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Journal articles on the topic 'Palytoxins'

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Author: Grafiati

Published: 11 March 2023

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1

Espiña, Begoña, Eva Cagide, M. Carmen Louzao, Maria M. Fernandez, Mercedes R. Vieytes, Panagiota Katikou, Adriano Villar, David Jaen, Luz Maman, and Luis M. Botana. "Specific and dynamic detection of palytoxins by in vitro microplate assay with human neuroblastoma cells." Bioscience Reports 29, no. 1 (December 10, 2008): 13–23. http://dx.doi.org/10.1042/bsr20080080.

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Palytoxin is one of the most complex and biggest molecules known to show extreme acute toxicity. The dinoflagellate Ostreopsis spp., the producer organism of palytoxin, has been shown to be distributed worldwide, thus making palytoxin an emerging toxin. Rat-derived hepatocytes (Clone 9) and BE (2)-M17 human neuroblastoma cells were used to test palytoxin or palytoxin-like compounds by measuring the cell metabolic rate with Alamar Blue. The dose-dependent decrease in viability was specifically inhibited by ouabain in the case of BE (2)-M17 neuroblastoma cells. This is a functional, dynamic and simple test for palytoxins with high sensitivity (as low as 0.2 ng/ml). This method was useful for toxin detection in Ostreopsis extracts and naturally contaminated mussel samples. A comparative study testing toxic mussel extracts by LC (liquid chromatography)-MS/MS (tandem MS), MBA (mouse bioassay), haemolysis neutralization assay and a cytotoxicity test indicated that our method is suitable for the routine determination and monitoring of palytoxins and palytoxin-like compounds.

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2

Bates, Nicola, Cassandra Morrison, Leah Flaig, and Andrew D. Turner. "Paralytic shellfish poisoning and palytoxin poisoning in dogs." Veterinary Record 187, no. 7 (April 17, 2020): e46-e46. http://dx.doi.org/10.1136/vr.105686.

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BackgroundFatal cases of exposure to paralytic shellfish toxins and palytoxins have occurred in companion animals but are poorly described.MethodsWe describe one case of paralytic shellfish poisoning (PSP) and three cases of palytoxin poisoning in dogs.ResultsMild PSP occurred following ingestion of crab while walking on a beach. Analysis confirmed the presence of paralytic shellfish toxins, particularly decarbamoyl saxitoxin, in clinical samples and marine organisms. This case occurred shortly after an outbreak of PSP in dogs on the eastern coast of England. Palytoxin poisoning occurred in a dog after it chewed coral removed from an aquarium. Signs included collapse, hypothermia, bloody diarrhoea and respiratory distress. The dog was euthanised due to rapid deterioration and poor prognosis. Palytoxin was not detected in a premortem blood sample. Two other dogs in a separate incident developed only mild signs (fever and respiratory distress) after suspected exposure to aerosolised palytoxin and recovered within a few hours.ConclusionCases of PSP are episodic and not common in dogs. Cases of palytoxin exposure are reportedly increasing in humans, and there is presumably also an increased risk to pets. There is no specific treatment for PSP or palytoxin poisoning.

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3

Uemura, Daisuke, Yoshimasa Hirata, Takashi Iwashita, and Hideo Naoki. "Studies on palytoxins." Tetrahedron 41, no. 6 (January 1985): 1007–17. http://dx.doi.org/10.1016/s0040-4020(01)96468-3.

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4

Riobó, Pilar, and José M. Franco. "Palytoxins: Biological and chemical determination." Toxicon 57, no. 3 (March 2011): 368–75. http://dx.doi.org/10.1016/j.toxicon.2010.09.012.

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5

Louzao, M. Carmen, Isabel R. Ares, Eva Cagide, Begoña Espiña, Natalia Vilariño, Amparo Alfonso, Mercedes R. Vieytes, and Luis M. Botana. "Palytoxins and cytoskeleton: An overview." Toxicon 57, no. 3 (March 2011): 460–69. http://dx.doi.org/10.1016/j.toxicon.2010.09.017.

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6

Ciminiello, Patrizia, Carmela Dell’Aversano, Ernesto Fattorusso, and Martino Forino. "Palytoxins: A still haunting Hawaiian curse." Phytochemistry Reviews 9, no. 4 (June 5, 2010): 491–500. http://dx.doi.org/10.1007/s11101-010-9185-x.

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7

Guillen, Paul O., Karla B. Jaramillo, Grégory Genta-Jouve, and Olivier P. Thomas. "Marine natural products from zoantharians: bioactivity, biosynthesis, systematics, and ecological roles." Natural Product Reports 37, no. 4 (2020): 515–40. http://dx.doi.org/10.1039/c9np00043g.

