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Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)

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Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP). / Houben, Till; Harder, Sönke; Schlüter, Hartmut; Kalbacher, Hubert; Hoffmann, Werner.

In: INT J MOL SCI, Vol. 20, No. 20, 10.10.2019.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Houben, T, Harder, S, Schlüter, H, Kalbacher, H & Hoffmann, W 2019, 'Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)', INT J MOL SCI, vol. 20, no. 20. https://doi.org/10.3390/ijms20205000

APA

Houben, T., Harder, S., Schlüter, H., Kalbacher, H., & Hoffmann, W. (2019). Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP). INT J MOL SCI, 20(20). https://doi.org/10.3390/ijms20205000

Vancouver

Houben T, Harder S, Schlüter H, Kalbacher H, Hoffmann W. Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP). INT J MOL SCI. 2019 Oct 10;20(20). https://doi.org/10.3390/ijms20205000

Bibtex

@article{ab01e43f48644715b6385540d9cec25f,
title = "Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)",
abstract = "The peptide TFF3 is a member of a family of secretory lectins, and is typically synthesized by mucous epithelia together with mucins. It is mainly released from intestinal goblet cells as a high-molecular mass heterodimer with IgG Fc binding protein (FCGBP). Herein, we investigated human saliva by fast protein liquid chromatography (FPLC) and proteomics and identified high- and low-molecular-mass forms of TFF3. Whereas the high-molecular-mass forms represent a heterodimer with FCGBP, the low-molecular-mass forms represent homodimeric TFF3 forms. Proteomic analysis also revealed a C-terminally truncated form of TFF3. We hypothesize that salivary TFF3-FCGBP might play a role in the innate immune defense of the oral cavity and that TFF3 might also bind to microbial glycans. The known interaction of TFF3 with the agglutinin DMBT-1, a typical constituent of human saliva, further supports this protective role.",
author = "Till Houben and S{\"o}nke Harder and Hartmut Schl{\"u}ter and Hubert Kalbacher and Werner Hoffmann",
year = "2019",
month = oct,
day = "10",
doi = "10.3390/ijms20205000",
language = "English",
volume = "20",
journal = "INT J MOL SCI",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "20",

}

RIS

TY - JOUR

T1 - Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)

AU - Houben, Till

AU - Harder, Sönke

AU - Schlüter, Hartmut

AU - Kalbacher, Hubert

AU - Hoffmann, Werner

PY - 2019/10/10

Y1 - 2019/10/10

N2 - The peptide TFF3 is a member of a family of secretory lectins, and is typically synthesized by mucous epithelia together with mucins. It is mainly released from intestinal goblet cells as a high-molecular mass heterodimer with IgG Fc binding protein (FCGBP). Herein, we investigated human saliva by fast protein liquid chromatography (FPLC) and proteomics and identified high- and low-molecular-mass forms of TFF3. Whereas the high-molecular-mass forms represent a heterodimer with FCGBP, the low-molecular-mass forms represent homodimeric TFF3 forms. Proteomic analysis also revealed a C-terminally truncated form of TFF3. We hypothesize that salivary TFF3-FCGBP might play a role in the innate immune defense of the oral cavity and that TFF3 might also bind to microbial glycans. The known interaction of TFF3 with the agglutinin DMBT-1, a typical constituent of human saliva, further supports this protective role.

AB - The peptide TFF3 is a member of a family of secretory lectins, and is typically synthesized by mucous epithelia together with mucins. It is mainly released from intestinal goblet cells as a high-molecular mass heterodimer with IgG Fc binding protein (FCGBP). Herein, we investigated human saliva by fast protein liquid chromatography (FPLC) and proteomics and identified high- and low-molecular-mass forms of TFF3. Whereas the high-molecular-mass forms represent a heterodimer with FCGBP, the low-molecular-mass forms represent homodimeric TFF3 forms. Proteomic analysis also revealed a C-terminally truncated form of TFF3. We hypothesize that salivary TFF3-FCGBP might play a role in the innate immune defense of the oral cavity and that TFF3 might also bind to microbial glycans. The known interaction of TFF3 with the agglutinin DMBT-1, a typical constituent of human saliva, further supports this protective role.

U2 - 10.3390/ijms20205000

DO - 10.3390/ijms20205000

M3 - SCORING: Journal article

C2 - 31658587

VL - 20

JO - INT J MOL SCI

JF - INT J MOL SCI

SN - 1661-6596

IS - 20

ER -