Rapid toxin sequestration modifies poison frog physiology
Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological adaptations that confer this unusual bioaccumulation ability. We conducted an alkaloid-feeding experiment with the Diablito poison frog ( ) to det...
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Published in | Journal of experimental biology Vol. 224; no. Pt 3 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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01.02.2021
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Abstract | Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological adaptations that confer this unusual bioaccumulation ability. We conducted an alkaloid-feeding experiment with the Diablito poison frog (
) to determine how quickly alkaloids are accumulated and how toxins modify frog physiology using quantitative proteomics. Diablito frogs rapidly accumulated the alkaloid decahydroquinoline within 4 days, and dietary alkaloid exposure altered protein abundance in the intestines, liver and skin. Many proteins that increased in abundance with decahydroquinoline accumulation are plasma glycoproteins, including the complement system and the toxin-binding protein saxiphilin. Other protein classes that change in abundance with decahydroquinoline accumulation are membrane proteins involved in small molecule transport and metabolism. Overall, this work shows that poison frogs can rapidly accumulate alkaloids, which alter carrier protein abundance, initiate an immune response, and alter small molecule transport and metabolism dynamics across tissues. |
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AbstractList | Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological adaptations that confer this unusual bioaccumulation ability. We conducted an alkaloid-feeding experiment with the Diablito poison frog (
) to determine how quickly alkaloids are accumulated and how toxins modify frog physiology using quantitative proteomics. Diablito frogs rapidly accumulated the alkaloid decahydroquinoline within 4 days, and dietary alkaloid exposure altered protein abundance in the intestines, liver and skin. Many proteins that increased in abundance with decahydroquinoline accumulation are plasma glycoproteins, including the complement system and the toxin-binding protein saxiphilin. Other protein classes that change in abundance with decahydroquinoline accumulation are membrane proteins involved in small molecule transport and metabolism. Overall, this work shows that poison frogs can rapidly accumulate alkaloids, which alter carrier protein abundance, initiate an immune response, and alter small molecule transport and metabolism dynamics across tissues. Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological adaptations that confer this unusual bioaccumulation ability. We conducted an alkaloid-feeding experiment with the Diablito poison frog ( Oophaga sylvatica ) to determine how quickly alkaloids are accumulated and how toxins modify frog physiology using quantitative proteomics. Diablito frogs rapidly accumulated the alkaloid decahydroquinoline within 4 days, and dietary alkaloid exposure altered protein abundance in the intestines, liver and skin. Many proteins that increased in abundance with decahydroquinoline accumulation are plasma glycoproteins, including the complement system and the toxin-binding protein saxiphilin. Other protein classes that change in abundance with decahydroquinoline accumulation are membrane proteins involved in small molecule transport and metabolism. Overall, this work shows that poison frogs can rapidly accumulate alkaloids, which alter carrier protein abundance, initiate an immune response, and alter small molecule transport and metabolism dynamics across tissues. Summary: Poison frogs rapidly accumulate toxins, which changes the abundance of proteins involved in the immune system and small molecule binding and metabolism across tissues. ABSTRACT Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological adaptations that confer this unusual bioaccumulation ability. We conducted an alkaloid-feeding experiment with the Diablito