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The dazzling marine zoantharians represent a reservoir of chemical diversity that remains to be unveiled. These fragile animals have so far been found to harbour the highly bioactive palytoxins or zoanthamines but also the harmless ecdysteroids or zoanthozanthins.

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8

Tubaro, A., P. Durando, G. Del Favero, F. Ansaldi, G. Icardi, J. R. Deeds, and S. Sosa. "Case definitions for human poisonings postulated to palytoxins exposure." Toxicon 57, no. 3 (March 2011): 478–95. http://dx.doi.org/10.1016/j.toxicon.2011.01.005.

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9

Ciminiello, Patrizia, Carmela Dell’Aversano, Emma Dello Iacovo, Martino Forino, and Luciana Tartaglione. "Liquid chromatography–high-resolution mass spectrometry for palytoxins in mussels." Analytical and Bioanalytical Chemistry 407, no. 5 (December 9, 2014): 1463–73. http://dx.doi.org/10.1007/s00216-014-8367-6.

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10

Ciminiello, Patrizia, Carmela Dell’Aversano, Ernesto Fattorusso, Martino Forino, Laura Grauso, and Luciana Tartaglione. "A 4-decade-long (and still ongoing) hunt for palytoxins chemical architecture." Toxicon 57, no. 3 (March 2011): 362–67. http://dx.doi.org/10.1016/j.toxicon.2010.09.005.

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11

Tubaro, A., G. Del Favero, D. Beltramo, P. Lorenzon, M. Sciancalepore, C. Florio, M. Poli, and S. Sosa. "Toxicological effects of palytoxins: An integrated in vivo and in vitro approach." Toxicon 75 (December 2013): 210. http://dx.doi.org/10.1016/j.toxicon.2013.08.017.

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12

Artigas, Pablo, and David C. Gadsby. "Large Diameter of Palytoxin-induced Na/K Pump Channels and Modulation of Palytoxin Interaction by Na/K Pump Ligands." Journal of General Physiology 123, no. 4 (March 15, 2004): 357–76. http://dx.doi.org/10.1085/jgp.200308964.

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Palytoxin binds to Na/K pumps to generate nonselective cation channels whose pore likely comprises at least part of the pump's ion translocation pathway. We systematically analyzed palytoxin's interactions with native human Na/K pumps in outside-out patches from HEK293 cells over a broad range of ionic and nucleotide conditions, and with or without cardiotonic steroids. With 5 mM internal (pipette) [MgATP], palytoxin activated the conductance with an apparent affinity that was highest for Na+-containing (K+-free) external and internal solutions, lowest for K+-containing (Na+-free) external and internal solutions, and intermediate for the mixed external Na+/internal K+, and external K+/internal Na+ conditions; with Na+ solutions and MgATP, the mean dwell time of palytoxin on the Na/K pump was about one day. With Na+ solutions, the apparent affinity for palytoxin action was low after equilibration of patches with nucleotide-free pipette solution. That apparent affinity was increased in two phases as the equilibrating [MgATP] was raised over the submicromolar, and submillimolar, ranges, but was increased by pipette MgAMPPNP in a single phase, over the submillimolar range; the apparent affinity at saturating [MgAMPPNP] remained ∼30-fold lower than at saturating [MgATP]. After palytoxin washout, the conductance decay that reflects palytoxin unbinding was accelerated by cardiotonic steroid. When Na/K pumps were preincubated with cardiotonic steroid, subsequent activation of palytoxin-induced conductance was greatly slowed, even after washout of the cardiotonic steroid, but activation could still be accelerated by increasing palytoxin concentration. These results indicate that palytoxin and a cardiotonic steroid can simultaneously occupy the same Na/K pump, each destabilizing the other. The palytoxin-induced channels were permeable to several large organic cations, including N-methyl-d-glucamine+, suggesting that the narrowest section of the pore must be ∼7.5 Å wide. Enhanced understanding of palytoxin action now allows its use for examining the structures and mechanisms of the gates that occlude/deocclude transported ions during the normal Na/K pump cycle.

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Vilariño, Natalia, M. Louzao, Paula Abal, Eva Cagide, Cristina Carrera, Mercedes Vieytes, and Luis Botana. "Human Poisoning from Marine Toxins: Unknowns for Optimal Consumer Protection." Toxins 10, no. 8 (August 9, 2018): 324. http://dx.doi.org/10.3390/toxins10080324.

