scholarly journals Molecular Characterization of Voltage-Gated Sodium Channels and Their Relations with Paralytic Shellfish Toxin Bioaccumulation in the Pacific Oyster Crassostrea gigas

Marine Drugs ◽  
2017 ◽  
Vol 15 (1) ◽  
pp. 21 ◽  
Author(s):  
Floriane Boullot ◽  
Justine Castrec ◽  
Adeline Bidault ◽  
Natanael Dantas ◽  
Laura Payton ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Sodium Channels ◽  
Crassostrea Gigas ◽  
Pacific Oyster ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Paralytic Shellfish ◽  
The Pacific ◽  
Shellfish Toxin

Molecular characterization of voltage-gated sodium channels in human gliomas

Neuroreport ◽  
2002 ◽  
Vol 13 (18) ◽  
pp. 2493-2498 ◽  
Author(s):  
Michael Schrey ◽  
Carolina Codina ◽  
Robert Kraft ◽  
Christian Beetz ◽  
Rolf Kalff ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Sodium Channels ◽  
Human Gliomas ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels

scholarly journals Sources of paralytic shellfish toxin accumulation variability in the Pacific oyster Crassostrea gigas

Toxicon ◽  
2018 ◽  
Vol 144 ◽  
pp. 14-22 ◽  
Author(s):  
Émilien Pousse ◽  
Jonathan Flye-Sainte-Marie ◽  
Marianne Alunno-Bruscia ◽  
Hélène Hégaret ◽  
Fred Jean
Keyword(s):  
Crassostrea Gigas ◽  
Pacific Oyster ◽  
Paralytic Shellfish Toxin ◽  
Paralytic Shellfish ◽  
The Pacific ◽  
Shellfish Toxin ◽  
Toxin Accumulation

scholarly journals Functional and Molecular Characterization of Voltage-Gated Sodium Channels in Uteri from Nonpregnant Rats1

2007 ◽  
Vol 77 (5) ◽  
pp. 855-863 ◽  
Author(s):  
Marian Seda ◽  
Francisco M. Pinto ◽  
Susan Wray ◽  
Cristina G. Cintado ◽  
Pedro Noheda ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Sodium Channels ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels

scholarly journals Molecular Characterization of a cDNA Encoding Putative Vitellogenin from the Pacific Oyster Crassostrea gigas

2003 ◽  
Vol 20 (1) ◽  
pp. 37-42 ◽  
Author(s):  
Toshie Matsumoto ◽  
Akihumi M. Nakamura ◽  
Katsuyoshi Mori ◽  
Toshiaki Kayano
Keyword(s):  
Molecular Characterization ◽  
Crassostrea Gigas ◽  
Pacific Oyster ◽  
The Pacific

Molecular characterization of a cathepsin L1 highly expressed in phagocytes of pacific oyster Crassostrea gigas

2018 ◽  
Vol 89 ◽  
pp. 152-162
Author(s):  
Zhao Lv ◽  
Limei Qiu ◽  
Zhaoqun Liu ◽  
Weilin Wang ◽  
Hao Chen ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Crassostrea Gigas ◽  
Pacific Oyster

Presence and characterization of multiple mantle lysozymes in the Pacific oyster, Crassostrea gigas

2010 ◽  
Vol 29 (1) ◽  
pp. 126-135 ◽  
Author(s):  
Naoki Itoh ◽  
Yuki Okada ◽  
Keisuke G. Takahashi ◽  
Makoto Osada
Keyword(s):  
Crassostrea Gigas ◽  
Pacific Oyster ◽  
The Pacific

scholarly journals Purification and Characterization of JZTx-14, a Potent Antagonist of Mammalian and Prokaryotic Voltage-Gated Sodium Channels

Toxins ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 408 ◽  
Author(s):  
Jie Zhang ◽  
Dongfang Tang ◽  
Shuangyu Liu ◽  
Haoliang Hu ◽  
Songping Liang ◽  
...  
Keyword(s):  
Sodium Channels ◽  
Resting State ◽  
Purification And Characterization ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Steady State Inactivation ◽  
Ic50 Values ◽  
Gating Modifier ◽  
Potent Antagonist

Exploring the interaction of ligands with voltage-gated sodium channels (NaVs) has advanced our understanding of their pharmacology. Herein, we report the purification and characterization of a novel non-selective mammalian and bacterial NaVs toxin, JZTx-14, from the venom of the spider Chilobrachys jingzhao. This toxin potently inhibited the peak currents of mammalian NaV1.2–1.8 channels and the bacterial NaChBac channel with low IC50 values (<1 µM), and it mainly inhibited the fast inactivation of the NaV1.9 channel. Analysis of NaV1.5/NaV1.9 chimeric channel showed that the NaV1.5 domain II S3–4 loop is involved in toxin association. Kinetics data obtained from studying toxin–NaV1.2 channel interaction showed that JZTx-14 was a gating modifier that possibly trapped the channel in resting state; however, it differed from site 4 toxin HNTx-III by irreversibly blocking NaV currents and showing state-independent binding with the channel. JZTx-14 might stably bind to a conserved toxin pocket deep within the NaV1.2–1.8 domain II voltage sensor regardless of channel conformation change, and its effect on NaVs requires the toxin to trap the S3–4 loop in its resting state. For the NaChBac channel, JZTx-14 positively shifted its conductance-voltage (G–V) and steady-state inactivation relationships. An alanine scan analysis of the NaChBac S3–4 loop revealed that the 108th phenylalanine (F108) was the key residue determining the JZTx-14–NaChBac interaction. In summary, this study provided JZTx-14 with potent but promiscuous inhibitory activity on both the ancestor bacterial NaVs and the highly evolved descendant mammalian NaVs, and it is a useful probe to understand the pharmacology of NaVs.

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