Ca2+ release induced by cyclic ADP-ribose

Galione, Antony; White, Alison M.

doi:10.1016/0962-8924(94)90104-x

Cited by 90 publications

(59 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Dnd1 encodes a cyclic nucleotide-gated ion channel (Clough et al, 2000). In mammals, cyclic nucleotides like cGMP or cADP-Rib are second messengers closely associated with NO signaling (Galione and White, 1994;Schmidt and Walter, 1994), and this has been suggested for plants as well (Pfeiffer et al, 1994;Durner et al, 1998;Clarke et al, 2000). It will be of interest to investigate if generation of NO leads to activation of Dnd1, which contributes to the development of symptoms characteristic of the HR.…”

Section: Discussionmentioning

confidence: 99%

Genetic Elucidation of Nitric Oxide Signaling in Incompatible Plant-Pathogen Interactions

et al. 2004

View full text Add to dashboard Cite

Recent experiments indicate that nitric oxide (NO) plays a pivotal role in disease resistance and several other physiological processes in plants. However, most of the current information about the function of NO in plants is based on pharmacological studies, and additional approaches are therefore required to ascertain the role of NO as an important signaling molecule in plants. We have expressed a bacterial nitric oxide dioxygenase (NOD) in Arabidopsis plants and/or avirulent Pseudomonas syringae pv tomato to study incompatible plant-pathogen interactions impaired in NO signaling. NOD expression in transgenic Arabidopsis resulted in decreased NO levels in planta and attenuated a pathogen-induced NO burst. Moreover, NOD expression in plant cells had very similar effects on plant defenses compared to NOD expression in avirulent Pseudomonas. The defense responses most affected by NO reduction during the incompatible interaction were decreased H 2 O 2 levels during the oxidative burst and a blockage of Phe ammonia lyase expression, the key enzyme in the general phenylpropanoid pathway. Expression of the NOD furthermore blocked UV light-induced Phe ammonia lyase and chalcone synthase gene expression, indicating a general signaling function of NO in the activation of the phenylpropanoid pathway. NO possibly functions in incompatible plant-pathogen interactions by inhibiting the plant antioxidative machinery, and thereby ensuring locally prolonged H 2 O 2 levels. Additionally, albeit to a lesser extent, we observed decreases in salicylic acid production, a diminished development of hypersensitive cell death, and a delay in pathogenesis-related protein 1 expression during these NO-deficient plant-pathogen interactions. Therefore, this genetic approach confirms that NO is an important regulatory component in the signaling network of plant defense responses.Plants have evolved several mechanisms to defend themselves from bacterial or fungal invasion. The rapid recognition of pathogenic microbes is based on the interaction of products from a pathogen-derived avirulence gene and a plant-derived resistance gene and represents a prerequisite to specific resistance in incompatible plant-pathogen interactions (Flor, 1956). The multicomponent defense responses associated with specific resistance include a burst of reactive oxygen intermediates (ROI; Lamb and Dixon, 1997), transcriptional activation of defense genes encoding phenylpropanoid pathway enzymes, lytic and antimicrobial pathogenesis-related (PR) proteins (Lamb et al., 1989), increase of intracellular levels of salicylic acid (SA; Malamy et al., 1990; Métraux et al., 1990), and development of the hypersensitive response (HR). The HR results in the rapid appearance of a dry, necrotic lesion at the infection site that is clearly delimited from surrounding healthy tissue and is thought to contribute to the limitation of pathogen spread (Keen, 1990).One of the earliest events following pathogen recognition is a burst of oxidative metabolism leading to the generation of su...

show abstract

Section: Discussionmentioning

confidence: 99%

Genetic Elucidation of Nitric Oxide Signaling in Incompatible Plant-Pathogen Interactions

et al. 2004

View full text Add to dashboard Cite

show abstract

“…Role of cADPR in store-operated Ca 2+ entry cADPR has recently emerged as a second messenger mediating Ca 2+ homeostasis in a variety of cell types by acting as an endogenous modulator of the RyR (8)(9)(10)(11)(12). We have shown that cADPR is important for agonist-stimulated Ca 2+ transients in smooth muscle cells (18)(19)(20)(21).…”