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Marine biotoxins are produced by aquatic microorganisms and accumulate in shellfish or finfish following the food web. These toxins usually reach human consumers by ingestion of contaminated seafood, although other exposure routes like inhalation or contact have also been reported and may cause serious illness. This review shows the current data regarding the symptoms of acute intoxication for several toxin classes, including paralytic toxins, amnesic toxins, ciguatoxins, brevetoxins, tetrodotoxins, diarrheic toxins, azaspiracids and palytoxins. The information available about chronic toxicity and relative potency of different analogs within a toxin class are also reported. The gaps of toxicological knowledge that should be studied to improve human health protection are discussed. In general, gathering of epidemiological data in humans, chronic toxicity studies and exploring relative potency by oral administration are critical to minimize human health risks related to these toxin classes in the near future.

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Kim, Young-Sang, Hyun-Joo An, Jaeseong Kim, and You-Jin Jeon. "Current Situation of Palytoxins and Cyclic Imines in Asia-Pacific Countries: Causative Phytoplankton Species and Seafood Poisoning." International Journal of Environmental Research and Public Health 19, no. 8 (April 18, 2022): 4921. http://dx.doi.org/10.3390/ijerph19084921.

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Among marine biotoxins, palytoxins (PlTXs) and cyclic imines (CIs), including spirolides, pinnatoxins, pteriatoxins, and gymnodimines, are not managed in many countries, such as the USA, European nations, and South Korea, because there are not enough poisoning cases or data for the limits on these biotoxins. In this article, we review unregulated marine biotoxins (e.g., PlTXs and CIs), their toxicity, causative phytoplankton species, and toxin extraction and detection protocols. Due to global warming, the habitat of the causative phytoplankton has expanded to the Asia-Pacific region. When ingested by humans, shellfish that accumulated toxins can cause various symptoms (muscle pain or diarrhea) and even death. There are no systematic reports on the occurrence of these toxins; however, it is important to continuously monitor causative phytoplankton and poisoning of accumulating shellfish by PlTXs and CI toxins because of the high risk of toxicity in human consumers.

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Ciminiello, Patrizia, Carmela Dell’Aversano, Emma Dello Iacovo, Ernesto Fattorusso, Martino Forino, Laura Grauso, and Luciana Tartaglione. "High Resolution LC-MSn Fragmentation Pattern of Palytoxin as Template to Gain New Insights into Ovatoxin-a Structure. The Key Role of Calcium in MS Behavior of Palytoxins." Journal of The American Society for Mass Spectrometry 23, no. 5 (February 22, 2012): 952–63. http://dx.doi.org/10.1007/s13361-012-0345-7.

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Biré, Ronel, Sophie Trotereau, Rodolphe Lemée, Davide Oregioni, Christine Delpont, Sophie Krys, and Thierry Guérin. "Hunt for Palytoxins in a Wide Variety of Marine Organisms Harvested in 2010 on the French Mediterranean Coast." Marine Drugs 13, no. 8 (August 21, 2015): 5425–46. http://dx.doi.org/10.3390/md13085425.

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17

Louzao, M. Carmen, Isabel R. Ares, Mercedes R. Vieytes, Iago Valverde, Juan M. Vieites, Takeshi Yasumoto, and Luis M. Botana. "The cytoskeleton, a structure that is susceptible to the toxic mechanism activated by palytoxins in human excitable cells." FEBS Journal 274, no. 8 (March 19, 2007): 1991–2004. http://dx.doi.org/10.1111/j.1742-4658.2007.05743.x.

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18

Biré, R., S. Trotereau, R. Lemée, C. Delpont, B. Chabot, Y. Aumond, and S. Krys. "Occurrence of palytoxins in marine organisms from different trophic levels of the French Mediterranean coast harvested in 2009." Harmful Algae 28 (August 2013): 10–22. http://dx.doi.org/10.1016/j.hal.2013.04.007.

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19

Mazzeo, Antonia, Michela Varra, Luciana Tartaglione, Patrizia Ciminiello, Zita Zendong, Philipp Hess, and Carmela Dell’Aversano. "Toward Isolation of Palytoxins: Liquid Chromatography Coupled to Low- or High-Resolution Mass Spectrometry for the Study on the Impact of Drying Techniques, Solvents and Materials." Toxins 13, no. 9 (September 14, 2021): 650. http://dx.doi.org/10.3390/toxins13090650.

