CD38-cADPR-SERCA Signaling Axis Determines Skeletal Muscle Contractile Force in Response to β-Adrenergic Stimulation

Park, Dae-Ryoung; Nam, Tae-Sik; Kim, Ye-Won; Lee, Seo-Ho; Kim, Uh-Hyun

doi:10.1159/000489441

Cited by 15 publications

(8 citation statements)

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“…If this is the case, then the action of maurocalcine (see above) lends support to the view that a critical factor in the selection of vasoconstriction over vasodilation might be the capacity of a vasoconstrictor to pre-load the SR prior to RyR activation [ 113 , 199 , 200 , 202 , 203 ]. In this respect it is worth noting that the studies of others have suggested that cADPR might act to accelerate SR-filling by activating SERCA [ 204 , 205 , 206 ], although our studies have revealed no clear evidence of this [ 109 ]. Such an action could provide an alternative explanation for the all-or-none block of HPV by 8-bromo-cADPR, if 8-bromo-cADPR blocks the initiation of HPV by inhibiting the activity of both SERCA and RyR1, 2 and 3.…”

Section: China Girl: How the Cell-wide Web Was Weavedcontrasting

confidence: 57%

On a Magical Mystery Tour with 8-Bromo-Cyclic ADP-Ribose: From All-or-None Block to Nanojunctions and the Cell-Wide Web

Evans

2020

Molecules

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A plethora of cellular functions are controlled by calcium signals, that are greatly coordinated by calcium release from intracellular stores, the principal component of which is the sarco/endooplasmic reticulum (S/ER). In 1997 it was generally accepted that activation of various G protein-coupled receptors facilitated inositol-1,4,5-trisphosphate (IP3) production, activation of IP3 receptors and thus calcium release from S/ER. Adding to this, it was evident that S/ER resident ryanodine receptors (RyRs) could support two opposing cellular functions by delivering either highly localised calcium signals, such as calcium sparks, or by carrying propagating, global calcium waves. Coincidentally, it was reported that RyRs in mammalian cardiac myocytes might be regulated by a novel calcium mobilising messenger, cyclic adenosine diphosphate-ribose (cADPR), that had recently been discovered by HC Lee in sea urchin eggs. A reputedly selective and competitive cADPR antagonist, 8‑bromo‑cADPR, had been developed and was made available to us. We used 8‑bromo‑cADPR to further explore our observation that S/ER calcium release via RyRs could mediate two opposing functions, namely pulmonary artery dilation and constriction, in a manner seemingly independent of IP3Rs or calcium influx pathways. Importantly, the work of others had shown that, unlike skeletal and cardiac muscles, smooth muscles might express all three RyR subtypes. If this were the case in our experimental system and cADPR played a role, then 8‑bromo‑cADPR would surely block one of the opposing RyR-dependent functions identified, or the other, but certainly not both. The latter seemingly implausible scenario was confirmed. How could this be, do cells hold multiple, segregated SR stores that incorporate different RyR subtypes in receipt of spatially segregated signals carried by cADPR? The pharmacological profile of 8‑bromo‑cADPR action supported not only this, but also indicated that intracellular calcium signals were delivered across intracellular junctions formed by the S/ER. Not just one, at least two. This article retraces the steps along this journey, from the curious pharmacological profile of 8‑bromo‑cADPR to the discovery of the cell-wide web, a diverse network of cytoplasmic nanocourses demarcated by S/ER nanojunctions, which direct site-specific calcium flux and may thus coordinate the full panoply of cellular processes.

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Section: China Girl: How the Cell-wide Web Was Weavedcontrasting

confidence: 57%

On a Magical Mystery Tour with 8-Bromo-Cyclic ADP-Ribose: From All-or-None Block to Nanojunctions and the Cell-Wide Web

Evans

2020

Molecules

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“…In addition to NAADP, ARCs have also been suggested to generate the Ca 2+ mobilizing messenger cADPR, which targets ryanodine receptors (RyRs) located on the E/SR (Lee, 2011; 2012). The role of the cADPR or RyR in mediating the Ca 2+ signaling during the differentiation and function of skeletal muscle cells have previously been reported (Brennan et al, 2005; Cheung et al, 2011; Park et al, 2018). Thus, it is possible that following ARC1-like-inhibition or knockdown, the defects in slow muscle cell development observed, might be due to a combinatorial effect of the loss of both cADPR/RyR/Ca 2+ signaling and NAADP/TPC2/Ca 2+ signaling.…”

