Extracellular NAD is a regulator for FcγR-mediated phagocytosis in murine macrophages

Eun Kyung Song; Young Rae Lee; Hong Nu Yu; Uh Hyun Kim; So Young Rah; Kwang Hyun Park; In Kyung Shim; Seung Jin Lee; Yeong Min Park; Weon Guu Chung; Jong Suk Kim; Myung Kwan Han

doi:10.1016/j.bbrc.2007.12.131

Extracellular NAD is a regulator for FcγR-mediated phagocytosis in murine macrophages

Eun Kyung Song, Young Rae Lee, Hong Nu Yu, Uh Hyun Kim, So Young Rah, Kwang Hyun Park, In Kyung Shim, Seung Jin Lee, Yeong Min Park, Weon Guu Chung, Jong Suk Kim, Myung Kwan Han

Department of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

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 Fcγ receptor (FcγR)-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 Ca²⁺ 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 FcγR-mediated phagocytosis in macrophages.

Original language	English
Pages (from-to)	156-161
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	367
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2007.12.131
State	Published - 29 Feb 2008

Bibliographical note

Funding Information:
This work was supported by grants of the Korea Science and Engineering Foundation (Nos. R01-2002-000-00493-0 and M10528010003-05N2801-00310) and the grant of Post-Doc Program, Chonbuk National University (E.-K. Song).

Keywords

Cyclic ADP-ribose
Fcγ receptor
Macrophages
NAD
Phagocytosis

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10.1016/j.bbrc.2007.12.131

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title = "Extracellular NAD is a regulator for FcγR-mediated phagocytosis in murine macrophages",

abstract = "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 Fcγ receptor (FcγR)-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 Ca2+ 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 FcγR-mediated phagocytosis in macrophages.",

keywords = "Cyclic ADP-ribose, Fcγ receptor, Macrophages, NAD, Phagocytosis",

author = "Song, {Eun Kyung} and Lee, {Young Rae} and Yu, {Hong Nu} and Kim, {Uh Hyun} and Rah, {So Young} and Park, {Kwang Hyun} and Shim, {In Kyung} and Lee, {Seung Jin} and Park, {Yeong Min} and Chung, {Weon Guu} and Kim, {Jong Suk} and Han, {Myung Kwan}",

note = "Funding Information: This work was supported by grants of the Korea Science and Engineering Foundation (Nos. R01-2002-000-00493-0 and M10528010003-05N2801-00310) and the grant of Post-Doc Program, Chonbuk National University (E.-K. Song).",

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AU - Song, Eun Kyung

AU - Lee, Young Rae

AU - Yu, Hong Nu

AU - Kim, Uh Hyun

AU - Rah, So Young

AU - Park, Kwang Hyun

AU - Shim, In Kyung

AU - Lee, Seung Jin

AU - Park, Yeong Min

AU - Chung, Weon Guu

AU - Kim, Jong Suk

AU - Han, Myung Kwan

N1 - Funding Information: This work was supported by grants of the Korea Science and Engineering Foundation (Nos. R01-2002-000-00493-0 and M10528010003-05N2801-00310) and the grant of Post-Doc Program, Chonbuk National University (E.-K. Song).

PY - 2008/2/29

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N2 - 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 Fcγ receptor (FcγR)-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 Ca2+ 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 FcγR-mediated phagocytosis in macrophages.

AB - 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 Fcγ receptor (FcγR)-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 Ca2+ 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 FcγR-mediated phagocytosis in macrophages.

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Extracellular NAD is a regulator for FcγR-mediated phagocytosis in murine macrophages

Abstract

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Keywords

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