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Palytoxin (PLTX) and its congeners are emerging toxins held responsible for a number of human poisonings following the inhalation of toxic aerosols, skin contact, or the ingestion of contaminated seafood. Despite the strong structural analogies, the relative toxic potencies of PLTX congeners are quite different, making it necessary to isolate them individually in sufficient amounts for toxicological and analytical purposes. Previous studies showed poor PLTX recoveries with a dramatic decrease in PLTX yield throughout each purification step. In view of a large-scale preparative work aimed at the preparation of PLTX reference material, we have investigated evaporation as a critical—although unavoidable—step that heavily affects overall recoveries. The experiments were carried out in two laboratories using different liquid chromatography-mass spectrometry (LC-MS) instruments, with either unit or high resolution. Palytoxin behaved differently when concentrated to a minimum volume rather than when evaporated to complete dryness. The recoveries strongly depended on the solubility as well as on the material of the used container. The LC-MS analyses of PLTX dissolved in aqueous organic blends proved to give a peak intensity higher then when dissolved in pure water. After drying, the PLTX adsorption appeared stronger on glass surfaces than on plastic materials. However, both the solvents used to dilute PLTX and that used for re-dissolution had an important role. A quantitative recovery (97%) was achieved when completely drying 80% aqueous EtOH solutions of PLTX under N2-stream in Teflon. The stability of PLTX in acids was also investigated. Although PLTX was quite stable in 0.2% acetic acid solutions, upon exposure to stronger acids (pH < 2.66), degradation products were observed, among which a PLTX methyl-ester was identified.

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20

Cen, Jingyi, Lei Cui, Yafei Duan, Hua Zhang, Yarou Lin, Jiping Zheng, and Songhui Lu. "Effects of palytoxins extracted from Ostreopsis ovata on the oxidative stress and immune responses in Pacific white shrimp Litopenaeus vannamei." Fish & Shellfish Immunology 95 (December 2019): 670–78. http://dx.doi.org/10.1016/j.fsi.2019.11.001.

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21

Selwood, Andrew I., Roel van Ginkel, D. Tim Harwood, Paul S. McNabb, Lesley R. Rhodes, and Patrick T. Holland. "A sensitive assay for palytoxins, ovatoxins and ostreocins using LC-MS/MS analysis of cleavage fragments from micro-scale oxidation." Toxicon 60, no. 5 (October 2012): 810–20. http://dx.doi.org/10.1016/j.toxicon.2012.05.024.

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22

Tartaglione, Luciana, Carmela Dell’Aversano, Antonia Mazzeo, Martino Forino, Andre Wieringa, and Patrizia Ciminiello. "Determination of Palytoxins in Soft Coral and Seawater from a Home Aquarium. Comparison between Palythoa- and Ostreopsis-Related Inhalatory Poisonings." Environmental Science & Technology 50, no. 2 (December 23, 2015): 1023–30. http://dx.doi.org/10.1021/acs.est.5b05469.

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23

Tartaglione, Luciana, Marco Pelin, Massimo Morpurgo, Carmela Dell'Aversano, Javier Montenegro, Giuseppe Sacco, Silvio Sosa, James Davis Reimer, Patrizia Ciminiello, and Aurelia Tubaro. "An aquarium hobbyist poisoning: Identification of new palytoxins in Palythoa cf. toxica and complete detoxification of the aquarium water by activated carbon." Toxicon 121 (October 2016): 41–50. http://dx.doi.org/10.1016/j.toxicon.2016.08.012.

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24

Mullin, J. M., K. V. Snock, and M. T. McGinn. "Effects of apical vs. basolateral palytoxin on LLC-PK1 renal epithelia." American Journal of Physiology-Cell Physiology 260, no. 6 (June 1, 1991): C1201—C1211. http://dx.doi.org/10.1152/ajpcell.1991.260.6.c1201.

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Research on palytoxin focuses on its action as a tumor promoter and its ionophoretic action in cell membranes. The first property is unusual because palytoxin is not a protein kinase C activator. The second property is remarkable in that it may require interaction with the Na(+)-K(+)-adenosinetriphosphatase (ATPase). Our studies here with palytoxin exposure to the LLC-PK1 renal epithelial cells have yielded the following results: 1) unlike protein kinase C-activating tumor promoters (tetradecanoylphorbol 12,13-acetate or teleocidin), palytoxin does not produce a specific effect on the tight junctions between epithelia; 2) palytoxin instead produces an irreversible cytotoxic effect characterized by a pronounced cell swelling associated with sharply elevated levels of intracellular Na+ and decreased levels of intracellular K+; 3) these fluctuations in intracellular Na+ and K+ levels are explained by marked elevations in the membrane flux of 22Na+ and 86Rb+; 4) the electrophysiological reflection of these altered ion fluxes is a pronounced depolarization of the cell sheet if palytoxin is presented to the basolateral cell surface and a pronounced hyperpolarization (due to sharply elevated apical Na+ flux and transepithelial short-circuit current) if palytoxin is administered apically; 5) the apical effect of palytoxin can be blocked by apical ouabain; and 6) this apical effect of palytoxin decreases as a function of the age of the cell sheet. This first report of palytoxin action in a polar epithelial cell system provides additional evidence for palytoxin effects being mediated by contact with the Na(+)-K(+)-ATPase. It also adds to a growing literature suggesting the existence of Na(+)-K(+)-ATPase in the apical cell surface of epithelia under certain conditions.

