scholarly journals Nicotinate-adenine dinucleotide phosphate-induced Ca2+-release does not behave as a Ca2+-induced Ca2+-release system

1996 ◽  
Vol 316 (3) ◽  
pp. 709-711 ◽  
Author(s):  
Eduardo N. CHINI ◽  
Thomas P. DOUSA
Keyword(s):  
Sea Urchin ◽  
The Other ◽  
Release Mechanism ◽  
Inositol 1 ◽  
Release System ◽  
Release Mechanisms ◽  
Sea Urchin Egg ◽  
Wide Range ◽  
Cyclic Adp Ribose ◽  
Regulatory Impact

We investigated the dependence of nicotinate–adenine dinucleotide phosphate (NAADP)-induced Ca2+ release from intracellular stores of sea urchin egg homogenates, upon extravesicular Ca2+. In contrast to the Ca2+ release induced by inositol 1´,4´,5´trisphosphate (IP3) or cyclic ADP-ribose (cADPR), the Ca2+ release induced by NAADP was completely independent of the free extravesicular Ca2+ over a wide range of concentrations (0–0.1 mM). The Ca2+ release triggered by either cADPR or IP3 was biphasically modulated by extravesicular Ca2+, and the Ca2+ release by these agents was abolished when the extravesicular Ca2+ was removed by chelation with 2 mM EGTA. On the other hand, NAADP-triggered Ca2+ release was not influenced by EGTA. These data indicate that while both cADPR and IP3 systems behave as functional Ca2+-induced Ca2+ release mechanisms, NAADP activates a Ca2+ release mechanism which is independent of the presence of extravesicular Ca2+. Therefore, the NAADP-sensitive Ca2+ release mechanisms may have a unique regulatory impact upon intracellular Ca2+ homoeostasis.

Psammechinus miliaris egg homogenate as a model to investigate Ca2+-release mechanisms

1999 ◽  
Vol 79 (2) ◽  
pp. 323-326 ◽  
Author(s):  
Armando A. Genazzani ◽  
Heather L. Wilson ◽  
Antony Galione
Keyword(s):  
Sea Urchin ◽  
Calcium Release ◽  
Lytechinus Pictus ◽  
Release Mechanisms ◽  
Psammechinus Miliaris ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
The Usa ◽  
Release Model ◽  
Convenient Model

The sea urchin egg has proved a reliable and robust system for measuring intracellular calcium release in response to three independent mechanisms: inositol 1,4,5 trisphosphate, cyclic ADP-ribose and the recently identified molecule, nicotinic acid adenine dinucleotide phosphate (NAADP). These calcium release mechanisms have been studied in homogenates of Lytechinus pictus and Spongylocentrotus purpuratus, which are two sea urchin species located off the west coast of the USA. A new calcium-release model from a species of sea urchin present off the coasts of Britain, Psammechinus miliaris is characterized and described. Although the Ca2+-release characteristics in this species do not differ from those of the other two sea urchin species, it may provide a more economical and convenient model for European scientists.

Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose

2000 ◽  
Vol 113 (24) ◽  
pp. 4413-4420 ◽  
Author(s):  
H.C. Lee ◽  
R. Aarhus
Keyword(s):  
Endoplasmic Reticulum ◽  
Sea Urchin ◽  
The Other ◽  
Calcium Stores ◽  
Cellular Functions ◽  
Large Size ◽  
Opposite Pole ◽  
Visual Evidence ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose

Cells possess multiple Ca(2+) stores and their selective mobilization provides the spatial-temporal Ca(2+) signals crucial in regulating diverse cellular functions. Except for the inositol trisphosphate (IP(3))-sensitive Ca(2+) stores, the identities and the mechanisms of how these internal stores are mobilized are largely unknown. In this study, we describe two Ca(2+) stores, one of which is regulated by cyclic ADP-ribose (cADPR) and the other by nicotinic acid adenine dinucleotide phosphate (NAADP). We took advantage of the large size of the sea urchin egg and stratified its organelles by centrifugation. Using photolysis to produce either uniform or localized increases of cADPR and NAADP from their respective caged analogs, the two separate stores could be visually identified by Ca(2+) imaging and shown to be segregated to the opposite poles of the eggs. The cADPR-pole also contained the IP(3)-sensitive Ca(2+) stores, the egg nucleus and the endoplasmic reticulum (ER); the latter was visualized using Bodipy-thapsigargin. On the other hand, the mitochondria, as visualized by rhodamine 123, were segregated to the opposite pole together with the NAADP-sensitive calcium stores. Fertilization of the stratified eggs elicited a Ca(2+) wave starting at the cADPR-pole and propagating toward the NAADP-pole. These results provide the first direct and visual evidence that the NAADP-sensitive Ca(2+) stores are novel and distinct from the ER. During fertilization, communicating signals appear to be transmitted from the ER to NAADP-sensitive Ca(2+) stores, leading to their activation.

scholarly journals Differential effect of pH upon cyclic-ADP-ribose and nicotinate–adenine dinucleotide phosphate-induced Ca2+ release systems

