NAADP Mobilizes Calcium from the Endoplasmic Reticular Ca2+ Store in T-lymphocytes

Steen, Mareike; Kirchberger, Tanja; Guse, Andreas H.

doi:10.1074/jbc.m610925200

Cited by 69 publications

(37 citation statements)

References 36 publications

(51 reference statements)

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“…At odds with the notion that NAADP activates a novel channel located on acidic organelles, several reports concluded instead that NAADP mobilized Ca 2+ from the ER through direct activation of ryanodine receptors (Hohenegger et al, 2002; Gerasimenko et al, 2003; Steen et al, 2007). An effect of NAADP on plasma membrane TRPM2 channels was also reported (Beck et al, 2006).…”

Section: Two-pore Channels As Naadp-sensitive Ca2+ Channelsmentioning

confidence: 97%

The Molecular Basis for Ca2+ Signalling by NAADP: Two-Pore Channels in a Complex?

Marchant¹,

Lin-Moshier²,

Walseth³

et al. 2012

messenger

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NAADP is a potent Ca2+ mobilizing messenger in a variety of cells but its molecular mechanism of action is incompletely understood. Accumulating evidence indicates that the poorly characterized two-pore channels (TPCs) in animals are NAADP sensitive Ca2+-permeable channels. TPCs localize to the endo-lysosomal system but are functionally coupled to the better characterized endoplasmic reticulum Ca2+ channels to generate physiologically relevant complex Ca2+ signals. Whether TPCs directly bind NAADP is not clear. Here we discuss the idea based on recent studies that TPCs are the pore-forming subunits of a protein complex that includes tightly associated, low molecular weight NAADP-binding proteins.

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Section: Two-pore Channels As Naadp-sensitive Ca2+ Channelsmentioning

confidence: 97%

The Molecular Basis for Ca2+ Signalling by NAADP: Two-Pore Channels in a Complex?

Marchant¹,

Lin-Moshier²,

Walseth³

et al. 2012

messenger

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“…In a number of reports we demonstrated that endogenous NAADP was formed upon stimulation of the T cell receptor (TCR)/CD3 complex (Gasser et al, 2006),RyR are necessary for both global and local Ca 2+ release (Langhorst et al, 2004; Dammermann and Guse 2005), andNAADP evoked Ca 2+ release was not blocked by the V-ATPase inhibitor bafilomycin A1 (Steen et al, 2007). …”

Section: Introductionmentioning

confidence: 99%

“…NAADP evoked Ca 2+ release was not blocked by the V-ATPase inhibitor bafilomycin A1 (Steen et al, 2007). …”

Section: Introductionmentioning

confidence: 99%

Nicotinic Acid Adenine Dinucleotide 2 -Phosphate (NAADP) Binding Proteins in T-Lymphocytes

Walseth¹,

Lin-Moshier²,

Weber³

et al. 2012

messenger

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Nicotinic acid adenine dinucleotide phosphate (NAADP) is a messenger that regulates calcium release from intracellular acidic stores. Although several channels, including two-pore channels (TPC), ryanodine receptor (RYR) and mucolipin (TRP-ML1) have been implicated in NAADP regulation of calcium signaling, the NAADP receptor has not been identified. In this study, the photoaffinity probe, [32P]–5-azido-NAADP ([32P]–5-N3-NAADP), was used to study NAADP binding proteins in extracts from NAADP responsive Jurkat T-lymphocytes. [32P]–5-N3-NAADP photolabeling of Jurkat S100 cytosolic fractions resulted in the labeling of at least ten distinct proteins. Several of these S100 proteins, including a doublet at 22/23 kDa and small protein at 15 kDa displayed selectivity for NAADP as the labeling was protected by inclusion of unlabeled NAADP, whereas the structurally similar NADP required much higher concentrations for protection. Interestingly, the labeling of several S100 proteins (60, 45, 33 and 28 kDa) was stimulated by low concentrations of unlabeled NAADP, but not by NADP. The effect of NAADP on the labeling of the 60 kDa protein was biphasic, peaking at 100 nM with a five-fold increase and displaying no change at 1 µM NAADP. Several proteins were also photolabeled when the P100 membrane fraction from Jurkat cells was examined. Similar to the results with S100, a 22/23 kDa doublet and a 15 kDa protein appeared to be selectively labeled. NAADP did not increase the labeling of any P100 proteins as it did in the S100 fraction. The photolabeled S100 and P100 proteins were successfully resolved by two-dimensional gel electrophoresis. [32P]–5-N3-NAADP photolabeling and two-dimensional electrophoresis should represent a suitable strategy in which to identify and characterize NAADP binding proteins.

