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Jens Christian Jensenius

Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A)

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Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A). / Malhotra, R; Haurum, J; Thiel, S; Jensenius, J C; Sim, R B.

In: Bioscience Reports, Vol. 13, No. 2, 01.04.1993, p. 79-90.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Malhotra, R, Haurum, J, Thiel, S, Jensenius, JC & Sim, RB 1993, 'Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A)', Bioscience Reports, vol. 13, no. 2, pp. 79-90.

APA

Malhotra, R., Haurum, J., Thiel, S., Jensenius, J. C., & Sim, R. B. (1993). Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A). Bioscience Reports, 13(2), 79-90.

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MLA

Vancouver

Author

Malhotra, R ; Haurum, J ; Thiel, S ; Jensenius, J C ; Sim, R B. / Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A). In: Bioscience Reports. 1993 ; Vol. 13, No. 2. pp. 79-90.

Bibtex

@article{2588b28356db4a20b6fa684337f8e309,
title = "Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A)",
abstract = "Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.",
keywords = "Calcium, Cell Line, Humans, Macrophages, Alveolar, Pollen, Protein Binding, Proteolipids, Pulmonary Surfactant-Associated Protein A, Pulmonary Surfactant-Associated Proteins, Pulmonary Surfactants",
author = "R Malhotra and J Haurum and S Thiel and Jensenius, {J C} and Sim, {R B}",
year = "1993",
month = "4",
day = "1",
language = "English",
volume = "13",
pages = "79--90",
journal = "Bioscience Reports",
issn = "0144-8463",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A)

AU - Malhotra, R

AU - Haurum, J

AU - Thiel, S

AU - Jensenius, J C

AU - Sim, R B

PY - 1993/4/1

Y1 - 1993/4/1

N2 - Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.

AB - Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.

KW - Calcium

KW - Cell Line

KW - Humans

KW - Macrophages, Alveolar

KW - Pollen

KW - Protein Binding

KW - Proteolipids

KW - Pulmonary Surfactant-Associated Protein A

KW - Pulmonary Surfactant-Associated Proteins

KW - Pulmonary Surfactants

M3 - Journal article

C2 - 8374060

VL - 13

SP - 79

EP - 90

JO - Bioscience Reports

JF - Bioscience Reports

SN - 0144-8463

IS - 2

ER -