Section: Role Of the Ryr In The Store-operated Ca 2+ Transient Pathwamentioning

confidence: 99%

“…Cyclic-ADP-ribose (cADPR) is a calcium-mobilizing metabolite of ß-NAD. cADPR was initially described as a potent activator of the ryanodine receptor channel (RyR) and as an endogenous modulator of Ca 2+ release from intracellular stores (8)(9)(10)(11)(12). Guse et al (13) were the first to implicate cADPR as a potential activator of Ca 2+ entry in T-lymphocytes.…”

Section: Introductionmentioning

confidence: 99%

Modulation of store-operated Ca2+ entry by cyclic-ADP-ribose

Thompson

White

Chini

2006

Braz J Med Biol Res

View full text Add to dashboard Cite

Store-operated Ca 2+ entry plays an important role in Ca 2+ homeostasis in cells but the mechanisms of control of these channels are not completely understood. We describe an investigation of the role of the CD38-cyclic-ADP-ribose (cADPR)-ryanodine-channel (RyR) signaling pathway in store-operated Ca 2+ entry in human smooth muscle. We observed that human myometrial cells have a functional storeoperated Ca 2+ entry mechanism. Furthermore, we observed the presence of transient receptor potential 1, 3, 4, 5, and 6 ion channels in human myometrial cells. Store-operated Ca 2+ transient was inhibited by at least 50-70% by several inhibitors of the RyR, including ryanodine (10 µM), dantrolene (10 µM), and ruthenium red (10 µM). Furthermore, the cell permeable inhibitor of the cADPR-system, 8-Br-cADPR (100 µM), is a potent inhibitor of the store-operated entry, decreasing the store operated entry by 80%. Pre-incubation of cells with 100 µM cADPR and the hydrolysis-resistant cADPR analog 3-deaza-cADPR (50 µM), but not with ADP-ribose (ADPR) leads to a 1.6-fold increase in the store-operated Ca 2+ transient. In addition, we observed that nicotinamide (1-10 mM), an inhibitor of cADPR synthesis, also leads to inhibition of the store-operated Ca 2+ transient by 50-80%. Finally, we observed that the transient receptor potential channels, RyR, and CD38 can be co-immunoprecipitated, indicating that they interact in vivo. Our observations clearly implicate the CD38-cADPR-ryanodine signaling pathway in the regulation of storeoperated Ca 2+ entry in human smooth muscle cells.

show abstract

“…The release of Ca 2+ from intracellular stores is a widespread component of several signaling pathways (1)(2)(3). Nicotinic acid adenine dinucleotide phosphate (NAADP) is a recently discovered nucleotide with intracellular Ca 2+ -releasing properties (4)(5)(6)(7)(8)(9)(10)(11).…”

Section: Introductionmentioning

confidence: 99%

Interactions between intracellular Ca2+ stores: Ca2+ released from the NAADP pool potentiates cADPR-induced Ca2+ release

Chini

2002

Braz J Med Biol Res

View full text Add to dashboard Cite

Cells possess multiple intracellular Ca 2+ -releasing systems. Sea urchin egg homogenates are a well-established model to study intracellular Ca 2+ release. In the present study the mechanism of interaction between three intracellular Ca 2+ pools, namely the nicotinic acid adenine dinucleotide phosphate (NAADP), the cyclic ADP-ribose (cADPR) and the inositol 1',4',5'-trisphosphate (IP 3 )-regulated Ca 2+ stores, is explored. The data indicate that the NAADP Ca 2+ pool could be used to sensitize the cADPR system. In contrast, the IP 3 pool was not affected by the Ca 2+ released by NAADP. The mechanism of potentiation of the cADPR-induced Ca 2+ release, promoted by Ca 2+ released from the NAADP pool, is mediated by the mechanism of Ca 2+ -induced Ca 2+ release. These data raise the possibility that the NAADP Ca 2+ store may have a role as a regulator of the cellular sensitivity to cADPR.

show abstract

Ca2+ release induced by cyclic ADP-ribose

Cited by 90 publications

References 46 publications

Genetic Elucidation of Nitric Oxide Signaling in Incompatible Plant-Pathogen Interactions

Genetic Elucidation of Nitric Oxide Signaling in Incompatible Plant-Pathogen Interactions

Modulation of store-operated Ca2+ entry by cyclic-ADP-ribose

Interactions between intracellular Ca2+ stores: Ca2+ released from the NAADP pool potentiates cADPR-induced Ca2+ release

Contact Info

Product

Resources

About