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“…In sea urchin eggs, NAADP releases Ca 2ϩ from acidic Ca 2ϩ stores, lysosome-related organelles (20). However, NAADP can also release Ca 2ϩ from the endoplasmic reticulum (21)(22)(23).…”

mentioning

confidence: 99%

Generation of Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate by CD38 for Ca2+ Signaling in Interleukin-8-treated Lymphokine-activated Killer Cells

Rah

Mushtaq

Nam

et al. 2010

Journal of Biological Chemistry

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We have previously demonstrated that cyclic ADP-ribose (cADPR) is a calcium signaling messenger in interleukin 8 (IL-8)-induced lymphokine-activated killer (LAK) cells. In this study we examined the possibility that IL-8 activates CD38 to produce another messenger, nicotinic acid adenine dinucleotide phosphate (NAADP), in LAK cells, and we showed that IL-8 induced NAADP formation after cADPR production. These calcium signaling messengers were not produced when LAK cells prepared from CD38 knock-out mice were treated with IL-8, indicating that the synthesis of both NAADP and cADPR is catalyzed by CD38 in LAK cells. Application of cADPR to LAK cells induced NAADP production, whereas NAADP failed to increase intracellular cADPR levels, confirming that the production of cADPR precedes that of NAADP in IL-8-treated LAK cells. Moreover, NAADP increased intracellular Ca 2؉ signaling as well as cell migration, which was completely blocked by bafilomycin A1, suggesting that NAADP is generated in lysosome-related organelles after cADPR production. A type II transmembrane protein, CD38, possesses ADP-ribosyl cyclase (ADPR cyclase) 3 and cyclic ADP-ribose hydrolase (cADPR hydrolase) activity (1, 2). These two enzyme activities are involved in the conversion of ␤-nicotinamide adenine dinucleotide (␤-NAD ϩ ) first to cADPR and then to ADPR (3-5). The metabolite cADPR is known to increase intracellular Ca 2ϩ concentration, [Ca 2ϩ ] i , by releasing Ca 2ϩ from intracellular stores or by Ca 2ϩ influx through plasma membrane Ca 2ϩ channels in a variety of cells (6 -10). It was shown that CD38 can also synthesize NAADP from NADP in the presence of nicotinic acid by a base exchange reaction in vitro (11). However, it still remains unclear whether the base exchange reaction occurs physiologically as intracellular nicotinic acid concentration is less than the millimolar concentration that is required for the enzymatic synthesis of nicotinic acid adenine dinucleotide phosphate (NAADP) in vitro (12).NAADP is a potent Ca 2ϩ -releasing messenger in a variety of cell types, including mammalian cells (13-15). Although D-myo-inositol 1,4,5-trisphosphate (IP 3 ) and cADPR are firmly established as secondary Ca 2ϩ messengers, receptor-mediated formation of NAADP has been shown in a limited number of cellular systems (16 -18). It has been demonstrated that NAADP triggers Ca 2ϩ release from thapsigargin-insensitive Ca 2ϩ stores through the activation of channels distinct from those sensitive to ryanodine and IP 3 (19). In sea urchin eggs, NAADP releases Ca 2ϩ from acidic Ca 2ϩ stores, lysosome-related organelles (20). However, NAADP can also release Ca 2ϩ from the endoplasmic reticulum (21-23).Previously, we have reported that IL-8 stimulated cADPR formation by activation of CD38 via cGMP/protein kinase G and induced an increase of [Ca 2ϩ ] i and migration of LAK cells (24). In this study we investigated whether NAADP is involved in IL-8-induced Ca 2ϩ signaling and migration of LAK cells. We showed that NAADP plays a key role in IL-8-stimul...

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NAADP Mobilizes Calcium from the Endoplasmic Reticular Ca2+ Store in T-lymphocytes

Cited by 69 publications

References 36 publications

The Molecular Basis for Ca<SUP>2</SUP><SUP>+</SUP> Signalling by NAADP: Two-Pore Channels in a Complex?

The Molecular Basis for Ca<SUP>2</SUP><SUP>+</SUP> Signalling by NAADP: Two-Pore Channels in a Complex?

Nicotinic Acid Adenine Dinucleotide 2 -Phosphate (NAADP) Binding Proteins in T-Lymphocytes

Generation of Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate by CD38 for Ca2+ Signaling in Interleukin-8-treated Lymphokine-activated Killer Cells

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