scholarly journals New Linear Precursors of cIDPR Derivatives as Stable Analogs of cADPR: A Potent Second Messenger with Ca2+-Modulating Activity Isolated from Sea Urchin Eggs

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 476
Author(s):  
Stefano D’Errico ◽  
Emy Basso ◽  
Andrea Patrizia Falanga ◽  
Maria Marzano ◽  
Tullio Pozzan ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Alkyl Chain ◽  
Second Messenger ◽  
Phosphate Group ◽  
C2c12 Cells ◽  
Sea Urchin Eggs ◽  
Cyclic Adp Ribose ◽  
Small Set

Herein, we report on the synthesis of a small set of linear precursors of an inosine analogue of cyclic ADP-ribose (cADPR), a second messenger involved in Ca2+ mobilization from ryanodine receptor stores firstly isolated from sea urchin eggs extracts. The synthesized compounds were obtained starting from inosine and are characterized by an N1-alkyl chain replacing the “northern” ribose and a phosphate group attached at the end of the N1-alkyl chain and/or 5′-sugar positions. Preliminary Ca2+ mobilization assays, performed on differentiated C2C12 cells, are reported as well.

Increase of cGMP, cADP-ribose and inositol 1,4,5-trisphosphate preceding Ca2+ transients in fertilization of sea urchin eggs

Development ◽  
2001 ◽  
Vol 128 (22) ◽  
pp. 4405-4414 ◽  
Author(s):  
Ritsu Kuroda ◽  
Kenji Kontani ◽  
Yasunari Kanda ◽  
Toshiaki Katada ◽  
Takashi Nakano ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Sea Urchin Eggs ◽  
Direct Measurements ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Receptor Channel

Transient increases, or oscillations, of cytoplasmic free Ca2+ concentration, [Ca2+]i, occur during fertilization of animal egg cells. In sea urchin eggs, the increased Ca2+ is derived from intracellular stores, but the principal signaling and release system involved has not yet been agreed upon. Possible candidates are the inositol 1,4,5-trisphosphate receptor/channel (IP3R) and the ryanodine receptor/channel (RyR) which is activated by cGMP or cyclic ADP-ribose (cADPR). Thus, it seemed that direct measurements of the likely second messenger candidates during sea urchin fertilization would be essential to an understanding of the Ca2+ signaling pathway. We therefore measured the cGMP, cADPR and inositol 1,4,5-trisphosphate (IP3) contents of sea urchin eggs during the early stages of fertilization and compared these with the [Ca2+]i rise in the presence or absence of an inhibitor against soluble guanylate cyclase. We obtained three major experimental results: (1) cytosolic cGMP levels began to rise first, followed by cADPR and IP3 levels, all almost doubling before the explosive increase of [Ca2+]i; (2) most of the rise in IP3 occurred after the Ca2+ peak; IP3 production could also be induced by the artificial elevation of [Ca2+]i, suggesting the large increase in IP3 is a consequence, rather than a cause, of the Ca2+ transient; (3) the measured increase in cGMP was produced by the soluble guanylate cyclase of eggs, and inhibition of soluble guanylate cyclase of eggs diminished the production of both cADPR and IP3 and the [Ca2+]i increase without the delay of Ca2+ transients. Taken together, these results suggest that the RyR pathway involving cGMP and cADPR is not solely responsible for the initiating event, but contributes to the Ca2+ transients by stimulating IP3 production during fertilization of sea urchin eggs.

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.

cGMP mobilizes intracellular Ca2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 456-459 ◽  
Author(s):  
Antony Galione ◽  
Alison White ◽  
Nicholas Willmott ◽  
Michelle Turner ◽  
Barry V. L. Potter ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Eggs ◽  
Cyclic Adp Ribose

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.

scholarly journals Ca2+ release triggered by nicotinate adenine dinucleotide phosphate in intact sea urchin eggs

1995 ◽  
Vol 312 (3) ◽  
pp. 955-959 ◽  
Author(s):  
C M Perez-Terzic ◽  
E N Chini ◽  
S S Shen ◽  
T P Dousa ◽  
D E Clapham
Keyword(s):  
Sea Urchin ◽  
Specific Inhibitor ◽  
Intact Cells ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
Dose Dependent Increase ◽  
Dose Dependent

Nicotinate adenine dinucleotide phosphate (NAADP) was recently identified [Lee and Aarhus (1995) J. Biol. Chem. 270, 2152-2157; Chini, Beers and Dousa (1995) J. Biol. Chem. 270, 3116-3223] as a potent Ca(2+)-releasing agent in sea urchin egg homogenates. NAADP triggered Ca2+ release by a mechanism that was distinct from inositol 1,4,5-trisphosphate (InsP3)- and cyclic ADP-ribose (cADPR)-induced Ca2+ release. When NAADP was microinjected into intact sea urchin eggs it induced a dose-dependent increase in cytoplasmic free Ca2+ which was independent of the extracellular [Ca2+]. The Ca2+ waves elicited by microinjections of NAADP originated at the site of injection and swept across the cytosol. As previously found in sea urchin egg homogenates, NAADP-induced Ca2+ release in intact eggs was not blocked by heparin or by prior desensitization to InsP3 or cADPR. Thio-NADP, a specific inhibitor of the NAADP-induced Ca2+ release in sea urchin homogenates [Chini, Beers and Dousa (1995) J. Biol. Chem. 270, 3116-3223] blocked NAADP (but not InsP3 or cADPR) injection-induced Ca2+ release in intact sea urchin eggs. Finally, fertilization of sea urchin eggs abrogated subsequent NAADP-induced Ca2+ release, suggesting that the NAADP-sensitive Ca2+ pool may participate in the fertilization response. This study demonstrates that NAADP acts as a selective Ca(2+)-releasing agonist in intact cells.

