Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain

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

Standard

Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. / Honoré, Christian; Rørvig, Sara; Hummelshøj, Tina; Skjoedt, Mikkel-Ole; Borregaard, Niels; Garred, Peter; Honoré, Christian; Rørvig, Sara; Hummelshøj, Tina; Skjoedt, Mikkel-Ole; Borregaard, Niels; Garred, Peter.

In: Journal of Leukocyte Biology, Vol. 88, No. 1, 01.07.2010, p. 145-58.

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

Harvard

Honoré, C, Rørvig, S, Hummelshøj, T, Skjoedt, M-O, Borregaard, N, Garred, P, Honoré, C, Rørvig, S, Hummelshøj, T, Skjoedt, M-O, Borregaard, N & Garred, P 2010, 'Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain', Journal of Leukocyte Biology, vol. 88, no. 1, pp. 145-58. https://doi.org/10.1189/jlb.1209802, https://doi.org/10.1189/jlb.1209802

APA

Honoré, C., Rørvig, S., Hummelshøj, T., Skjoedt, M-O., Borregaard, N., Garred, P., Honoré, C., Rørvig, S., Hummelshøj, T., Skjoedt, M-O., Borregaard, N., & Garred, P. (2010). Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. Journal of Leukocyte Biology, 88(1), 145-58. https://doi.org/10.1189/jlb.1209802, https://doi.org/10.1189/jlb.1209802

Vancouver

Honoré C, Rørvig S, Hummelshøj T, Skjoedt M-O, Borregaard N, Garred P et al. Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. Journal of Leukocyte Biology. 2010 Jul 1;88(1):145-58. https://doi.org/10.1189/jlb.1209802, https://doi.org/10.1189/jlb.1209802

Author

Honoré, Christian ; Rørvig, Sara ; Hummelshøj, Tina ; Skjoedt, Mikkel-Ole ; Borregaard, Niels ; Garred, Peter ; Honoré, Christian ; Rørvig, Sara ; Hummelshøj, Tina ; Skjoedt, Mikkel-Ole ; Borregaard, Niels ; Garred, Peter. / Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. In: Journal of Leukocyte Biology. 2010 ; Vol. 88, No. 1. pp. 145-58.

Bibtex

@article{e3281ba0ecb011dfb6d2000ea68e967b,
title = "Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain",
abstract = "Three Ficolins have been identified in humans: Ficolin-1 (M-Ficolin), Ficolin-2 (L-Ficolin), and Ficolin-3 (H-Ficolin). Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. Ficolin-1 has been reported on the surface of monocytes and granulocytes and was suggested originally to function as a phagocytic receptor. However, the molecule does not contain any obvious transmembrane domain, and no binding partners have been identified. To gain further insight in the physiological role of Ficolin-1, we sought to identify the molecular mechanism responsible for the membrane association of Ficolin-1 to monocytes and granulocytes. We demonstrate that expression of Ficolin-1 on the cell surface is restricted to monocytes and granulocytes. Ficolin-1 is tethered to the cell surface of these cells through its fibrinogen-like domain, and the ligand involved in the binding of Ficolin-1 is shown to be sialic acid. Moreover, rFicolin-1 bound activated but not resting T lymphocytes. Together, these results demonstrate a novel self-recognition mechanism of leukocytes mediated by the fibrinogen-like domain of Ficolin-1.",
author = "Christian Honor{\'e} and Sara R{\o}rvig and Tina Hummelsh{\o}j and Mikkel-Ole Skjoedt and Niels Borregaard and Peter Garred and Christian Honor{\'e} and Sara R{\o}rvig and Tina Hummelsh{\o}j and Mikkel-Ole Skjoedt and Niels Borregaard and Peter Garred",
note = "Keywords: Calcium; Fibrinogen; Granulocytes; Humans; Lectins; Lymphocyte Activation; Monocytes; N-Acetylneuraminic Acid; Protein Structure, Tertiary; Recombinant Proteins; T-Lymphocytes; U937 Cells",
year = "2010",
month = jul,
day = "1",
doi = "10.1189/jlb.1209802",
language = "English",
volume = "88",
pages = "145--58",
journal = "Journal of Leukocyte Biology",
issn = "0741-5400",
publisher = "Federation of American Societies for Experimental Biology",
number = "1",

}

RIS

TY - JOUR

T1 - Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain

AU - Honoré, Christian

AU - Rørvig, Sara

AU - Hummelshøj, Tina

AU - Skjoedt, Mikkel-Ole

AU - Borregaard, Niels

AU - Garred, Peter

AU - Honoré, Christian

AU - Rørvig, Sara

AU - Hummelshøj, Tina

AU - Skjoedt, Mikkel-Ole

AU - Borregaard, Niels

AU - Garred, Peter

N1 - Keywords: Calcium; Fibrinogen; Granulocytes; Humans; Lectins; Lymphocyte Activation; Monocytes; N-Acetylneuraminic Acid; Protein Structure, Tertiary; Recombinant Proteins; T-Lymphocytes; U937 Cells

PY - 2010/7/1

Y1 - 2010/7/1

N2 - Three Ficolins have been identified in humans: Ficolin-1 (M-Ficolin), Ficolin-2 (L-Ficolin), and Ficolin-3 (H-Ficolin). Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. Ficolin-1 has been reported on the surface of monocytes and granulocytes and was suggested originally to function as a phagocytic receptor. However, the molecule does not contain any obvious transmembrane domain, and no binding partners have been identified. To gain further insight in the physiological role of Ficolin-1, we sought to identify the molecular mechanism responsible for the membrane association of Ficolin-1 to monocytes and granulocytes. We demonstrate that expression of Ficolin-1 on the cell surface is restricted to monocytes and granulocytes. Ficolin-1 is tethered to the cell surface of these cells through its fibrinogen-like domain, and the ligand involved in the binding of Ficolin-1 is shown to be sialic acid. Moreover, rFicolin-1 bound activated but not resting T lymphocytes. Together, these results demonstrate a novel self-recognition mechanism of leukocytes mediated by the fibrinogen-like domain of Ficolin-1.

AB - Three Ficolins have been identified in humans: Ficolin-1 (M-Ficolin), Ficolin-2 (L-Ficolin), and Ficolin-3 (H-Ficolin). Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. Ficolin-1 has been reported on the surface of monocytes and granulocytes and was suggested originally to function as a phagocytic receptor. However, the molecule does not contain any obvious transmembrane domain, and no binding partners have been identified. To gain further insight in the physiological role of Ficolin-1, we sought to identify the molecular mechanism responsible for the membrane association of Ficolin-1 to monocytes and granulocytes. We demonstrate that expression of Ficolin-1 on the cell surface is restricted to monocytes and granulocytes. Ficolin-1 is tethered to the cell surface of these cells through its fibrinogen-like domain, and the ligand involved in the binding of Ficolin-1 is shown to be sialic acid. Moreover, rFicolin-1 bound activated but not resting T lymphocytes. Together, these results demonstrate a novel self-recognition mechanism of leukocytes mediated by the fibrinogen-like domain of Ficolin-1.

U2 - 10.1189/jlb.1209802

DO - 10.1189/jlb.1209802

M3 - Journal article

C2 - 20400674

VL - 88

SP - 145

EP - 158

JO - Journal of Leukocyte Biology

JF - Journal of Leukocyte Biology

SN - 0741-5400

IS - 1

ER -

ID: 23064547