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Kockskämper, Jens, Gias U. Ahmmed, Aleksey V. Zima, Katherine A. Sheehan, Helfried G. Glitsch, and Lothar A. Blatter. "Palytoxin disrupts cardiac excitation-contraction coupling through interactions with P-type ion pumps." American Journal of Physiology-Cell Physiology 287, no. 2 (August 2004): C527—C538. http://dx.doi.org/10.1152/ajpcell.00541.2003.

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Palytoxin is a coral toxin that seriously impairs heart function, but its effects on excitation-contraction (E-C) coupling have remained elusive. Therefore, we studied the effects of palytoxin on mechanisms involved in atrial E-C coupling. In field-stimulated cat atrial myocytes, palytoxin caused elevation of diastolic intracellular Ca2+ concentration ([Ca2+]i), a decrease in [Ca2+]i transient amplitude, Ca2+ alternans followed by [Ca2+]i waves, and failures of Ca2+ release. The decrease in [Ca2+]i transient amplitude occurred despite high sarcoplasmic reticulum (SR) Ca2+ load. In voltage-clamped myocytes, palytoxin induced a current with a linear current-voltage relationship (reversal potential ∼5 mV) that was blocked by ouabain. Whole cell Ca2+ current and ryanodine receptor Ca2+ release channel function remained unaffected by the toxin. However, palytoxin significantly reduced Ca2+ pumping of isolated SR vesicles. In current-clamped myocytes stimulated at 1 Hz, palytoxin induced a depolarization of the resting membrane potential that was accompanied by delayed afterdepolarizations. No major changes of action potential configuration were observed. The results demonstrate that palytoxin interferes with the function of the sarcolemmal Na+-K+ pump and the SR Ca2+ pump. The suggested mode of palytoxin toxicity in the atrium involves the conversion of Na+-K+ pumps into nonselective cation channels as a primary event followed by depolarization, Na+ accumulation, and Ca2+ overload, which, in turn, causes arrhythmogenic [Ca2+]i waves and delayed afterdepolarizations.

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Wattenberg, Elizabeth V. "Palytoxin: exploiting a novel skin tumor promoter to explore signal transduction and carcinogenesis." American Journal of Physiology-Cell Physiology 292, no. 1 (January 2007): C24—C32. http://dx.doi.org/10.1152/ajpcell.00254.2006.

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Palytoxin is a novel skin tumor promoter, which has been used to help probe the role of different types of signaling mechanisms in carcinogenesis. The multistage mouse skin model indicates that tumor promotion is an early, prolonged, and reversible phase of carcinogenesis. Understanding the molecular mechanisms underlying tumor promotion is therefore important for developing strategies to prevent and treat cancer. Naturally occurring tumor promoters that bind to specific cellular receptors have proven to be useful tools for investigating important biochemical events in multistage carcinogenesis. For example, the identification of protein kinase C as the receptor for the prototypical skin tumor promoter 12- O-tetradecanoylphorbol-13-acetate (TPA) (also called phorbol 12-myristate 13-acetate, PMA) provided key evidence that tumor promotion involves the aberrant modulation of signaling cascades that govern cell fate and function. The subsequent discovery that palytoxin, a marine toxin isolated from zoanthids (genus Palythoa), is a potent skin tumor promoter yet does not activate protein kinase C indicated that investigating palytoxin action could help reveal new aspects of tumor promotion. Interestingly, the putative receptor for palytoxin is the Na+,K+-ATPase. This review focuses on palytoxin-stimulated signaling and how palytoxin has been used to investigate alternate biochemical mechanisms by which important targets in carcinogenesis can be modulated.

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27

Rakowski, R. F., Pablo Artigas, Francisco Palma, Miguel Holmgren, Paul De Weer, and David C. Gadsby. "Sodium Flux Ratio in Na/K Pump-Channels Opened by Palytoxin." Journal of General Physiology 130, no. 1 (June 11, 2007): 41–54. http://dx.doi.org/10.1085/jgp.200709770.

