brevetoxin and gambierol

brevetoxin has been researched along with gambierol* in 3 studies

Reviews

1 review(s) available for brevetoxin and gambierol

ArticleYear
Ladder-Shaped Ion Channel Ligands: Current State of Knowledge.
    Marine drugs, 2017, Jul-20, Volume: 15, Issue:7

    Ciguatoxins (CTX) and brevetoxins (BTX) are polycyclic ethereal compounds biosynthesized by the worldwide distributed planktonic and epibenthic dinoflagellates of

    Topics: Animals; Ciguatera Poisoning; Ciguatoxins; Dinoflagellida; Humans; Ligands; Marine Toxins; Oxocins; Potassium Channels, Voltage-Gated

2017

Other Studies

2 other study(ies) available for brevetoxin and gambierol

ArticleYear
TRPV1 as a key determinant in ciguatera and neurotoxic shellfish poisoning.
    Biochemical and biophysical research communications, 2007, Sep-14, Volume: 361, Issue:1

    Ciguatera fish poisoning and neurotoxic shellfish poisoning are distinct clinical entities characterized by gastrointestinal and neurological disturbances, following the consumption of certain reef fish and shellfish containing toxic polyether compounds sporadically present in certain toxic marine dinoflagellates. The biotransformation and bioaccumulation of gambierol and brevetoxin, and their congeners, are believed to be involved in the pathogenesis of these "food-chain diseases", for which no effective treatments are available. Here, we describe for the first time the potent effect of gambierol and brevetoxin on TRPV1 channels, a key player in thermal and pain sensation. Our findings may lead to promising new therapeutic interventions.

    Topics: Animals; Ciguatera Poisoning; Ciguatoxins; Ethers, Cyclic; Humans; Marine Toxins; Oxocins; Patch-Clamp Techniques; Polycyclic Compounds; Shellfish; TRPV Cation Channels; Xenopus laevis

2007
Inhibition of brevetoxin binding to the voltage-gated sodium channel by gambierol and gambieric acid-A.
    Toxicon : official journal of the International Society on Toxinology, 2003, Volume: 41, Issue:4

    Brevetoxins (BTXs) and ciguatoxins (CTXs) bind to site 5 of the voltage-gated sodium channel of excitable membranes. In the present study, we performed a competitive inhibition assay with other structurally distinct naturally occurring polyethers using isotope-labeled dihydro BTX-B ([3H]PbTx-3), which showed, for the first time, that gambierol and gambieric acid-A inhibit the binding of [3H]PbTx-3 while yessotoxins are inactive in this assay. The inhibition assay also suggested that there is a significant relationship between the size of the polycyclic region and inhibitory activity. Interestingly, the acute mouse toxicities of the compounds do not correspond directly to their inhibitory activities. These observations will serve as a guide for designing artificial polyethers with desired activity.

    Topics: Animals; Binding, Competitive; Brain; Ciguatoxins; Drug Interactions; Ethers, Cyclic; Marine Toxins; Molecular Structure; Mollusk Venoms; Oxocins; Polycyclic Compounds; Protein Binding; Rats; Sodium Channels; Synaptosomes

2003