scholarly journals Second Messenger Function of Nicotinic Acid Adenine Dinucleotide Phosphate Revealed by an Improved Enzymatic Cycling Assay

2006 ◽  
Vol 281 (25) ◽  
pp. 16906-16913 ◽  
Author(s):  
Andreas Gasser ◽  
Sören Bruhn ◽  
Andreas H. Guse
2007 ◽  
Vol 364 (2) ◽  
pp. 97-103 ◽  
Author(s):  
Fumihiko Yamaguchi ◽  
Toshihisa Ohshima ◽  
Haruhiko Sakuraba

2015 ◽  
Vol 43 (3) ◽  
pp. 384-389 ◽  
Author(s):  
Anthony J. Morgan ◽  
Lianne C. Davis ◽  
Margarida Ruas ◽  
Antony Galione

The Ca2+-mobilizing second messenger, NAADP (nicotinic acid adenine dinucleotide phosphate), has been with us for nearly 20 years and yet we still cannot fully agree on the identity of its target Ca2+-release channel. In spite of some recent robust challenges to the idea that two-pore channels (TPCs) represent the elusive “NAADP receptor”, evidence continues to accumulate that TPCs are important for NAADP-mediated responses. This article will briefly outline the background and review more recent work pertaining to the TPC story.


2013 ◽  
Vol 453 (1) ◽  
pp. e1-e2 ◽  
Author(s):  
Andreas H. Guse

NAADP (nicotinic acid–adenine dinucleotide phosphate) is the most potent Ca2+-releasing second messenger known to date. Since its discovery in 1995 identifying the NAADP receptor protein/Ca2+ channel has been a major persuit of the Ca2+ signalling community. In their paper ‘The N-terminal region of two-pore channel 1 regulates trafficking and activation by NAADP’ published in this issue of the Biochemical Journal Patel and colleagues describe that the N-terminus of one of the NAADP receptor protein/Ca2+ channel candidates, TPC1 (two-pore channel 1), is crucial for protein targeting and for sensitivity to NAADP.


2013 ◽  
Vol 288 (16) ◽  
pp. 10986-10993 ◽  
Author(s):  
Parvinder K. Aley ◽  
Nisha Singh ◽  
G. Cristina Brailoiu ◽  
Eugen Brailoiu ◽  
Grant C. Churchill

2002 ◽  
Vol 362 (1) ◽  
pp. 125-130 ◽  
Author(s):  
Eduardo N. CHINI ◽  
Claudia C. S. CHINI ◽  
Ichiro KATO ◽  
Shin TAKASAWA ◽  
Hiroshi OKAMOTO

In the present study, we have determined the role of the enzyme CD38 upon the synthesis of the Ca2+-releasing nucleotide nicotinic acid—adenine dinucleotide phosphate (NAADP). In rat tissues, we observed that the capacity for NAADP synthesis could be co-immunoprecipitated with CD38 using an anti-CD38 antibody. Furthermore, we observed that several tissues from CD38 knockout mice had no capacity for the synthesis of this nucleotide. In addition, CD38 was also identified as the major enzyme responsible for the synthesis of the second messenger cyclic ADP-ribose. These observations lead to the conclusion that CD38 is the major enzyme responsible for the synthesis of NAADP and cyclic ADP-ribose, and raises the possibility of a new signalling pathway where two different Ca2+-releasing nucleotides are synthesized by the same enzyme.


2002 ◽  
Vol 282 (6) ◽  
pp. C1191-C1198 ◽  
Author(s):  
Eduardo N. Chini ◽  
Frederico G. S. De Toledo

Nicotinic acid adenine dinucleotide phosphate (NAADP) is one of the most potent stimulators of intracellular Ca2+ release known to date. The role of the NAADP system in physiological processes is being extensively investigated at the present time. Exciting new discoveries in the last 5 years suggest that the NAADP-regulated system may have a significant role in intracellular Ca2+ signaling. The NAADP receptor and its associated Ca2+ pool have been hypothesized to be important in several physiological processes including fertilization, T cell activation, and pancreatic secretion. However, whether NAADP is a new second messenger or a tool for the discovery of a new Ca2+ channel is still an unanswered question.


2009 ◽  
Vol 422 (3) ◽  
pp. 503-512 ◽  
Author(s):  
Vinita Pandey ◽  
Chia-Chen Chuang ◽  
Alexander M. Lewis ◽  
Parvinder K. Aley ◽  
Eugen Brailoiu ◽  
...  

NAADP (nicotinic acid–adenine dinucleotide phosphate) is an unusual second messenger thought to mobilize acidic Ca2+ stores, such as lysosomes or lysosome-like organelles, that are functionally coupled to the ER (endoplasmic reticulum). Although NAADP-sensitive Ca2+ stores have been described in neurons, the physiological cues that recruit them are not known. Here we show that in both hippocampal neurons and glia, extracellular application of glutamate, in the absence of external Ca2+, evoked cytosolic Ca2+ signals that were inhibited by preventing organelle acidification or following osmotic bursting of lysosomes. The sensitivity of both cell types to glutamate correlated well with lysosomal Ca2+ content. However, interfering with acidic compartments was largely without effect on the Ca2+ content of the ER or Ca2+ signals in response to ATP. Glutamate but not ATP elevated cellular NAADP levels. Our results provide evidence for the agonist-specific recruitment of NAADP-sensitive Ca2+ stores by glutamate. This links the actions of NAADP to a major neurotransmitter in the brain.


2021 ◽  
Vol 14 (675) ◽  
pp. eabd5605 ◽  
Author(s):  
Gihan S. Gunaratne ◽  
Eugen Brailoiu ◽  
Shijun He ◽  
Ellen M. Unterwald ◽  
Sandip Patel ◽  
...  

Nicotinic acid adenine dinucleotide phosphate (NAADP) is a second messenger that releases Ca2+ from acidic organelles through the activation of two-pore channels (TPCs) to regulate endolysosomal trafficking events. NAADP action is mediated by NAADP-binding protein(s) of unknown identity that confer NAADP sensitivity to TPCs. Here, we used a “clickable” NAADP-based photoprobe to isolate human NAADP-binding proteins and identified Jupiter microtubule-associated homolog 2 (JPT2) as a TPC accessory protein required for endogenous NAADP-evoked Ca2+ signaling. JPT2 was also required for the translocation of a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pseudovirus through the endolysosomal system. Thus, JPT2 is a component of the NAADP receptor complex that is essential for TPC-dependent Ca2+ signaling and control of coronaviral entry.


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