1998 ◽  
Vol 335 (3) ◽  
pp. 499-504 ◽  
Author(s):  
Eduardo N. CHINI ◽  
Mingyu LIANG ◽  
Thomas P. DOUSA
Keyword(s):  
Functional Properties ◽  
Sea Urchin ◽  
Differential Effect ◽  
Ph Dependence ◽  
Thiol Group ◽  
The Other ◽  
Sea Urchin Egg ◽  
Group Modification ◽  
Cyclic Adp Ribose ◽  
Ca2 Channels

We investigated the pH dependence and the effects of thimerosal and dithiothreitol (DTT) upon the Ca2+ release induced by cADP-ribose (cADPR) and nicotinate–adenine dinucleotide phosphate (NAADP) in sea urchin egg homogenates. Both Ca2+ release triggered by cADPR and the binding of [3H]cADPR to sea urchin egg homogenates were decreased by alkalization of the assay media from pH 7.2 to 8.9. In contrast, NAADP-triggered Ca2+ release was not influenced by changes in pH. The Ca2+ release induced by cADPR was potentiated by thimerosal and inhibited by DTT, but neither thimerosal nor DTT had any effect upon the Ca2+ release induced by NAADP. We conclude that cADPR-sensitive Ca2+-release mechanisms are dependent on pH of the assay media and are sensitive to thiol group modification. On the other hand, these functional properties are not shared by NAADP-regulated Ca2+ channels.

Specific modulation of cyclic ADP-ribose-induced Ca2+ release by polyamines

1995 ◽  
Vol 269 (4) ◽  
pp. C1042-C1047 ◽  
Author(s):  
E. N. Chini ◽  
K. W. Beers ◽  
C. C. Chini ◽  
T. P. Dousa
Keyword(s):  
Sea Urchin ◽  
Potent Inhibitor ◽  
Inhibitory Effect ◽  
Release System ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
Endogenous Regulators ◽  
Ryanodine Channel ◽  
Specific Inhibitors

Cyclic ADP-ribose (cADPR) is a potent mediator of Ca2+ mobilization from intracellular stores in sea urchin eggs. However, the regulation of the cADPR-induced Ca2+ release system is not yet fully elucidated. We now report that spermine and related polyamines, in physiological concentrations, were able to inhibit the Ca2+ release induced by cADPR in sea urchin egg homogenate bioassays, as measured using the Ca2+ indicator fluo 3, but had no effect on the Ca2+ release induced by D-myo-inositol 1,4,5-trisphosphate (IP3) or by nicotinate adenine dinucleotide phosphate (NAADP). Spermine was a more potent inhibitor of the cADPR-induced Ca2+ release than spermidine and putrescine. Spermine inhibited not only the release induced by cADPR but also the Ca2+ release induced by caffeine and ryanodine. Finally, pretreatment of the sea urchin egg homogenates with caffeine or Sr2+ and Ca2+ prevented the inhibitory effect of spermine on cADPR-induced Ca2+ release. We propose that polyamines, which are present in millimolar concentrations in fertilized eggs, are specific inhibitors of the ryanodine channel and perhaps may serve as endogenous regulators of the cADPR-induced Ca2+ release system.

NAADP, a new intracellular messenger that mobilizes Ca2+ from acidic stores

2006 ◽  
Vol 34 (5) ◽  
pp. 922-926 ◽  
Author(s):  
A. Galione
Keyword(s):  
Sea Urchin ◽  
Mammalian Cells ◽  
Ryanodine Receptors ◽  
Release Mechanism ◽  
Release Channel ◽  
Sea Urchin Egg ◽  
Wide Range ◽  
Inositol 1,4,5 Trisphosphate ◽  
Molecular Nature ◽  
Made In

NAADP (nicotinic acid–adenine dinucleotide phosphate) is a recently described Ca2+-mobilizing molecule. First characterized in the sea urchin egg, it has been shown to mobilize Ca2+ from intracellular stores in a wide range of cells from different organisms. It is a remarkably potent molecule, and recent reports show that its cellular levels change in response to a variety of agonists, confirming its role as a Ca2+-mobilizing messenger. In many cases, NAADP appears to interact with other Ca2+-mobilizing messengers such as IP3 (inositol 1,4,5-trisphosphate) and cADP-ribose in shaping cytosolic Ca2+ signals. What is not clear is the molecular nature of the NAADP-sensitive Ca2+ release mechanism and its subcellular localization. This review focuses on the recent progress made in sea urchin eggs, which indicates that NAADP activates a novel Ca2+ release channel distinct from the relatively well-characterized IP3 and ryanodine receptors. Furthermore, in the sea urchin egg, the NAADP-sensitive store appears to be separate from the endoplasmic reticulum and is most likely an acidic store. These findings have also been reinforced by similar findings in mammalian cells, and a unified model for NAADP-induced Ca2+ signalling is presented.

