NAADP Controls Cross-talk between Distinct Ca2+ Stores in the Heart

Macgregor, A; Yamasaki, Michiko; Rakovic, Stevan; Sanders, Luke; Parkesh, Raman; Churchill, Grant C.; Galione, Antony; Terrar, Derek A.

doi:10.1074/jbc.m611167200

Cited by 100 publications

(172 citation statements)

References 33 publications

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“…Thus, NAADP does not appear to mediate intracellular Ca 2ϩ signals by activating either RyR1 or RyR3, and previous studies on ventricular myocytes have demonstrated quite conclusively that NAADP does not directly activate RyR2 (33). It would therefore appear that NAADP is inca- pable of activating RyRs, at least at physiologically relevant concentrations.…”

Section: Discussionmentioning

confidence: 73%

Cyclic Adenosine Diphosphate Ribose Activates Ryanodine Receptors, whereas NAADP Activates Two-pore Domain Channels

Ogunbayo

Zhu

Rossi

et al. 2011

Journal of Biological Chemistry

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The mechanism by which cyclic adenosine diphosphate ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize intracellular Ca 2؉ Intracellular Ca 2ϩ signals are initiated by Ca 2ϩ release from intracellular stores, and traditionally, the sarco/endoplasmic reticulum (S/ER) 2 has been considered to be the major releasable store. From this store, Ca 2ϩ may be released through the opening of inositol 1,4,5-trisphosphate receptors (IP 3 Rs) and/or ryanodine receptors (RyRs), the two groups of intracellular Ca 2ϩ release channels located on S/ER membranes. It is generally accepted that of the recognized Ca 2ϩ -mobilizing second messengers, inositol 1,4,5-trisphosphate facilitates this process by activating IP 3 Rs (1).By contrast, the mechanism by which the pyridine nucleotides cyclic adenosine diphosphate ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) (2) mobilize intracellular Ca 2ϩ stores remains controversial. Although a wealth of evidence across a variety of cell types (3-9) supports the original proposal that cADPR activates RyRs (10), studies on reconstituted RyRs in lipid bilayers have failed to conclusively demonstrate direct regulation of these channels by cADPR (11), and it has been suggested that cADPR may initiate Ca 2ϩ signals via RyRs and IP 3 Rs by promoting Ca 2ϩ uptake into the S/ER by S/ER Ca 2ϩ ATPases (SERCA) (12)(13)(14). This proposal has not been effectively countered by studies on ventricular myocytes, which exclusively express RyR2. This is due to the fact that the principal regulatory effect of cADPR with respect to RyR2 is to increase the sensitivity of this RyR subtype to Ca 2ϩ -induced Ca 2ϩ release (8, 9), and in light of the fact that the sensitivity of RyRs to Ca 2ϩ -induced Ca 2ϩ release may be augmented by an increase in Ca 2ϩ concentration within the cytoplasm and/or S/ER lumen (15).The mechanism by which NAADP triggers intracellular Ca 2ϩ release has also been hotly debated. We recently identified a family of two-pore domain channels (TPC1-3, TPCN1-3 for gene name) as endolysosome-targeted, NAADP-gated Ca 2ϩ release channels (16, 17), and our findings have since been confirmed by others (18,19

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Section: Discussionmentioning

confidence: 73%

Cyclic Adenosine Diphosphate Ribose Activates Ryanodine Receptors, whereas NAADP Activates Two-pore Domain Channels

Ogunbayo

Zhu

Rossi

et al. 2011

Journal of Biological Chemistry

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“…Both, C2C12 myoblasts and primary murine myoblasts show an increased expression of transcripts that are part of the myogenic differentiation program, such as myogenin and skNAC, when differentiated in the presence of NAADP-AM. On the other hand, both bafilomycin, an inhibitor of the lysosomal H + -ATPase, which is known to inhibit NAADP-dependent calcium release in a number of cell types (33)(34)(35), and Ned-19, a highly selective inhibitor of the NAADP signaling pathway (19,36,37), prevent expression of these transcripts and inhibits the formation of myotubes positive for myosin heavy chain. Taken together, these results are unique in showing that calcium release triggered by NAADP is essential of skeletal muscle differentiation.…”

Section: Discussionmentioning

confidence: 99%

Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels

Aley

Mikołajczyk

Munz

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Calcium signaling is essential for the differentiation of many cell types, including skeletal muscle cells, but its mechanisms remain elusive. Here we demonstrate a crucial role for nicotinic acid adenine dinucleotide phosphate (NAADP) signaling in skeletal muscle differentiation. Although the inositol trisphosphate pathway may have a partial role to play in this process, the ryanodine signaling cascade is not involved. In both skeletal muscle precursors and C2C12, cells interfering with NAADP signaling prevented differentiation, whereas promoting NAADP signaling potentiated differentiation. Moreover, siRNA knockdown of two-pore channels, the target of NAADP, attenuated differentiation. The data presented here strongly suggest that in myoblasts, NAADP acts at acidic organelles on the recently discovered two-pore channels to promote differentiation.

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“…Therefore, important modules of this signaling system are the target organelle and target Ca (20,21). Although RyR are assumed to be localized at the ER (or SR), suggesting that the NAADP-sensitive Ca 2ϩ pool is located there, convincing data from other cell systems, including sea urchin eggs (10, 11), pancreatic acinar-and ␤-cells (33), neurosecretory PC12 cells (34), and guinea pig cardiac myocytes (35), prompted us to investigate involvement of a lysosomal Ca 2ϩ store in NAADP-mediated Ca 2ϩ signaling in T cells. The first approach, lysis of lysosomes using the cathepsin substrate GPN, has successfully been used in sea urchin eggs (11) and pancreatic acinar cells (33); in sea urchin eggs, GPN-mediated bursting of lysosomes selectively abolished Ca 2ϩ signaling by NAADP but not by InsP 3 or cADPR (11).…”

Section: Discussionmentioning

confidence: 98%

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

Steen

Kirchberger

Guse

2007

Journal of Biological Chemistry

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NAADP Controls Cross-talk between Distinct Ca2+ Stores in the Heart

Cited by 100 publications

References 33 publications

Cyclic Adenosine Diphosphate Ribose Activates Ryanodine Receptors, whereas NAADP Activates Two-pore Domain Channels

Cyclic Adenosine Diphosphate Ribose Activates Ryanodine Receptors, whereas NAADP Activates Two-pore Domain Channels

Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels

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

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