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DC Field | Value | Language |
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dc.contributor.author | Pandit, H | - |
dc.contributor.author | Thakur, G | - |
dc.contributor.author | Koippallil Gopalakrishnan, AR | - |
dc.contributor.author | Dodagatta-Marri, E | - |
dc.contributor.author | Patil, A | - |
dc.contributor.author | Kishore, U | - |
dc.contributor.author | Madan, T | - |
dc.date.accessioned | 2016-05-24T15:35:09Z | - |
dc.date.available | 2016-02 | - |
dc.date.available | 2016-05-24T15:35:09Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Immunobiology, 2016, 221 (2), pp. 310 - 322 | en_US |
dc.identifier.issn | 0171-2985 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/12678 | - |
dc.description.abstract | Surfactant Protein D (SP-D) is an integral molecule of the innate immunity secreted by the epithelial cells lining the mucosal surfaces. Its C-type lectin domain offers pattern recognition functions while it binds to putative receptors on immune cells to modify cellular functions. Activated PBMCs and increased serum levels of SP-D are observed under a range of pathophysiological conditions including infections. Thus, we speculated if SP-D can modulate systemic immune response via direct interaction with activated PBMCs. Here, we have examined interaction of a recombinant fragment of human SP-D (rhSP-D) on PHA-activated PBMCs. We observed a significant downregulation of TLR2, TLR4, CD11c and CD69 upon rhSP-D treatment. rhSP-D inhibited production of Th1 (TNF-α and IFN-γ) and Th17 (IL-17) cytokines along with IL-6. Interestingly, levels of IL-2, Th2 (IL-4) and regulatory (IL-10 and TGF-β) cytokines were unaltered. Differential expression of co-stimulatory CD28 and co-inhibitory CTLA4 expression along with their ligands CD80 and CD86 revealed selective up-regulation of CTLA4 at both mRNA and protein level. In addition, rhSP-D induced apoptosis only in the activated but not in non-activated PBMCs. Blockade of CTLA4 inhibited rhSP-D mediated apoptosis, confirming an involvement of CTLA4 in induction of apoptosis. We conclude that SP-D restores immune homeostasis: it regulates expression of immunomodulatory receptors and cytokines, which is followed by apoptosis induction of immune-activated cells. These findings appear to suggest a general role for SPD in immune surveillance against activated immune cells. | en_US |
dc.format.extent | 310 - 322 | - |
dc.language.iso | en | en_US |
dc.title | Surfactant protein D induces immune quiescence and apoptosis of mitogen-activated peripheral blood mononuclear cells | en_US |
dc.type | Article | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/j.imbio.2015.10.004 | - |
dc.relation.isPartOf | Immunobiology | - |
pubs.issue | 2 | - |
pubs.notes | publisher: Elsevier articletitle: Surfactant protein D induces immune quiescence and apoptosis of mitogen-activated peripheral blood mononuclear cells journaltitle: Immunobiology articlelink: http://dx.doi.org/10.1016/j.imbio.2015.10.004 content_type: article copyright: Copyright © 2015 Elsevier GmbH. All rights reserved. | - |
pubs.publication-status | Published | - |
pubs.volume | 221 | - |
Appears in Collections: | Dept of Life Sciences Research Papers |
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FullText.pdf | 4.77 MB | Adobe PDF | View/Open |
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