechanism of amygdala hyperexcitability in certain stress-related mood disorders (Aroniadou-Anderjaska et al, 2007;Drevets et al, 2008). Furthermore, previous studies showed that the neural expression of TFF3 includes the hypothalamus and amygdala (Hinz et al, 2004). Our results also showed that Fos expression, an indicator of neuronal activation, was increased in the BLA by systemic TFF3 administration.…”

Section: Homeostatic Adaption Of Neuropeptide Tff3 In Response To Stresssupporting

confidence: 70%

PI3K/Akt Signaling Pathway in the Basolateral Amygdala Mediates the Rapid Antidepressant-like Effects of Trefoil Factor 3

Shi

Zhu

Liu

et al. 2012

Neuropsychopharmacol

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Section: Homeostatic Adaption Of Neuropeptide Tff3 In Response To Stresssupporting

confidence: 70%

PI3K/Akt Signaling Pathway in the Basolateral Amygdala Mediates the Rapid Antidepressant-like Effects of Trefoil Factor 3

Shi

Zhu

Liu

et al. 2012

Neuropsychopharmacol

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“…For example, TFF2 is found in macrophages and lymphocytes (24,25) as well as in the anterior pituitary and the developing brain (26).…”

Section: Tff2 a Muc6-binding Lectin Stabilizing The Gastric Mucus Bamentioning

confidence: 99%

TFF2, a MUC6-binding lectin stabilizing the gastric mucus barrier and more (Review)

Hoffmann

2015

International Journal of Oncology

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Abstract. The peptide TFF2 (formerly 'spasmolytic polypeptide'), a member of the trefoil factor family (TFF) containing two TFF domains, is mainly expressed together with the mucin MUC6 in the gastric epithelium and duodenal Brunner's glands. Pathologically, TFF2 expression is observed ectopically during stone diseases, chronic inflammatory conditions and in several metaplastic and neoplastic epithelia; most prominent being the 'spasmolytic polypeptide-expressing metaplasia' (SPEM), which is an established gastric precancerous lesion. TFF2 plays a critical role in maintaining gastric mucosal integrity and appears to restrain tumorigenesis in the stomach. Recently, porcine TFF2 has been shown to interact with the gastric mucin MUC6 and thus stabilize the gastric mucus barrier. On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcα1→4Galβ1→R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges. Thus, implications for the complex multimeric assembly, cross-linking, and packaging of MUC6 as well as the rheology of gastric mucus are discussed in detail in this review. Furthermore, TFF2 is also expressed in minor amounts in the immune and nervous systems. Thus, similar to galectins, its lectin activity would perfectly enable TFF2 to form multivalent complexes and cross-linked lattices with a plethora of transmembrane glycoproteins and thus modulate different signal transduction processes. This could explain the multiple and diverse biological effects of TFF2 [e.g., motogenic, (anti)apoptotic, and angiogenic effects]. Finally, a function during fertilization is also possible for TFF domains because they occur as shuffled modules in certain zona pellucida proteins.

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“…TFF2 is also expressed in the brain and pituitary [33] as well as in immune cells such as macrophages and lymphocytes [30,34]. Tff2 KO mice show an altered expression of genes implicated in immune regulation [35] and their immune cells are hyperresponsive to IL-1β stimulation [30].…”

Section: Introductionmentioning

confidence: 99%

Porcine Gastric TFF2 is a Mucus Constituent and Differs from Pancreatic TFF2

Stürmer

Müller

Hanisch

et al. 2014

Cell Physiol Biochem

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Background/Aims: TFF2 is a secretory peptide (106 amino acid residues) of the gastric mucosa, the porcine exocrine pancreas as well as immune cells and the CNS. It was the aim of this study to compare gastric and pancreatic TFF2. Methods: TFF2 was purified from the porcine stomach and pancreas, respectively, by size-exclusion and anion-exchange chromatography and then analyzed by Western blots as well as mass spectrometry. Results: Gastric and pancreatic TFF2 differed markedly, i.e. gastric TFF2 was exclusively associated with the high molecular mass mucus fraction, whereas pancreatic TFF2 appeared as a low molecular mass product. Unexpectedly, the latter predominantly formed a non-covalently linked homodimer resistant to boiling SDS. In contrast, gastric TFF2 is an integral mucus constituent predominantly binding to the mucin MUC6 in a non-covalent fashion. Conclusion: The non-covalent interaction of TFF2 with the mucin MUC6 is typical of a "link peptide" which is perfectly suited to assemble and stabilize the laminated structure of gastric mucus and to modulate its rheological properties.

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Trefoil factor family (TFF) expression in the mouse brain and pituitary: changes in the developing cerebellum

Cited by 42 publications

References 27 publications

PI3K/Akt Signaling Pathway in the Basolateral Amygdala Mediates the Rapid Antidepressant-like Effects of Trefoil Factor 3

PI3K/Akt Signaling Pathway in the Basolateral Amygdala Mediates the Rapid Antidepressant-like Effects of Trefoil Factor 3

TFF2, a MUC6-binding lectin stabilizing the gastric mucus barrier and more (Review)

Porcine Gastric TFF2 is a Mucus Constituent and Differs from Pancreatic TFF2

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