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Ichida, Seiji; Abe, Jun‐ichi; Zhang, Y A; Sugihara, Kensuke; Imoto, Koichiro; Wada, Tetuyuki; Fujita, Norihisa; Sohma, Hitoshi

doi:10.1023/a:1026674721542

Cited by 8 publications

(2 citation statements)

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“…Of interest, the microtubule remnant present within the first polar body was not associated with calmodulin (Figure 7, far right, arrow), suggesting calmodulin's role in functional (spindle) microtubules. We could not consistently inhibit polar body emission using W7 (Su and Eppig, 2002) either added to the medium or by injection (up to 50 μM final intracellular concentration), calmodulin-binding domain peptide 290–309 of CMKII (Ichida et al , 2000; 10–100 nl of 0.5 mM stock solution, per oocyte), or morpholino oligos antisense to Xenopus calmodulin (unpublished data). However, the same inhibitors also did not block egg activation (unpublished data).…”

Section: Resultsmentioning

confidence: 99%

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Leblanc

et al. 2016

MBoC

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Section: Resultsmentioning

confidence: 99%

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Leblanc

et al. 2016

MBoC

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“…The μ-conotoxins are used for the immobilization of skeletal muscles without affecting axonal or synaptic events because of their ability to block the muscle Na + channel Na v 1.4, but not axonal Na + channels Na v 1.1–Na v 1.3 and Na v 1.6–Na v 1.9 [4,5]. The ω-conotoxins are used as standard pharmacological reagents in voltage-gated calcium (Ca 2+ ) channel-related research and are used to block neurotransmitter release [6,7]. ω-conotoxins have also been used to diagnose the Ca 2+ channel targeted disease, Lambert-Eaton myasthenic syndrome [8].…”

Section: Introductionmentioning

confidence: 99%

Conotoxins that Confer Therapeutic Possibilities

2012

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Cone snails produce a distinctive repertoire of venom peptides that are used both as a defense mechanism and also to facilitate the immobilization and digestion of prey. These peptides target a wide variety of voltage- and ligand-gated ion channels, which make them an invaluable resource for studying the properties of these ion channels in normal and diseased states, as well as being a collection of compounds of potential pharmacological use in their own right. Examples include the United States Food and Drug Administration (FDA) approved pharmaceutical drug, Ziconotide (Prialt®; Elan Pharmaceuticals, Inc.) that is the synthetic equivalent of the naturally occurring ω-conotoxin MVIIA, whilst several other conotoxins are currently being used as standard research tools and screened as potential therapeutic drugs in pre-clinical or clinical trials. These developments highlight the importance of driving conotoxin-related research. A PubMed query from 1 January 2007 to 31 August 2011 combined with hand-curation of the retrieved articles allowed for the collation of 98 recently identified conotoxins with therapeutic potential which are selectively discussed in this review. Protein sequence similarity analysis tentatively assigned uncharacterized conotoxins to predicted functional classes. Furthermore, conotoxin therapeutic potential for neurodegenerative disorders (NDD) was also inferred.

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Characteristics of Omega-conotoxin GVI A and MVIIC Binding to Cav 2.1 and Cav 2.2 Channels Captured by Anti-Ca2+ Channel Peptide Antibodies

et al. 2005

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A New Binding Method (NBM) was used to investigate the characteristics of the specific binding of 125I-omega-conotoxin (omega-CTX) GVIA and 125I-omega-CTX MVIIC to Cav2.1 and Cav2.2 channels captured from chick brain membranes by antibodies against B1Nt (a peptide sequence in Car2.1 and Cav2.2 channels). The results for the NBM were as follows. (1) The ED50 values for specific binding of 125I-omega-CTX GVIA and 125I-omega-CTX MVIIC to Cav2.1 and Cav2.2 channels were about 68 and 60 pM, respectively, and very similar to those (87 and 35 pM, respectively) to crude membranes from chick brain. (2) The specific 125I-omega-CTX GVIA (100 pM) binding was inhibited by omega-CTX GVIA (0.5 nM), dynorphine A (Dyn), gentamicin (Gen), neomycin (Neo) and tobramicin (Tob) (100 microM each), but not by omega-agaconotoxin (Aga) IVA, calciseptine, omega-CTX SVIB, omega-CTX MVIIC (0.5 nM each), PN200-110 (PN), diltiazem (Dil) or verapamil (Ver) (100 microM each). Calmodulin (CaM) inhibited the specific binding in a dose-dependent manner (IC50 value of about 100 microg protein/ml). (3) The specific 125I-omega-CTX MVIIC (60 pM) binding was inhibited by omega-CTX MVIIC, omega-CTX GVIA, omega-CTX SVIB (0.5 nM each), Dyn, Neo and Tob (100 microM, each), but not by omega-Aga IVA, calciseptine (0.5 nM each), PN, Dil, Ver (100 microM each) or 100 microg protein/ml CaM. These results suggested that the characteristics of the specific binding of 125I-omega-CTX GVIA and 125I-omega-CTX MVIIC to Cav2.1 and Cav2.2 channels in the NBM were very similar to those to crude membranes from chick brain, although the IC50 values for CaM and free Ca2+ of CaM were about 33- and 5000-fold higher, respectively, than those for the specific binding of 125I-omega-CTX GVIA and 125I-omega-CTX MVIIC to crude membranes.

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Cited by 8 publications

References 40 publications

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Spindle function inXenopusoocytes involves possible nanodomain calcium signaling

Conotoxins that Confer Therapeutic Possibilities

Characteristics of Omega-conotoxin GVI A and MVIIC Binding to Cav 2.1 and Cav 2.2 Channels Captured by Anti-Ca2+ Channel Peptide Antibodies

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