poison frog (Oophaga sylvatica) to determine how quickly alkaloids are accumulated and how toxins modify frog physiology using quantitative proteomics. Diablito frogs rapidly accumulated the alkaloid decahydroquinoline within 4 days, and dietary alkaloid exposure altered protein abundance in the intestines, liver and skin. Many proteins that increased in abundance with decahydroquinoline accumulation are plasma glycoproteins, including the complement system and the toxin-binding protein saxiphilin. Other protein classes that change in abundance with decahydroquinoline accumulation are membrane proteins involved in small molecule transport and metabolism. Overall, this work shows that poison frogs can rapidly accumulate alkaloids, which alter carrier protein abundance, initiate an immune response, and alter small molecule transport and metabolism dynamics across tissues. |
Author | Gygi, Steven P O'Connell, Jeremy D O'Connell, Lauren A Paulo, Joao A Trauger, Sunia A Murray, Andrew W |
AuthorAffiliation | 4 Harvard Center for Mass Spectrometry, Harvard University , Cambridge, MA 02138 , USA 3 Department of Cell Biology, Harvard Medical School, Boston, MA 02115 , USA 1 Department of Biology , Stanford University , Stanford, CA 94305 , USA 2 Department of Molecular and Cellular Biology , Harvard University , Cambridge, MA 02138 , USA 5 Department of Molecular and Cellular Biology , Harvard University , Cambridge, MA 02138 , USA |
AuthorAffiliation_xml | – name: 3 Department of Cell Biology, Harvard Medical School, Boston, MA 02115 , USA – name: 1 Department of Biology , Stanford University , Stanford, CA 94305 , USA – name: 4 Harvard Center for Mass Spectrometry, Harvard University , Cambridge, MA 02138 , USA – name: 5 Department of Molecular and Cellular Biology , Harvard University , Cambridge, MA 02138 , USA – name: 2 Department of Molecular and Cellular Biology , Harvard University , Cambridge, MA 02138 , USA |
Author_xml | – sequence: 1 givenname: Lauren A orcidid: 0000-0002-2706-4077 surname: O'Connell fullname: O'Connell, Lauren A email: loconnel@stanford.edu organization: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA – sequence: 2 givenname: Jeremy D surname: O'Connell fullname: O'Connell, Jeremy D organization: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA – sequence: 3 givenname: Joao A surname: Paulo fullname: Paulo, Joao A organization: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA – sequence: 4 givenname: Sunia A surname: Trauger fullname: Trauger, Sunia A organization: Harvard Center for Mass Spectrometry, Harvard University, Cambridge, MA 02138, USA – sequence: 5 givenname: Steven P surname: Gygi fullname: Gygi, Steven P organization: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA – sequence: 6 givenname: Andrew W orcidid: 0000-0002-0868-6604 surname: Murray fullname: Murray, Andrew W organization: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA |
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Cites_doi | 10.1007/s00049-009-0018-6 10.1073/pnas.1010952108 10.1016/j.toxicon.2010.04.007 10.1007/s10886-013-0361-5 10.1007/s00049-012-0112-z 10.1016/0041-0101(94)90335-2 10.1021/acs.jproteome.6b01050 10.1021/ac502040v 10.1016/j.cell.2010.12.001 10.1073/pnas.1511706112 10.1007/BF02059589 10.1007/978-1-60761-444-9_5 10.1073/pnas.2133521100 10.1073/pnas.1834430100 10.1021/np0580560 10.1038/s41467-017-01710-1 10.1016/0003-9861(88)90487-0 10.1086/426599 10.1034/j.1600-065X.2001.1800103.x 10.1002/jmor.11021 10.1016/S1028-4559(09)60296-5 10.1007/s00049-011-0088-0 10.1111/febs.12302 10.2165/00003088-200140030-00002 10.3390/genes10100733 10.1007/s10886-016-0715-x 10.1016/0040-8166(79)90029-6 10.1016/j.cub.2014.05.044 10.1002/ece3.3503 10.1126/sciadv.aax2650 10.1016/0041-0101(91)90039-T 10.1007/978-3-319-22026-0_21 10.2174/1389200023337054 10.1016/j.toxicon.2019.12.090 10.3987/REV-08-SR(D)11 10.1016/j.canlet.2015.10.010 10.1016/j.molimm.2014.06.020 10.1038/nrd4626 10.1890/13-0927.1 10.1016/S0169-409X(02)00169-2 10.1016/j.addr.2007.09.007 10.1242/jeb.204149 10.1093/nar/gkv007 |
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Keywords | Alkaloids Cytochrome P450s Complement system Saxiphilin Proteomics |