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Palytoxin binds to Na+/K+ pumps in the plasma membrane of animal cells and opens an electrodiffusive cation pathway through the pumps. We investigated properties of the palytoxin-opened channels by recording macroscopic and microscopic currents in cell bodies of neurons from the giant fiber lobe, and by simultaneously measuring net current and 22Na+ efflux in voltage-clamped, internally dialyzed giant axons of the squid Loligo pealei. The conductance of single palytoxin-bound “pump-channels” in outside-out patches was ∼7 pS in symmetrical 500 mM [Na+], comparable to findings in other cells. In these high-[Na+], K+-free solutions, with 5 mM cytoplasmic [ATP], the K0.5 for palytoxin action was ∼70 pM. The pump-channels were ∼40–50 times less permeable to N-methyl-d-glucamine (NMG+) than to Na+. The reversal potential of palytoxin-elicited current under biionic conditions, with the same concentration of a different permeant cation on each side of the membrane, was independent of the concentration of those ions over the range 55–550 mM. In giant axons, the Ussing flux ratio exponent (n') for Na+ movements through palytoxin-bound pump-channels, over a 100–400 mM range of external [Na+] and 0 to −40 mV range of membrane potentials, averaged 1.05 ± 0.02 (n = 28). These findings are consistent with occupancy of palytoxin-bound Na+/K+ pump-channels either by a single Na+ ion or by two Na+ ions as might be anticipated from other work; idiosyncratic constraints are needed if the two Na+ ions occupy a single-file pore, but not if they occupy side-by-side binding sites, as observed in related structures, and if only one of the sites is readily accessible from both sides of the membrane.

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Suh, Edward M., and Yoshito Kishi. "Synthesis of Palytoxin from Palytoxin Carboxylic Acid." Journal of the American Chemical Society 116, no. 24 (November 1994): 11205–6. http://dx.doi.org/10.1021/ja00103a065.

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29

Harmel, Nadine, and Hans-Jürgen Apell. "Palytoxin-induced Effects on Partial Reactions of the Na,K-ATPase." Journal of General Physiology 128, no. 1 (June 26, 2006): 103–18. http://dx.doi.org/10.1085/jgp.200609505.

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The interaction of palytoxin with the Na,K-ATPase was studied by the electrochromic styryl dye RH421, which monitors the amount of ions in the membrane domain of the pump. The toxin affected the pump function in the state P-E2, independently of the type of phosphorylation (ATP or inorganic phosphate). The palytoxin-induced modification of the protein consisted of two steps: toxin binding and a subsequent conformational change into a transmembrane ion channel. At 20°C, the rate-limiting reaction had a forward rate constant of 105 M−1s−1 and a backward rate constant of about 10−3 s−1. In the palytoxin-modified state, the binding affinity for Na+ and H+ was increased and reached values between those obtained in the E1 and P-E2 conformation under physiological conditions. Even under saturating palytoxin concentrations, the ATPase activity was not completely inhibited. In the Na/K mode, ∼50% of the enzyme remained active in the average, and in the Na-only mode 25%. The experimental findings indicate that an additional exit from the inhibited state exists. An obvious reaction pathway is a slow dephosphorylation of the palytoxin-inhibited state with a time constant of ∼100 s. Analysis of the effect of blockers of the extracellular and cytoplasmic access channels, TPA+ and Br2-Titu3+, respectively, showed that both access channels are part of the ion pathway in the palytoxin-modified protein. All experiments can be explained by an extension of the Post-Albers cycle, in which three additional states were added that branch off in the P-E2 state and lead to states in which the open-channel conformation is introduced and returns into the pump cycle in the occluded E2 state. The previously suggested molecular model for the channel state of the Na,K-ATPase as a conformation in which both gates between binding sites and aqueous phases are simultaneously in their open state is supported by this study.

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30

Patocka, Jiri, Eugenie Nepovimova, Qinghua Wu, and Kamil Kuca. "Palytoxin congeners." Archives of Toxicology 92, no. 1 (November 7, 2017): 143–56. http://dx.doi.org/10.1007/s00204-017-2105-8.

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31

Boente-Juncal, Andrea, Sandra Raposo-García, Carmen Vale, M. Carmen Louzao, Paz Otero, and Luis M. Botana. "In Vivo Evaluation of the Chronic Oral Toxicity of the Marine Toxin Palytoxin." Toxins 12, no. 8 (July 30, 2020): 489. http://dx.doi.org/10.3390/toxins12080489.

