Cyclic ADP-Ribose-Induced Calcium Release in Sea Urchin Egg Homogenates Is a Cooperative Process

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 2815-2818 ◽  
Author(s):  
Yajun Xu ◽  
Armen H. Tashjian
Keyword(s):  
Sea Urchin ◽  
Calcium Release ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Cooperative Process

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.

scholarly journals Nicotinamide inhibits cyclic ADP-ribose-mediated calcium signalling in sea urchin eggs

1996 ◽  
Vol 319 (2) ◽  
pp. 613-617 ◽  
Author(s):  
Jaswinder K SETHI ◽  
Ruth M EMPSON ◽  
Antony GALIONE
Keyword(s):  
Sea Urchin ◽  
Calcium Release ◽  
Calcium Signalling ◽  
Hydrolytic Activity ◽  
Calcium Release Channels ◽  
Adp Ribosyl Cyclase ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Single Polypeptide ◽  
Hydrolysis Of

Cyclic ADP ribose (cADPR) is a potent Ca2+-releasing agent, and putative second messenger, the endogenous levels of which are tightly regulated by synthetic (ADP-ribosyl cyclases) and degradative (cADPR hydrolase) enzymes. These enzymes have been characterized in a number of mammalian and invertebrate tissues and their activities are often found on a single polypeptide. β-NAD+, cGMP and nitric oxide (NO) have been reported to mobilize Ca2+ in the sea urchin egg via the cADPR-mediated pathway. We now report that in sea urchin egg homogenates, nicotinamide inhibits the Ca2+-mobilizing action of β-NAD+, cGMP and NO, but has no effect on cADPR-induced Ca2+ release. Moreover, nicotinamide inhibits cGMP-induced regenerative Ca2+ waves in the intact sea urchin egg. By successfully separating the cADPR-metabolizing machinery from that which releases Ca2+, we have shown that nicotinamide inhibits cADPR-mediated Ca2+ signalling at the level of cADPR generation. Importantly, nicotinamide had no effect upon the hydrolysis of cADPR, and its selective action on cyclase activity was supported by its inhibition of purified Aplysia ADP-ribosyl cyclase, which does not exhibit detectable hydrolytic activity. The action of nicotinamide in blocking Ca2+ release by β-NAD+, cGMP and NO strongly suggests that these agents act as modulators of cADPR synthesis rather than to sensitize calcium release channels to cADPR.

Synergistic Calcium Release in the Sea Urchin Egg by Ryanodine and Cyclic ADP Ribose

1994 ◽  
Vol 163 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Wayne R. Buck ◽  
Erin E. Hoffmann ◽  
Terese L. Rakow ◽  
Sheldon S. Shen
Keyword(s):  
Sea Urchin ◽  
Calcium Release ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose

cADP-ribose releases Ca2+ from cardiac sarcoplasmic reticulum independently of ryanodine receptor

1997 ◽  
Vol 273 (3) ◽  
pp. H1082-H1089 ◽  
Author(s):  
P. Lahouratate ◽  
J. Guibert ◽  
J. F. Faivre
Keyword(s):  
Endoplasmic Reticulum ◽  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Calcium Release ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Consistent Effect ◽  
Cyclic Adp Ribose

Cyclic ADP-ribose (cADPR), an endogenous metabolite of beta-NAD+, activates Ca2+ release from endoplasmic reticulum in sea urchin eggs via the ryanodine receptor (RyR) pathway. A similar role has been proposed in cardiac sarcoplasmic reticulum (SR), although this remains controversial. We therefore investigated the ability of cADPR to induce Ca2+ release from canine cardiac SR microsomes using fluo 3 to monitor extravesicular Ca2+ concentration. We found that cADPR induced Ca2+ release in a concentration-dependent manner, whereas neither its precursor, NAD+, nor its metabolite, ADP-ribose, elicited a consistent effect. In addition, an additive effect on calcium release between cADPR and 9-Me-7-Br-eudistomin-D (MBED), an activator of RyR, was found as well as no cross-desensitization between cADPR and MBED. Specific blockers of the RyR did not abolish the cADPR-induced Ca2+ release. These results provide evidence for cADPR-induced Ca2+ release from dog cardiac SR via a novel mechanism which is independent of RyR activation.

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.

scholarly journals Cortical localization of a calcium release channel in sea urchin eggs.

1992 ◽  
Vol 116 (5) ◽  
pp. 1111-1121 ◽  
Author(s):  
S M McPherson ◽  
P S McPherson ◽  
L Mathews ◽  
K P Campbell ◽  
F J Longo
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Calcium Release ◽  
Staining Pattern ◽  
Cortical Granule ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg

We have used an antibody against the ryanodine receptor/calcium release channel of skeletal muscle sarcoplasmic reticulum to localize a calcium release channel in sea urchin eggs. The calcium release channel is present in less than 20% of immature oocytes, where it does not demonstrate a specific cytoplasmic localization, while it is confined to the cortex of all mature eggs examined. This is in contrast to the cortical and subcortical localization of calsequestrin in mature and immature eggs. Immunolocalization of the calcium release channel reveals a cortical reticulum or honeycomb staining network that surrounds cortical granules and is associated with the plasma membrane. The network consists of some immunoreactive electron-dense material coating small vesicles and elongate cisternae of the endoplasmic reticulum. The fluorescent reticular staining pattern is lost when egg cortices are treated with agents known to affect sarcoplasmic reticulum calcium release and induce cortical granule exocytosis (ryanodine, calcium, A-23187, and caffeine). An approximately 380-kD protein of sea urchin egg cortices is identified by immunoblot analysis with the ryanodine receptor antibody. These results demonstrate: (a) the presence of a ryanodine-sensitive calcium release channel that is located within the sea urchin egg cortex; (b) an altered calcium release channel staining pattern as a result of treatments that initiate the cortical granule reaction; and (c) a spatial and functional dichotomy of the ER which may be important in serving different roles in the mobilization of calcium at fertilization.

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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