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References | Liu (2021042623074000500_JEB230342C16) 2009; 48 Wühr (2021042623074000500_JEB230342C41) 2014; 24 Santos (2021042623074000500_JEB230342C31) 2016; 13 Lin (2021042623074000500_JEB230342C15) 2015; 14 McGugan (2021042623074000500_JEB230342C19) 2016; 42 Darst (2021042623074000500_JEB230342C10) 2005; 165 Daly (2021042623074000500_JEB230342C7) 2005; 68 Mahar (2021042623074000500_JEB230342C17) 1991; 29 Elias (2021042623074000500_JEB230342C11) 2010; 604 Raaymakers (2021042623074000500_JEB230342C24) 2017; 8 Saporito (2021042623074000500_JEB230342C33) 2011; 22 Savitzky (2021042623074000500_JEB230342C34) 2012; 22 Sanchez (2021042623074000500_JEB230342C28) 2019; 10 Danielson (2021042623074000500_JEB230342C9) 2002; 3 Ritchie (2021042623074000500_JEB230342C25) 2015; 43 Alston (2021042623074000500_JEB230342C1) 1988; 260 Neuwirth (2021042623074000500_JEB230342C20) 1979; 11 Prates (2021042623074000500_JEB230342C23) 2012; 273 Ujvari (2021042623074000500_JEB230342C39) 2015; 112 Gibbs (2021042623074000500_JEB230342C12) 2020; 177 Sahu (2021042623074000500_JEB230342C27) 2001; 180 Daly (2021042623074000500_JEB230342C6) 2003; 100 Opitz (2021042623074000500_JEB230342C21) 2009; 19 Huttlin (2021042623074000500_JEB230342C14) 2010; 143 McAlister (2021042623074000500_JEB230342C18) 2014; 86 Zhang (2021042623074000500_JEB230342C43) 2001; 40 Hantak (2021042623074000500_JEB230342C13) 2013; 39 Santos (2021042623074000500_JEB230342C30) 2003; 100 Roland (2021042623074000500_JEB230342C26) 2016; 7 Perálvarez-Marín (2021042623074000500_JEB230342C22) 2013; 280 Santos (2021042623074000500_JEB230342C29) 2011; 108 Chen (2021042623074000500_JEB230342C3) 2016; 370 Trevaskis (2021042623074000500_JEB230342C38) 2008; 60 Daly (2021042623074000500_JEB230342C4) 1994; 20 Saporito (2021042623074000500_JEB230342C32) 2009; 79 Schinkel (2021042623074000500_JEB230342C35) 2003; 55 Stynoski (2021042623074000500_JEB230342C36) 2014; 95 Daly (2021042623074000500_JEB230342C5) 1994; 32 Caty (2021042623074000500_JEB230342C2) 2019; 222 Vogel (2021042623074000500_JEB230342C40) 2010; 56 Yen (2021042623074000500_JEB230342C42) 2019; 5 D'Angelo (2021042623074000500_JEB230342C8) 2017; 16 Tambourgi (2021042623074000500_JEB230342C37) 2014; 61 |
References_xml | – volume: 19 start-page: 117 year: 2009 ident: 2021042623074000500_JEB230342C21 article-title: Plant chemistry and insect sequestration publication-title: Chemoecology doi: 10.1007/s00049-009-0018-6 contributor: fullname: Opitz – volume: 108 start-page: 6175 year: 2011 ident: 2021042623074000500_JEB230342C29 article-title: Phenotypic integration emerges from aposematism and scale in poison frogs publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1010952108 contributor: fullname: Santos – volume: 56 start-page: 1198 year: 2010 ident: 2021042623074000500_JEB230342C40 article-title: Cobra venom factor: Structure, function, and humanization for therapeutic complement depletion publication-title: Toxicon doi: 10.1016/j.toxicon.2010.04.007 contributor: fullname: Vogel – volume: 39 start-page: 1400 year: 2013 ident: 2021042623074000500_JEB230342C13 article-title: Dietary alkaloid sequestration in a poison frog: an experimental test of alkaloid uptake in Melanophryniscus stelzneri (Bufonidae) publication-title: J. Chem. Ecol. doi: 10.1007/s10886-013-0361-5 contributor: fullname: Hantak – volume: 22 start-page: 141 year: 2012 ident: 2021042623074000500_JEB230342C34 article-title: Sequestered defensive toxins in tetrapod vertebrates: principles, patterns, and prospects for future studies publication-title: Chemoecology doi: 10.1007/s00049-012-0112-z contributor: fullname: Savitzky – volume: 32 start-page: 657 year: 1994 ident: 2021042623074000500_JEB230342C5 article-title: An uptake system for dietary alkaloids in poison frogs (Dendrobatidae) publication-title: Toxicon doi: 10.1016/0041-0101(94)90335-2 contributor: fullname: Daly – volume: 16 start-page: 3124 year: 2017 ident: 2021042623074000500_JEB230342C8 article-title: Statistical models for the analysis of isobaric tags multiplexed quantitative proteomics publication-title: J. Proteome