Section: Discussionmentioning

confidence: 94%

Characterization of ADP-ribosyl cyclase 1-like (ARC1-like) activity and NAADP signaling during slow muscle cell development in zebrafish embryos

Kelu

Webb

Galione

et al. 2019

Developmental Biology

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We recently demonstrated the requirement of two-pore channel type 2 (TPC2)-mediated Ca2+ release during slow muscle cell differentiation and motor circuit maturation in intact zebrafish embryos. However, the upstream trigger of TPC2/Ca2+ signaling during these developmental processes remains unclear. Nicotinic acid adenine dinucleotide phosphate (NAADP) is a potent Ca2+ mobilizing messenger, which is suggested to target TPC2 in mediating the release of Ca2+ from acidic vesicles. Here, we report the molecular cloning of the zebrafish ADP ribosyl cyclase (ARC) homolog (i.e., ARC1-like), which is the putative enzyme for generating NAADP. We characterized the expression of the arc1-like transcript and the NAADP level between ~16 hours post-fertilization (hpf) and ~48 hpf in whole zebrafish embryos. We showed that when ARC1-like was fused with either EGFP or tdTomato, it was localized in the plasma membrane, and associated with intracellular organelles, such as the acidic vesicles, Golgi complex and sarcoplasmic reticulum, in primary muscle cell cultures. Morpholino (MO)-mediated knockdown of arc1-like or pharmacological inhibition of ARC1 (via treatment with nicotinamide), led to an attenuation of Ca2+ signaling and disruption of slow muscle cell development. In addition, the injection of arc1-like mRNA into ARC1-like morphants partially rescued the Ca2+ signals and slow muscle cell development. Together, our data might suggest a link between ARC1-like, NAADP, TPC2 and Ca2+ signaling during zebrafish myogenesis.

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“…Ablation of the CD38 gene in mice produces multiple physiological defects (reviewed in Refs. [11][12][13][14], including altering the response of skeletal muscle contractile force to ␤-adrenergic stimulation (31) and impaired development of astrocytes and oligodendrocytes (32), confirming its biological relevance. Gene ablation also provides strong evidence that CD38 is responsible for producing cADPR and NAADP.…”

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confidence: 83%

Resolving the topological enigma in Ca2+ signaling by cyclic ADP-ribose and NAADP

Lee

Zhao

2019

Journal of Biological Chemistry

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Edited by Mike Shipston Cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) are two structurally distinct messengers that mobilize the endoplasmic and endolysosomal Ca 2؉ stores, respectively. Both are synthesized by the CD38 molecule (CD38), which has long been thought to be a type II membrane protein whose catalytic domain, intriguingly, faces to the outside of the cell. Accordingly, for more than 20 years, it has remained unresolved how CD38 can use cytosolic substrates such as NAD and NADP to produce messengers that target intracellular Ca 2؉ stores. The discovery of type III CD38, whose catalytic domain faces the cytosol, has now begun to clarify this topological conundrum. This article reviews the ideas and clues leading to the discovery of the type III CD38; highlights an innovative approach for uncovering its natural existence; and discusses the regulators of its activity, folding, and degradation. We also review the compartmentalization of cADPR and NAADP biogenesis. We further discuss the possible mechanisms that promote type III CD38 expression and appraise a proposal of a Ca 2؉-signaling mechanism based on substrate limitation and product translocation. The surprising finding of another enzyme that produces cADPR and NAADP, sterile ␣ and TIR motif-containing 1 (SARM1), is described. SARM1 regulates axonal degeneration and has no sequence similarity with CD38 but can catalyze the same set of multireactions and has the same cytosolic orientation as the type III CD38. The intriguing finding that SARM1 is activated by nicotinamide mononucleotide to produce cADPR and NAADP suggests that it may function as a regulated Ca 2؉-signaling enzyme like CD38.

show abstract

CD38-cADPR-SERCA Signaling Axis Determines Skeletal Muscle Contractile Force in Response to β-Adrenergic Stimulation

Cited by 15 publications

References 50 publications

On a Magical Mystery Tour with 8-Bromo-Cyclic ADP-Ribose: From All-or-None Block to Nanojunctions and the Cell-Wide Web

On a Magical Mystery Tour with 8-Bromo-Cyclic ADP-Ribose: From All-or-None Block to Nanojunctions and the Cell-Wide Web

Characterization of ADP-ribosyl cyclase 1-like (ARC1-like) activity and NAADP signaling during slow muscle cell development in zebrafish embryos

Resolving the topological enigma in Ca2+ signaling by cyclic ADP-ribose and NAADP

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