Separate Activation of the Cytoplasmic and Nuclear Calcium Pools in Maturing Starfish Oocytes

Santella, Luigia; Riso, Laura De; Gragnaniello, Giovanni; Kyozuka, Keiichiro

doi:10.1006/bbrc.1998.9583

Cited by 43 publications

(23 citation statements)

References 17 publications

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“…In spite of the evidence for the existence of such a complete Ca 2+ release system in the nucleus, there is little evidence (Lui et al, 1998;Santella and Kyozuka, 1997;Santella et al, 1998) of its independent involvement in nuclear Ca 2+ signal generation. In fact, there are more reports indicating that Ca 2+ released primarily into the cytoplasm (Ca 2+ puffs) can diffuse into the nucleoplasm (Bootman et al, 1997;Bootman et al, 2000;Hennager et al, 1995;Lipp et al, 1997;Shirakawa and Miyazaki, 1996).…”

Section: Discussionmentioning

confidence: 99%

New aspects of nuclear calcium signalling

Gerasimenko

2004

Journal of Cell Science

128

104

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Nuclear calcium signalling has been a controversial battlefield for many years and the question of how permeable the nuclear pore complexes (NPCs) are to Ca2+ has been the subject of a particularly hot dispute. Recent data from isolated nuclei suggest that the NPCs are open even after depletion of the Ca2+ store in the nuclear envelope. Other research has suggested that a new Ca2+-releasing messenger, nicotinic acid adenine dinucleotide phosphate (NAADP), can liberate Ca2+ only from acidic organelles, probably lysosomes, rather than from the traditional Ca2+ store in the endoplasmic reticulum (ER). Recent work indicates that NAADP can release Ca2+ from the nuclear envelope (NE), which has a thapsigargin-sensitive, ER-type Ca2+ store. NAADP acts in a manner similar to inositol (1,4,5)-trisphosphate [Ins(1,4,5)P3] or cyclic ADP-ribose (cADPR): all three messengers are equally able to reduce the Ca2+ concentration inside the NE and this is associated with a transient rise in the nucleoplasmic Ca2+ concentration. The NE contains ryanodine receptors (RyRs) and Ins(1,4,5)P3 receptors [Ins(1,4,5)P3Rs], and these can be activated separately and independently: the RyRs by either NAADP or cADPR, and the Ins(1,4,5)P3Rs by Ins(1,4,5)P3.

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Section: Discussionmentioning

confidence: 99%

New aspects of nuclear calcium signalling

Gerasimenko

2004

Journal of Cell Science

128

104

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“…In attempting to reconcile these contradictory results, it should be noted that 1-MA causes oocytes of the starfish Asterina pectinifera and Astropecten aranciacus to generate both cytoplasmic and nuclear Ca 2+ elevations before GVBD (Santella and Kyozuka, 1994;Santella et al, 1998;Lim et al, 2003), and that injections of BAPTA into the nucleus, but not into the cytoplasm, can inhibit 1-MA-induced GVBD (Santella and Kyozuka, 1994). Similarly, in 1-MA-treated A. pectinifera oocytes, all elevations in Ca 2+ and subsequent GVBD are eliminated by the membrane-permeable calcium release blocker TMB-8 (Tosuji et al, 2007), presumably because, unlike BAPTA, TMB-8 can cross the nuclear envelope to affect nuclear Ca 2+ signals.…”

Section: Echinodermata (Starfish Sea Urchins)mentioning

confidence: 99%

Calcium signals and oocyte maturation in marine invertebrates

Deguchi¹,

Takeda²,

Stricker³

2015

Int. J. Dev. Biol.

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In various oocytes and eggs of animals, transient elevations in cytoplasmic calcium ion concentrations are known to regulate key processes during fertilization and the completion of meiosis. However, whether or not calcium transients also help to reinitiate meiotic progression at the onset of oocyte maturation remains controversial. This article summarizes reports of calcium signals playing essential roles during maturation onset (=germinal vesicle breakdown, GVBD) in several kinds of marine invertebrate oocytes. Conversely, other data from the literature, as well as previously unpublished findings for jellyfish oocytes, fail to support the view that calcium signals are required for GVBD. In addition to assessing the effects of calcium transients on GVBD in marine invertebrate oocytes, the ability of maturing oocytes to enhance their calcium-releasing capabilities after GVBD is also reviewed. Furthermore, possible explanations are proposed for the contradictory results that have been obtained regarding calcium signals during oocyte maturation in marine invertebrates.

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“…However, it has been demonstrated both in oocytes and in HeLa cells that it is possible to induce an IP 3 -dependent rise of nuclear Ca 2+ , independently of the cytoplasm (Lui et al, 1998;Santella et al, 1998). The participation of IP 3 Rs in regulating nuclear Ca 2+ in skeletal muscle has not yet been described.…”

Section: Camentioning

confidence: 99%

Nuclear inositol 1,4,5-trisphosphate receptors regulate local Ca2+ transients and modulate cAMP response element binding protein phosphorylation

Cárdenas

Liberona

Molgó

et al. 2005

Journal of Cell Science

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Several lines of evidence indicate that increases in nuclear Ca2+ have specific biological effects that differ from those of cytosolic Ca2+, suggesting that they occur independently. The mechanisms involved in controlling nuclear Ca2+ signaling are both controversial and still poorly understood. Using hypotonic shock combined with mechanical disruption, we obtained and characterized a fraction of purified nuclei from cultured rat skeletal myotubes. Both immunoblot studies and radiolabeled inositol 1,4,5-trisphosphate [IP3] binding revealed an important concentration of IP3 receptors in the nuclear fraction. Immunofluorescence and immunoelectron microscopy studies localized type-1 and type-3 IP3 receptors in the nucleus with type-1 receptors preferentially localized in the inner nuclear membrane. Type-2 IP3 receptor was confined to the sarcoplasmic reticulum. Isolated nuclei responded to IP3 with rapid and transient Ca2+ concentration elevations, which were inhibited by known blockers of IP3 signals. Similar results were obtained with isolated nuclei from the 1B5 cell line, which does not express ryanodine receptors but releases nuclear Ca2+ in an IP3-dependent manner. Nuclear Ca2+ increases triggered by IP3 evoked phosphorylation of cAMP response element binding protein with kinetics compatible with sequential activation. These results support the idea that Ca2+ signals, mediated by nuclear IP3 receptors in muscle cells, are part of a distinct Ca2+ release component that originates in the nucleus and probably participates in gene regulation mediated by cAMP response element binding protein.

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Separate Activation of the Cytoplasmic and Nuclear Calcium Pools in Maturing Starfish Oocytes

Cited by 43 publications

References 17 publications

New aspects of nuclear calcium signalling

New aspects of nuclear calcium signalling

Calcium signals and oocyte maturation in marine invertebrates

Nuclear inositol 1,4,5-trisphosphate receptors regulate local Ca2+ transients and modulate cAMP response element binding protein phosphorylation

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