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

Chini, Eduardo N.

doi:10.1590/s0100-879x2002000500005

Cited by 7 publications

(5 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A complex coordination of extracellular Ca 2ϩ and intracellular messengers appears to be fundamental for the oxytocin-induced Ca 2ϩ transients in human myometrial cells. Similar interactions between Ca 2ϩ pools have been described previously (19,20,24). We postulated that the cADPR system regulates the Ca 2ϩ -induced Ca 2ϩ release mediated by the RyR and augments the intracellular Ca 2ϩ transient possibly initiated by extracellular Ca 2ϩ influx or activation of the IP 3 -receptor.…”

Section: Role Of the Cadpr-signaling Pathway In Oxytocin-induced Ca 2supporting

confidence: 73%

The Role of Cyclic-ADP-Ribose-Signaling Pathway in Oxytocin-Induced Ca2+ Transients in Human Myometrium Cells

et al. 2004

View full text Add to dashboard Cite

Human myometrial contraction plays a fundamental role in labor. Dysfunction of uterine contraction is an important cause of labor progression failure. Although the mechanisms controlling uterine contraction are not completely understood, intracellular Ca2+ mobilization plays an important role during uterine contraction. Several mechanisms of intracellular Ca2+ mobilization are present in smooth muscle, but in the human uterus, only 1,4,5-trisphosphate-induced Ca2+ release has been studied extensively. Ryanodine receptor channels are present in myometrium. We determined the role of the cyclic ADP-ribose (cADPR)-signaling pathway in oxytocin-induced intracellular Ca2+ [(Ca2+)i] transients in human myometrial cells. We found that oxytocin-induced Ca2+ transient is dependent on several sources of Ca2+, including extracellular Ca2+ and intracellular Ca2+ stores. In addition, we found that both the 1,4,5-trisphosphate- and the cADPR-induced Ca2+ releasing systems are important for the induction of [Ca2+]i transients by oxytocin in human myometrial cells. Furthermore, we investigated TNFalpha regulation of oxytocin-induced [Ca2+]i transients, CD38 cyclase activity, and CD38 expression in human myometrial cells. We found that oxytocin-induced [Ca2+]i transients were significantly increased by 50 ng/ml TNF. Similarly, CD38 mRNA levels, CD38 expression, and cyclase activity were increased by TNFalpha, thus increasing cADPR levels. We propose that a complex interaction between multiple signaling pathways is important for the development of intracellular Ca2+ transients induced by oxytocin and that TNFalpha may contribute for the myometrium preparation for labor by regulating the cADPR-signaling pathway. The observation that the cADPR-signaling pathway is important for the development of intracellular Ca2+ transients in human myometrial cells raises the possibility that this signaling pathway could serve as a target for the development of new therapeutic strategies for abnormal myometrial contraction observed during pregnancy.

show abstract

Section: Role Of the Cadpr-signaling Pathway In Oxytocin-induced Ca 2supporting

confidence: 73%

The Role of Cyclic-ADP-Ribose-Signaling Pathway in Oxytocin-Induced Ca2+ Transients in Human Myometrium Cells

et al. 2004

View full text Add to dashboard Cite

show abstract

Section: Cyclic-adp-ribose Induced Ca 2؉ Releasementioning

confidence: 99%

“…cADPR-induced Ca 2ϩ release was determined in sea urchin egg homogenates using fluo-3 as a Ca 2ϩ indicator as extensively described before (14). Homogenates from Lytechinus pictus egg were prepared as described previously (14). Frozen homogenates were thawed in a 17°C water bath and diluted to 1.25% with an intracellular medium containing 250 mM N-methyl glutamine, 250 mM potassium gluconate, 20 mM HEPES buffer, pH 7.2, 1 mM MgCl 2 , 2 U/ml creatine kinase, 4 mM phosphocreatine, 1 mM ATP, 3 g/ml oligomycin, and 3 g/ml antimycin.…”

Section: Cyclic-adp-ribose Induced Ca 2؉ Releasementioning

confidence: 99%

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

Barbosa¹,

Soares²,

Novak³

et al. 2007

FASEB j.

228

230

View full text Add to dashboard Cite

Obesity is one of the major health problems of our times. Elucidating the signaling mechanisms by which high-fat caloric diet induces obesity is critical for the understanding of this condition and for the development of therapeutic strategies for its treatment. Here, we demonstrate a novel role for protein CD38 as a regulator of body weight during a high-fat diet. CD38 is a ubiquitous enzyme that catalyzes the synthesis of second messengers and has been implicated in the regulation of a wide variety of signaling pathways. We report that CD38-deficient mice are protected against high-fat diet-induced obesity owing to enhanced energy expenditure. In fact, calorimetric studies indicate that CD38-deficient animals have a higher metabolic rate compared to control mice. Analysis of the mechanism revealed that this resistance to diet-induced obesity is mediated at least in part via a NAD-dependent activation of SIRT-PGC1alpha axis, a well-established cascade, involved in the regulation of mitochondrial biogenesis and energy homeostasis. Thus, together these results identify a novel pathway regulating body weight and clearly show that CD38 is a nearly obligatory component of the cellular cascade that led to diet-induced obesity.

show abstract

“…According to the cell type or phase of development, two Ca pools with different functional properties are formed, which are defined by specific activating agonists such as IP 3 , cADP-ribose, NAADP, ryanodine, and caffeine. These Ca pools are interconvertible and partially overlapping (Turner et al, 2001;Chini, 2002). 8.…”

Section: Main Characteristics Of Ca Signalingmentioning

confidence: 99%

“…In the pumping vesicle picture, the explanation for interconversion and overlapping of different Ca stores (Turner et al, 2001;Chini, 2002) is rather controversial because those vesicles equipped with both Ca channel types would not display separated release properties but would be emptied regardless whether stimulated by IP 3 or ryanodine. On the other side, different vesicle populations equipped with only one type of release channels cannot explain interconversion of the pools.…”

Section: Cooperative Binding Of Cofilin and Gelsolin To F-actinmentioning

confidence: 99%

F‐actin‐based Ca signaling—a critical comparison with the current concept of Ca signaling

Lange¹,

Gartzke²

2006

Journal Cellular Physiology

View full text Add to dashboard Cite

A short comparative survey on the current idea of Ca signaling and the alternative concept of F-actin-based Ca signaling is given. The two hypotheses differ in one central aspect, the mechanism of Ca storage. The current theory rests on the assumption of Ca-accumulating endoplasmic/sarcoplasmic reticulum-derived vesicles equipped with an ATP-dependent Ca pump and IP3- or ryanodine-sensitive channel-receptors for Ca-release. The alternative hypothesis proceeds from the idea of Ca storage at the high-affinity binding sites of actin filaments. Cellular sites of F-actin-based Ca storage are microvilli and the submembrane cytoskeleton. Several specific features of Ca signaling such as store-channel coupling, quantal Ca release, spiking and oscillations, biphasic and "phasic" uptake kinetics, and Ca-induced Ca release (CICR), which are not adequately described by the current concept, are inherent properties of the F-actin system and its dynamic state of treadmilling.

show abstract

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

Cited by 7 publications

References 23 publications

The Role of Cyclic-ADP-Ribose-Signaling Pathway in Oxytocin-Induced Ca2+ Transients in Human Myometrium Cells

The Role of Cyclic-ADP-Ribose-Signaling Pathway in Oxytocin-Induced Ca2+ Transients in Human Myometrium Cells

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

F‐actin‐based Ca signaling—a critical comparison with the current concept of Ca signaling

Contact Info

Product

Resources

About