Extracellular NAD is a regulator for FcgammaR-mediated phagocytosis in murine macrophages
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2008 |
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| Erschienen: |
2008 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:367 |
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| Enthalten in: |
Biochemical and biophysical research communications - 367(2008), 1 vom: 29. Feb., Seite 156-61 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Song, Eun-Kyung [VerfasserIn] |
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| Links: |
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| Themen: |
0U46U6E8UK |
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| Anmerkungen: |
Date Completed 07.03.2008 Date Revised 16.11.2017 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bbrc.2007.12.131 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM176592474 |
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| 100 | 1 | |a Song, Eun-Kyung |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Extracellular NAD is a regulator for FcgammaR-mediated phagocytosis in murine macrophages |
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| 520 | |a 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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| 700 | 1 | |a Lee, Young-Rae |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Hong-Nu |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Uh-Hyun |e verfasserin |4 aut | |
| 700 | 1 | |a Rah, So-Young |e verfasserin |4 aut | |
| 700 | 1 | |a Park, Kwang-Hyun |e verfasserin |4 aut | |
| 700 | 1 | |a Shim, In-Kyung |e verfasserin |4 aut | |
| 700 | 1 | |a Lee, Seung-Jin |e verfasserin |4 aut | |
| 700 | 1 | |a Park, Yeong-Min |e verfasserin |4 aut | |
| 700 | 1 | |a Chung, Weon-Guu |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Jong-Suk |e verfasserin |4 aut | |
| 700 | 1 | |a Han, Myung-Kwan |e verfasserin |4 aut | |
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