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Palytoxin (PLTX) is one of the most poisonous substances known to date and considered as an emergent toxin in Europe. Palytoxin binds to the Na+-K+ ATPase, converting the enzyme in a permeant cation channel. This toxin is known for causing human fatal intoxications associated with the consumption of contaminated fish and crustaceans such as crabs, groupers, mackerel, and parrotfish. Human intoxications by PLTX after consumption of contaminated fishery products are a serious health issue and can be fatal. Different reports have previously explored the acute oral toxicity of PLTX in mice. Although the presence of palytoxin in marine products is currently not regulated in Europe, the European Food Safety Authority expressed its opinion on PLTX and demanded assessment for chronic toxicity studies of this potent marine toxin. In this study, the chronic toxicity of palytoxin was evaluated after oral administration to mice by gavage during a 28-day period. After chronic exposure of mice to the toxin, a lethal dose 50 (LD50) of 0.44 µg/kg of PLTX and a No-Observed-Adverse-Effect Level (NOAEL) of 0.03 µg/kg for repeated daily oral administration of PLTX were determined. These results indicate a much higher chronic toxicity of PLTX and a lower NOAEL than that previously described in shorter treatment periods, pointing out the need to further reevaluate the levels of this compound in marine products.

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32

Falciola, Jacques, Bernard Volet, Rolf M. Anner, Marlis Moosmayer, Danielle Lacotte, and Beatrice M. Anner. "Role of cell membrane Na,K-ATPase for survival of human lymphocytes in vitro." Bioscience Reports 14, no. 4 (August 1, 1994): 189–204. http://dx.doi.org/10.1007/bf01200248.

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Lymphocytes are primordial immune cells with variable life times. Besides genetic programming, extracellular factors interacting with cell surface receptors might alter cell survival. We investigated whether the activity of the membrane-embedded Na,K-ATPase (EC 3.6.1.37) or sodium pump (NKA) plays a role for cell survival since this ubiquitous system establishes the vital transmembrane Na and K gradients as well as the resulting high intracellular K/Na ratio required for macromolecule synthesis; furthermore, the system exposes an extracellular inhibitory receptors for cardioactive steroids and palytoxin. Isolated human lymphocytes were incubated in vitro and their viability assessed by exclusion of trypan blue. Various incubation conditions were compared; in RPMI-1640 medium cell viability was preserved for 30 h at 37 °C. Externally added ouabain, a hydrophilic cardioactive steroid, blocked the [86Rb]potassium uptake at nanomolar concentrations. Despite pump inhibition ouabain did not alter lymphocyte survival, even at 10 mM for 30 h. By contrast, the hydrophilic toxin palytoxin, the most potent animal poison described so far, killed all cells within 2 h at 10 nM; this toxin is known to act via the sodium pump and to provoke deadly cation-leaks by unmasking a channel component. Intracellular Na increased and K decreased as measured by atomic absorption spectrometry in presence of palytoxin; cell swelling was seen by electron microscopy. Ouabain protected the cells from the toxic effect of palytoxin. The results reveal a pivotal role of NKA integrity for lymphocyte survival.

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33

Armstrong, Robert W., Jean Marie Beau, Seung Hoon Cheon, William J. Christ, Hiromichi Fujioka, Won Hun Ham, Lynn D. Hawkins, Haolun Jin, and Sung Ho Kang. "Total synthesis of palytoxin carboxylic acid and palytoxin amide." Journal of the American Chemical Society 111, no. 19 (September 1989): 7530–33. http://dx.doi.org/10.1021/ja00201a038.

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34

Pelin, Marco, Chiara Florio, Cristina Ponti, Marianna Lucafò, Davide Gibellini, Aurelia Tubaro, and Silvio Sosa. "Pro-inflammatory effects of palytoxin: an in vitro study on human keratinocytes and inflammatory cells." Toxicology Research 5, no. 4 (2016): 1172–81. http://dx.doi.org/10.1039/c6tx00084c.

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35

Mebs, D., and S. Gleibs. "Ecology of palytoxin." Toxicon 35, no. 6 (June 1997): 814. http://dx.doi.org/10.1016/s0041-0101(97)90327-5.

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36

Hall, Christine, David Levy, and Steven Sattler. "A Case of Palytoxin Poisoning in a Home Aquarium Enthusiast and His Family." Case Reports in Emergency Medicine 2015 (2015): 1–3. http://dx.doi.org/10.1155/2015/621815.

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Inhalational exposure to palytoxin is an extremely rare cause of respiratory distress. This little-known marine toxin has the potential to cause significant morbidity and mortality. Toxicity has been best documented in cases of ingestion but has also been seen in cases of dermal exposure and inhalation of vapors. Palytoxin has been found in several coral species, some of which are favored by home aquarium enthusiasts and are commercially available. We report a case of a family who were exposed to the aerosolized toxin following the cleaning of a coral in their home aquarium. It is important that clinicians be aware of this source of toxic exposure to provide necessary care to these patients.

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37

Abe, Takahiro, Takayuki Naito, and Daisuke Uemura. "Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) Analysis of Palytoxin." Natural Product Communications 12, no. 8 (August 2017): 1934578X1701200. http://dx.doi.org/10.1177/1934578x1701200815.

