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- W4313380746 abstract "Abstract There is evidence that lung surfactant protein A (SP-A) plays an important role in modulating inflammation during lung infection. However, it has been reported that SP-A either stimulates or inhibits the inflammatory activity of IFN-γ on alveolar macrophages (aMϕ). The aim of this study was to determine the effect of human SP-A on alveolar macrophages stimulated with IFN-γ in the presence or absence of LPS. To accomplish this, purified rat aMϕ were cultured in the presence or absence of IFN-γ (10 ng/ml), LPS (1 ng/ml), SP-A (5, 12.5, 25 μg/mL), and combinations thereof. We measured iNOS synthesis, TNF-α secretion, as well as STAT-1, ERK, and Akt phosphorylation by rat aMϕ. We found that SP-A inhibited STAT1 phosphorylation activated by IFN-γ. In addition, SP-A diminished LPS-induced ERK and Akt phosphorylation. Finally, SP-A inhibited [LPS+IFN-γ]-induced TNF-α and iNOS production. Therefore, the inhibitory effect of SP-A on [IFN-γ+LPS]-elicited macrophage activation is due to SP-A attenuation of both inflamatory agents. To determine the mechanism by which SP-A abrogates IFN-γ effects, we studied the potential interaction between SP-A and IFN-γ. SP-A specifically bound to IFN-γ, with Kd = 28, 2 ± 8 nM. These data support the biological function of SP-A in host defense, revealing a role of this alveolar protein in limiting classical activation of aMϕ elicited by IFN-γ + LPS." @default.
- W4313380746 created "2023-01-06" @default.
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- W4313380746 date "2012-05-01" @default.
- W4313380746 modified "2023-10-16" @default.
- W4313380746 title "Lung surfactant protein A attenuates alveolar macrophage classical activation induced by LPS + IFN-γ through binding to IFN-γ and blocking LPS-signaling (172.5)" @default.
- W4313380746 doi "https://doi.org/10.4049/jimmunol.188.supp.172.5" @default.
- W4313380746 hasPublicationYear "2012" @default.
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