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.

journal_name

Biosci Rep

journal_title

Bioscience reports

authors

Malhotra R,Haurum J,Thiel S,Jensenius JC,Sim RB

doi

10.1007/BF01145960

subject

Has Abstract

pub_date

1993-04-01 00:00:00

pages

79-90

issue

2

eissn

0144-8463

issn

1573-4935

journal_volume

13

pub_type

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