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Many natural products have been isolated from various marine organisms. These natural products, especially huge polyol and polyether compounds, are expected to be promising drug-leads. On the other hand, the accumulation of these compounds in fish and shellfish can cause food poisoning in humans. Therefore, the development of effective methods for the detection of these compounds is important from both academic and public health perspectives. We subjected palytoxin to an SDS-PAGE analysis, which is very easy, quick, and inexpensive, to determine whether this approach could be effective for detecting huge polyol natural products. Eventually, we were able to detect a band of palytoxin by SDS-PAGE analysis, which demonstrated that SDS-PAGE could be useful for detecting polyol and polyether compounds.

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38

Crawford, Mark H. "Harvard Synthesizes Palytoxin Molecule." Science 246, no. 4926 (October 6, 1989): 34. http://dx.doi.org/10.1126/science.246.4926.34.d.

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39

CRAWFORD, M. H. "Harvard Synthesizes Palytoxin Molecule." Science 246, no. 4926 (October 6, 1989): 34. http://dx.doi.org/10.1126/science.246.4926.34-c.

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40

Munday, Rex. "Palytoxin toxicology: Animal studies." Toxicon 57, no. 3 (March 2011): 470–77. http://dx.doi.org/10.1016/j.toxicon.2010.10.003.

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41

Kishi, Y. "Natural products synthesis: palytoxin." Pure and Applied Chemistry 61, no. 3 (January 1, 1989): 313–24. http://dx.doi.org/10.1351/pac198961030313.

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42

Levine, Lawrence, Hirota Fujiki, Hilda B. Gjika, and Helen Van Vunakis. "A radioimmunoassay for palytoxin." Toxicon 26, no. 12 (January 1988): 1115–21. http://dx.doi.org/10.1016/0041-0101(88)90295-4.

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43

Patocka, Jiří, Ramesh C. Gupta, Qing-hua Wu, and Kamil Kuca. "Toxic potential of palytoxin." Journal of Huazhong University of Science and Technology [Medical Sciences] 35, no. 5 (October 2015): 773–80. http://dx.doi.org/10.1007/s11596-015-1506-3.

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44

Levine, Lawrence, Hirota Fujiki, Hilda B. Gjika, and Helen Van Vunakis. "Production of antibodies to palytoxin: Neutralization of several biological properties of palytoxin." Toxicon 25, no. 12 (January 1987): 1273–82. http://dx.doi.org/10.1016/0041-0101(87)90005-5.

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45

Pelin, Marco, Sabrina Boscolo, Mark Poli, Silvio Sosa, Aurelia Tubaro, and Chiara Florio. "Characterization of Palytoxin Binding to HaCaT Cells Using a Monoclonal Anti-Palytoxin Antibody." Marine Drugs 11, no. 12 (February 26, 2013): 584–98. http://dx.doi.org/10.3390/md11030584.

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46

Kerbrat, Anne Sophie, Zouher Amzil, Ralph Pawlowiez, Stjepko Golubic, Manoella Sibat, Helene Taiana Darius, Mireille Chinain, and Dominique Laurent. "First Evidence of Palytoxin and 42-Hydroxy-palytoxin in the Marine Cyanobacterium Trichodesmium." Marine Drugs 9, no. 4 (March 31, 2011): 543–60. http://dx.doi.org/10.3390/md9040543.

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47

Del Favero, G., P. Lorenzon, C. Florio, S. Sosa, P. Ciminiello, E. Fattorusso, M. Poli, G. Bignami, and A. Tubaro. "Toxicity of palytoxin and 42-hydroxy-palytoxin on cultured mouse skeletal muscle cells." Toxicology Letters 196 (July 2010): S348—S349. http://dx.doi.org/10.1016/j.toxlet.2010.03.1103.

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48

Tubaro, A., G. Del Favero, D. Beltramo, M. Ardizzone, M. Forino, M. De Bortoli, M. Pelin, et al. "Acute oral toxicity in mice of a new palytoxin analog: 42-Hydroxy-palytoxin." Toxicon 57, no. 5 (April 2011): 755–63. http://dx.doi.org/10.1016/j.toxicon.2011.02.009.

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49

Wu, Chau H. "Palytoxin: Membrane mechanisms of action." Toxicon 54, no. 8 (December 2009): 1183–89. http://dx.doi.org/10.1016/j.toxicon.2009.02.030.

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50

Thakur, Lokendra K., and Kunal K. Jha. "Palytoxin-induced acute respiratory failure." Respiratory Medicine Case Reports 20 (2017): 4–6. http://dx.doi.org/10.1016/j.rmcr.2016.10.014.

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