Probing Ca2+ release mechanisms using sea urchin egg homogenates

2019 ◽  
pp. 445-458
Author(s):  
Yu Yuan ◽  
Gihan S. Gunaratne ◽  
Jonathan S. Marchant ◽  
Sandip Patel
Keyword(s):  
Sea Urchin ◽  
Release Mechanisms ◽  
Sea Urchin Egg

scholarly journals Ca2+ release triggered by NAADP in hepatocyte microsomes

2006 ◽  
Vol 395 (2) ◽  
pp. 233-238 ◽  
Author(s):  
Miklós Mándi ◽  
Balázs Tóth ◽  
György Timár ◽  
Judit Bak
Keyword(s):  
Nicotinic Acid ◽  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Mammalian Cells ◽  
Liver Microsomes ◽  
The Other ◽  
Release Mechanism ◽  
Ip3 Receptors ◽  
Rat Hepatocyte ◽  
Inositol 1,4,5 Trisphosphate

NAADP (nicotinic acid–adenine dinucleotide phosphate) is fast emerging as a new intracellular Ca2+-mobilizing messenger. NAADP induces Ca2+ release by a mechanism that is distinct from IP3 (inositol 1,4,5-trisphosphate)- and cADPR (cADP-ribose)-induced Ca2+ release. In the present study, we demonstrated that micromolar concentrations of NAADP trigger Ca2+ release from rat hepatocyte microsomes. Cross-desensitization to IP3 and cADPR by NAADP did not occur in liver microsomes. We report that non-activating concentrations of NAADP can fully inactivate the NAADP-sensitive Ca2+-release mechanism in hepatocyte microsomes. The ability of thapsigargin to block the NAADP-sensitive Ca2+ release is not observed in sea-urchin eggs or in intact mammalian cells. In contrast with the Ca2+ release induced by IP3 and cADPR, the Ca2+ release induced by NAADP was completely independent of the free extravesicular Ca2+ concentration and pH (in the range 6.4–7.8). The NAADP-elicited Ca2+ release cannot be blocked by the inhibitors of the IP3 receptors and the ryanodine receptor. On the other hand, verapamil and diltiazem do inhibit the NAADP- (but not IP3- or cADPR-) induced Ca2+ release.

scholarly journals Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg

1962 ◽  
Vol 45 (3) ◽  
pp. 427-438 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Soluble Fraction ◽  
Water Soluble ◽  
The Other ◽  
Original Sample ◽  
Water Soluble Fraction ◽  
Sea Urchin Egg ◽  
Soluble Fractions

The contractility of the thread model prepared from the KCl-soluble proteins of the egg and in vivo factors for the contraction are investigated in Hemicentrotus, Anthocidaris, and Pseudocentrotus eggs. The contractility of the thread model induced by metal ions or cystine changes during development in the characteristic pattern of high at the metaphase and low at the monaster and the interkinetic stages. The change in contractility is paralleled by the change in the —SH content of the protein. The water-soluble fraction of the eggs has activity in causing contraction of the thread model. This activity changes during development in the same way as the contractility itself. The contraction of the thread induced by the water-soluble fractions is accompanied by a decrease in the —SH content of the thread. The activity of the water-soluble fraction in inducing the contraction is proportional to its ability to decrease the number of —SH groups. On boiling, the activity is largely destroyed. The activity is due to two components, one being non-dialyzable and the other dialyzable. Separately each component has little effect, but when mixed, the activity of the original sample is completely restored.

scholarly journals Pharmacological properties of the Ca2+ -release mechanism sensitive to NAADP in the sea urchin egg

1997 ◽  
Vol 121 (7) ◽  
pp. 1489-1495 ◽  
Author(s):  
A A Genazzani ◽  
M Mezna ◽  
D M Dickey ◽  
F Michelangeli ◽  
T F Walseth ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Release Mechanism ◽  
Pharmacological Properties ◽  
Sea Urchin Egg

Cyclic ADP-ribose signaling in sea urchin gametes: metabolism in spermatozoa

1997 ◽  
Vol 272 (2) ◽  
pp. C416-C420 ◽  
Author(s):  
E. N. Chini ◽  
M. A. Thompson ◽  
C. C. Chini ◽  
T. P. Dousa
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Sea Urchin ◽  
High Performance ◽  
Hplc Analysis ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Ambient Content ◽  
Homologous Desensitization ◽  
Sea Urchin Sperm

The molecular mechanism that initiates Ca2+ signaling in sea urchin egg fertilization has not yet been clarified. To determine whether sea urchin sperm may generate and possibly supply cyclic ADP-ribose (cADPR) as a Ca2+-releasing factor in the course of sea urchin egg fertilization, we determined cADPR content and the capacity for cADPR synthesis in sea urchin sperm. cADPR content was determined using the sea urchin egg homogenate Ca2+-release bioassay combined with high-performance liquid chromatography (HPLC). We found that sperm homogenates synthesized cADPR from beta-NAD but did not synthesize cADPR when alpha-NAD was the substrate. The identity of cADPR generated by sperm homogenates was verified by HPLC analysis, use of specific Ca2+-release antagonists, and homologous desensitization of the sea urchin egg homogenate Ca2+-release bioassay. The ambient content of cADPR was approximately 0.3 nmol cADPR/g wet wt sea urchin sperm. Our results show that sperm can synthesize cADPR and that they contain cADPR levels comparable to other tissues.

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