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Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions

Standard

Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions. / Weste, Jens; Houben, Till; Harder, Sönke; Schlüter, Hartmut; Lücke, Eva; Schreiber, Jens; Hoffmann, Werner.

in: INT J MOL SCI, Jahrgang 23, Nr. 23, 15359, 06.12.2022.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Weste, J, Houben, T, Harder, S, Schlüter, H, Lücke, E, Schreiber, J & Hoffmann, W 2022, 'Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions', INT J MOL SCI, Jg. 23, Nr. 23, 15359. https://doi.org/10.3390/ijms232315359

APA

Weste, J., Houben, T., Harder, S., Schlüter, H., Lücke, E., Schreiber, J., & Hoffmann, W. (2022). Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions. INT J MOL SCI, 23(23), [15359]. https://doi.org/10.3390/ijms232315359

Vancouver

Weste J, Houben T, Harder S, Schlüter H, Lücke E, Schreiber J et al. Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions. INT J MOL SCI. 2022 Dez 6;23(23). 15359. https://doi.org/10.3390/ijms232315359

Bibtex

@article{5e0aca76aaeb47bfb8e7c28c78867ed0,
title = "Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions",
abstract = "The polypeptide TFF3 belongs to the trefoil factor family (TFF) of lectins. TFF3 is typically secreted from mucous epithelia together with mucins. Both intestinal and salivary TFF3 mainly exist as disulfide-linked heterodimers with IgG Fc binding protein (FCGBP). Here, we investigated bronchial tissue specimens, bronchial secretions, and bronchoalveolar lavage (BAL) fluid from patients with a chronic obstructive pulmonary disease (COPD) background by fast protein liquid chromatography and proteomics. For the first time, we identified different molecular forms of TFF3 in the lung. The high-molecular mass form represents TFF3-FCGBP oligomers, whereas the low-molecular mass forms are homodimeric and monomeric TFF3 with possibly anti-apoptotic activities. In addition, disulfide-linked TFF3 heterodimers with an Mr of about 60k and 30k were detected in both bronchial secretions and BAL fluid. In these liquids, TFF3 is partly N-terminally truncated probably by neutrophil elastase cleavage. TFF3-FCGBP is likely involved in the mucosal innate immune defense against microbial infections. We discuss a hypothetical model how TFF3 might control FCGBP oligomerization. Furthermore, we did not find indications for interactions of TFF3-FCGBP with DMBT1gp340 or the mucin MUC5AC, glycoproteins involved in mucosal innate immunity. Surprisingly, bronchial MUC5AC appeared to be degraded when compared with gastric MUC5AC.",
keywords = "Humans, Trefoil Factor-2/metabolism, Trefoil Factor-3/metabolism, Mucins/metabolism, Carrier Proteins, Bronchi/metabolism, Disulfides/metabolism, Immunoglobulin G/metabolism, Cell Adhesion Molecules/metabolism",
author = "Jens Weste and Till Houben and S{\"o}nke Harder and Hartmut Schl{\"u}ter and Eva L{\"u}cke and Jens Schreiber and Werner Hoffmann",
year = "2022",
month = dec,
day = "6",
doi = "10.3390/ijms232315359",
language = "English",
volume = "23",
journal = "INT J MOL SCI",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "23",

}

RIS

TY - JOUR

T1 - Different Molecular Forms of TFF3 in the Human Respiratory Tract: Heterodimerization with IgG Fc Binding Protein (FCGBP) and Proteolytic Cleavage in Bronchial Secretions

AU - Weste, Jens

AU - Houben, Till

AU - Harder, Sönke

AU - Schlüter, Hartmut

AU - Lücke, Eva

AU - Schreiber, Jens

AU - Hoffmann, Werner

PY - 2022/12/6

Y1 - 2022/12/6

N2 - The polypeptide TFF3 belongs to the trefoil factor family (TFF) of lectins. TFF3 is typically secreted from mucous epithelia together with mucins. Both intestinal and salivary TFF3 mainly exist as disulfide-linked heterodimers with IgG Fc binding protein (FCGBP). Here, we investigated bronchial tissue specimens, bronchial secretions, and bronchoalveolar lavage (BAL) fluid from patients with a chronic obstructive pulmonary disease (COPD) background by fast protein liquid chromatography and proteomics. For the first time, we identified different molecular forms of TFF3 in the lung. The high-molecular mass form represents TFF3-FCGBP oligomers, whereas the low-molecular mass forms are homodimeric and monomeric TFF3 with possibly anti-apoptotic activities. In addition, disulfide-linked TFF3 heterodimers with an Mr of about 60k and 30k were detected in both bronchial secretions and BAL fluid. In these liquids, TFF3 is partly N-terminally truncated probably by neutrophil elastase cleavage. TFF3-FCGBP is likely involved in the mucosal innate immune defense against microbial infections. We discuss a hypothetical model how TFF3 might control FCGBP oligomerization. Furthermore, we did not find indications for interactions of TFF3-FCGBP with DMBT1gp340 or the mucin MUC5AC, glycoproteins involved in mucosal innate immunity. Surprisingly, bronchial MUC5AC appeared to be degraded when compared with gastric MUC5AC.

AB - The polypeptide TFF3 belongs to the trefoil factor family (TFF) of lectins. TFF3 is typically secreted from mucous epithelia together with mucins. Both intestinal and salivary TFF3 mainly exist as disulfide-linked heterodimers with IgG Fc binding protein (FCGBP). Here, we investigated bronchial tissue specimens, bronchial secretions, and bronchoalveolar lavage (BAL) fluid from patients with a chronic obstructive pulmonary disease (COPD) background by fast protein liquid chromatography and proteomics. For the first time, we identified different molecular forms of TFF3 in the lung. The high-molecular mass form represents TFF3-FCGBP oligomers, whereas the low-molecular mass forms are homodimeric and monomeric TFF3 with possibly anti-apoptotic activities. In addition, disulfide-linked TFF3 heterodimers with an Mr of about 60k and 30k were detected in both bronchial secretions and BAL fluid. In these liquids, TFF3 is partly N-terminally truncated probably by neutrophil elastase cleavage. TFF3-FCGBP is likely involved in the mucosal innate immune defense against microbial infections. We discuss a hypothetical model how TFF3 might control FCGBP oligomerization. Furthermore, we did not find indications for interactions of TFF3-FCGBP with DMBT1gp340 or the mucin MUC5AC, glycoproteins involved in mucosal innate immunity. Surprisingly, bronchial MUC5AC appeared to be degraded when compared with gastric MUC5AC.

KW - Humans

KW - Trefoil Factor-2/metabolism

KW - Trefoil Factor-3/metabolism

KW - Mucins/metabolism

KW - Carrier Proteins

KW - Bronchi/metabolism

KW - Disulfides/metabolism

KW - Immunoglobulin G/metabolism

KW - Cell Adhesion Molecules/metabolism

U2 - 10.3390/ijms232315359

DO - 10.3390/ijms232315359

M3 - SCORING: Journal article

C2 - 36499686

VL - 23

JO - INT J MOL SCI

JF - INT J MOL SCI

SN - 1661-6596

IS - 23

M1 - 15359

ER -