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      Shellfish Toxins Targeting Voltage-Gated Sodium Channels

      review-article
      Author(s): , , , *
      Publication date (Electronic):
      Journal: Marine Drugs
      Publisher: MDPI
      Keywords: VGSCs, shellfish toxins, structure, bioactivity, pharmaceutical potential

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          Abstract

          Voltage-gated sodium channels (VGSCs) play a central role in the generation and propagation of action potentials in excitable neurons and other cells and are targeted by commonly used local anesthetics, antiarrhythmics, and anticonvulsants. They are also common targets of neurotoxins including shellfish toxins. Shellfish toxins are a variety of toxic secondary metabolites produced by prokaryotic cyanobacteria and eukaryotic dinoflagellates in both marine and fresh water systems, which can accumulate in marine animals via the food chain. Consumption of shellfish toxin-contaminated seafood may result in potentially fatal human shellfish poisoning. This article provides an overview of the structure, bioactivity, and pharmacology of shellfish toxins that act on VGSCs, along with a brief discussion on their pharmaceutical potential for pain management.

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          Ion channel voltage sensors: structure, function, and pathophysiology.

          William Catterall (2010)
          Voltage-gated ion channels generate electrical signals in species from bacteria to man. Their voltage-sensing modules are responsible for initiation of action potentials and graded membrane potential changes in response to synaptic input and other physiological stimuli. Extensive structure-function studies, structure determination, and molecular modeling are now converging on a sliding-helix mechanism for electromechanical coupling in which outward movement of gating charges in the S4 transmembrane segments catalyzed by sequential formation of ion pairs pulls the S4-S5 linker, bends the S6 segment, and opens the pore. Impairment of voltage-sensor function by mutations in Na+ channels contributes to several ion channelopathies, and gating pore current conducted by mutant voltage sensors in Na(V)1.4 channels is the primary pathophysiological mechanism in hypokalemic periodic paralysis. The emerging structural model for voltage sensor function opens the way to development of a new generation of ion-channel drugs that act on voltage sensors rather than blocking the pore. Copyright © 2010 Elsevier Inc. All rights reserved.
          Article 0 comments Cited 151 times – based on 0 reviews     Review now
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            Loss-of-function mutations in the Nav1.7 gene underlie congenital indifference to pain in multiple human populations.

            Y Goldberg, C Radomski, Aaron M Samuels … (2007)
            Congenital indifference to pain (CIP) is a rare condition in which patients have severely impaired pain perception, but are otherwise essentially normal. We identified and collected DNA from individuals from nine families of seven different nationalities in which the affected individuals meet the diagnostic criteria for CIP. Using homozygosity mapping and haplotype sharing methods, we narrowed the CIP locus to chromosome 2q24-q31, a region known to contain a cluster of voltage-gated sodium channel genes. From these prioritized candidate sodium channels, we identified 10 mutations in the SCN9A gene encoding the sodium channel protein Nav1.7. The mutations completely co-segregated with the disease phenotype, and nine of these SCN9A mutations resulted in truncation and loss-of-function of the Nav1.7 channel. These genetic data further support the evidence that Nav1.7 plays an essential role in mediating pain in humans, and that SCN9A mutations identified in multiple different populations underlie CIP.
            Article 0 comments Cited 120 times – based on 0 reviews     Review now
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              Phylogeny of some of the major genera of dinoflagellates based on ultrastructure and partial LSU rDNA sequence data, including the erection of three new genera of unarmoured dinoflagellates

              N Daugbjerg, T G Hansen, J J Larsen … (2000)
              Article 0 comments Cited 113 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Mar Drugs
                Journal ID (iso-abbrev): Mar Drugs
                Journal ID (publisher-id): marinedrugs
                Title: Marine Drugs
                Publisher: MDPI
                ISSN (Electronic): 1660-3397
                Publication date (Electronic): 28 November 2013
                Publication date Collection: December 2013
                Volume: 11
                Issue: 12
                Pages: 4698-4723
                Affiliations
                Cooperative Innovation Center of Engineering and New Products for Developmental Biology, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China; E-Mails: zhangfan20111112@ 123456126.com (F.Z.); xxxu20120101@ 123456126.com (X.X.); Demi4869@ 123456126.com (T.L.)
                Author notes
                [* ] Author to whom correspondence should be addressed; E-Mail: liuzh@ 123456hunnu.edu.cn ; Tel.: +86-731-88-872-556; Fax: +86-731-88-861-304.
                Article
                Publisher ID: marinedrugs-11-04698
                DOI: 10.3390/md11124698
                PMC ID: 3877881
                PubMed ID: 24287955
                SO-VID: 13193759-0c85-4b67-aebd-7d3df59d1401
                Copyright © © 2013 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 12 September 2013
                Date revision received : 10 November 2013
                Date accepted : 12 November 2013
                Categories
                Subject: Review

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: shellfish toxins,structure,bioactivity,pharmaceutical potential,vgscs
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: shellfish toxins, structure, bioactivity, pharmaceutical potential, vgscs

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