Cyclic ADP-ribose activates caffeine-sensitive calcium channels from sea urchin egg microsomes

1998 ◽  
Vol 274 (2) ◽  
pp. C430-C439 ◽  
Author(s):  
Claudio F. Pérez ◽  
Juan José Marengo ◽  
Ricardo Bull ◽  
Cecilia Hidalgo
Keyword(s):  
Sea Urchin ◽  
Microsomal Fraction ◽  
Ruthenium Red ◽  
Single Channels ◽  
Channel Activity ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
Intracellular Ca

Adenosine 5′-cyclic diphosphoribose [cyclic ADP-ribose (cADPR)], a metabolite of NAD+ that promotes Ca2+ release from sea urchin egg homogenates and microsomal fractions, has been proposed to act as an endogenous agonist of Ca2+ release in sea urchin eggs. We describe experiments showing that a microsomal fraction isolated from Tetrapigus nyger sea urchin eggs displayed Ca2+-selective single channels with conductances of 155.0 ± 8.0 pS in asymmetric Cs+ solutions and 47.5 ± 1.1 pS in asymmetric Ca2+ solutions. These channels were sensitive to stimulation by Ca2+, ATP, and caffeine, but not inositol 1,4,5-trisphosphate, and were inhibited by ruthenium red. The channels were also activated by cADP-ribose in a Ca2+-dependent fashion. Calmodulin and Mg2+, but not heparin, modulated channel activity in the presence of cADP-ribose. We propose that these Ca2+ channels constitute the intracellular Ca2+-induced Ca2+ release pathway that is activated by cADP-ribose in sea urchin eggs.

scholarly journals Role of the Second-Messenger Cyclic-Adenosine 5′-Diphosphate-Ribose on Adrenocorticotropin Secretion from Pituitary Cells

Endocrinology ◽  
2005 ◽  
Vol 146 (5) ◽  
pp. 2186-2192 ◽  
Author(s):  
Sandra M. Soares ◽  
Michael Thompson ◽  
Eduardo N. Chini
Keyword(s):  
Tumor Cell ◽  
Receptor Antagonist ◽  
Ryanodine Receptor ◽  
Tumor Cell Line ◽  
Second Messenger ◽  
Pituitary Cells ◽  
Acth Secretion ◽  
Cyclic Adp Ribose ◽  
Ryanodine Channel

Abstract We examined the role of the second-messenger cyclic-ADP-ribose (cADPR) on the regulation of ACTH secretion using AtT20 corticotroph tumor cell line. We found that the cADPR antagonist, 8-Br-cADPR, substantially diminished the secretion of ACTH induced by CRH and potassium in these cells, whereas xestospongin C, an inositol 1,4,5-triphosphate receptor antagonist, had no effect. In addition, the cADPR agonist, 3-deaza-cADPR, augmented ACTH secretion. The presence of the components of the cADPR system, namely ryanodine receptor, CD38, and cADPR itself, was determined in AtT20 cells. Furthermore, we observed that antagonists of the ryanodine channel and cADPR system can decrease the potassium-induced Ca2+ transients in these cells. These results suggest that cADPR is a second messenger in pituitary cells and regulates ACTH secretion by a mechanism dependent on activation of the ryanodine channel by extracellular Ca2+.

Molecular cloning and characterization of ryanodine receptor from unfertilized sea urchin eggs

2002 ◽  
Vol 282 (3) ◽  
pp. R727-R737 ◽  
Author(s):  
Mieko Shiwa ◽  
Takashi Murayama ◽  
Yasuo Ogawa
Keyword(s):  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Sea Urchins ◽  
Structural Features ◽  
Release Channel ◽  
Terminal Domain ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Hemicentrotus Pulcherrimus

Unfertilized eggs of sea urchins ( Hemicentrotus pulcherrimus) demonstrated cyclic ADP-ribose (cADPR)-induced Ca2+ release and caffeine-induced Ca2+ release, both of which were considered to be mediated through the ryanodine receptor (RyR). We cloned cDNAs for sea urchin egg RyR (suRyR), which encode a 597-kDa protein of 5,317 amino acids. suRyR shares common structural features with known RyRs: the well-conserved COOH-terminal domain, which forms a functional Ca2+ channel, and a large hydrophilic NH2-terminal domain. suRyR shows amino acid sequence identity (43–45%) similar to the three mammalian RyR isoforms. Phylogenetic analysis indicates that suRyR branched from three isoforms of vertebrates before they diverged, suggesting that suRyR may be the only RyR isoform in the sea urchin. Four in-frame insertions were found in suRyR cDNAs, one of which was novel and unique, in that it had a cluster of serine residues. The transcripts with and without these insertions were found in the egg RNA. These results suggest that suRyR may be expressed as a functional Ca2+-induced Ca2+ release channel, which might also be involved in cADPR-induced Ca2+ release.

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