Source:http://linkedlifedata.com/resource/pubmed/id/18166151
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-1-18
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pubmed:abstractText |
NAD is available in the extracellular environment and elicits immune modulation such as T cell apoptosis by being used as the substrate of cell surface ADP-ribosyl transferase. However, it is unclear whether extracellular NAD affects function of macrophages expressing cell surface ADP-ribosyl transferase. Here we show that extracellular NAD enhances Fcgamma receptor (FcgammaR)-mediated phagocytosis in J774A.1 macrophages via the conversion into cyclic ADP-ribose (cADPR), a potent calcium mobilizer, by CD38, an ADP-ribosyl cyclase. Extracellular NAD increased the phagocytosis of IgG-coated sheep red blood cells (IgG-SRBC) in J774A.1 macrophages, which was completely abolished by pretreatment of 8-bromo-cADPR, an antagonist of cADPR, or CD38 knockdown. Extracellular NAD increased basal intracellular Ca(2+) concentration, which also was abolished by pretreatment of 8-bromo-cADPR or CD38 knockdown. Moreover, the chelation of intracellular calcium abolished NAD-induced enhancement of phagocytosis of IgG-SRBC. Our results suggest that extracellular NAD act as a regulator for FcgammaR-mediated phagocytosis in macrophages.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD38,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic ADP-Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1090-2104
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pubmed:author |
pubmed-author:ChungWeon-GuuWG,
pubmed-author:HanMyung-KwanMK,
pubmed-author:KimJong-SukJS,
pubmed-author:KimUh-HyunUH,
pubmed-author:LeeSeung-JinSJ,
pubmed-author:LeeYoung-RaeYR,
pubmed-author:ParkKwang-HyunKH,
pubmed-author:ParkYeong-MinYM,
pubmed-author:RahSo-YoungSY,
pubmed-author:ShimIn-KyungIK,
pubmed-author:SongEun-KyungEK,
pubmed-author:YuHong-NuHN
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
367
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
156-61
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pubmed:meshHeading |
pubmed-meshheading:18166151-Animals,
pubmed-meshheading:18166151-Antigens, CD38,
pubmed-meshheading:18166151-Biological Transport,
pubmed-meshheading:18166151-Calcium,
pubmed-meshheading:18166151-Cells, Cultured,
pubmed-meshheading:18166151-Cyclic ADP-Ribose,
pubmed-meshheading:18166151-Extracellular Space,
pubmed-meshheading:18166151-Immunoglobulin G,
pubmed-meshheading:18166151-Macrophages,
pubmed-meshheading:18166151-Mice,
pubmed-meshheading:18166151-NAD,
pubmed-meshheading:18166151-Phagocytosis,
pubmed-meshheading:18166151-Receptors, IgG
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pubmed:year |
2008
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pubmed:articleTitle |
Extracellular NAD is a regulator for FcgammaR-mediated phagocytosis in murine macrophages.
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pubmed:affiliation |
Department of Microbiology and Immunology, Chonbuk National University Medical School, Jeonju 561-182, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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