Res. doi: 10.1021/acs.jproteome.6b01050 contributor: fullname: D'Angelo – volume: 86 start-page: 7150 year: 2014 ident: 2021042623074000500_JEB230342C18 article-title: MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes publication-title: Anal. Chem. doi: 10.1021/ac502040v contributor: fullname: McAlister – volume: 143 start-page: 1174 year: 2010 ident: 2021042623074000500_JEB230342C14 article-title: A tissue-specific atlas of mouse protein phosphorylation and expression publication-title: Cell doi: 10.1016/j.cell.2010.12.001 contributor: fullname: Huttlin – volume: 112 start-page: 11911 year: 2015 ident: 2021042623074000500_JEB230342C39 article-title: Widespread convergence in toxin resistance by predictable molecular evolution publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1511706112 contributor: fullname: Ujvari – volume: 20 start-page: 943 year: 1994 ident: 2021042623074000500_JEB230342C4 article-title: Dietary source for skin alkaloids of poison frogs (Dendrobatidae)? publication-title: J. Chem. Ecol. doi: 10.1007/BF02059589 contributor: fullname: Daly – volume: 604 start-page: 55 year: 2010 ident: 2021042623074000500_JEB230342C11 article-title: Target-decoy search strategy for mass spectrometry-based proteomics publication-title: Methods Mol. Biol. doi: 10.1007/978-1-60761-444-9_5 contributor: fullname: Elias – volume: 100 start-page: 12792 year: 2003 ident: 2021042623074000500_JEB230342C30 article-title: Multiple, recurring origins of aposematism and diet specialization in poison frogs publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.2133521100 contributor: fullname: Santos – volume: 100 start-page: 11092 year: 2003 ident: 2021042623074000500_JEB230342C6 article-title: Evidence for an enantioselective pumiliotoxin 7-hydroxylase in dendrobatid poison frogs of the genus Dendrobates publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1834430100 contributor: fullname: Daly – volume: 68 start-page: 1556 year: 2005 ident: 2021042623074000500_JEB230342C7 article-title: Alkaloids from amphibian skin: a tabulation of over eight-hundred compounds publication-title: J. Nat. Prod. doi: 10.1021/np0580560 contributor: fullname: Daly – volume: 8 start-page: 1495 year: 2017 ident: 2021042623074000500_JEB230342C24 article-title: Antimicrobial peptides in frog poisons constitute a molecular toxin delivery system against predators publication-title: Nat. Commun. doi: 10.1038/s41467-017-01710-1 contributor: fullname: Raaymakers – volume: 260 start-page: 601 year: 1988 ident: 2021042623074000500_JEB230342C1 article-title: Substrate specificity of nicotinamide methyltransferase isolated from porcine liver publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(88)90487-0 contributor: fullname: Alston – volume: 165 start-page: 56 year: 2005 ident: 2021042623074000500_JEB230342C10 article-title: Evolution of dietary specialization and chemical defense in poison frogs (Dendrobatidae): a comparative analysis publication-title: Am. Nat. doi: 10.1086/426599 contributor: fullname: Darst – volume: 180 start-page: 35 year: 2001 ident: 2021042623074000500_JEB230342C27 article-title: Structure and biology of complement protein C3, a connecting link between innate and acquired immunity publication-title: Immunol. Rev. doi: 10.1034/j.1600-065X.2001.1800103.x contributor: fullname: Sahu – volume: 273 start-page: 279 year: 2012 ident: 2021042623074000500_JEB230342C23 article-title: Skin glands, poison and mimicry in dendrobatid and leptodactylid amphibians publication-title: J. Morphol. doi: 10.1002/jmor.11021 contributor: fullname: Prates – volume: 48 start-page: 239 year: 2009 ident: 2021042623074000500_JEB230342C16 article-title: Mechanisms of chemotherapeutic drug resistance in cancer therapy—a quick review publication-title: Taiwan. J. Obstet. Gynecol. doi: 10.1016/S1028-4559(09)60296-5 contributor: fullname: Liu – volume: 22 start-page: 159 year: 2011 ident: 2021042623074000500_JEB230342C33 article-title: A review of chemical ecology in poison frogs publication-title: Chemoecology doi: 10.1007/s00049-011-0088-0 contributor: fullname: Saporito – volume: 280 start-page: 5471 year: 2013 ident: 2021042623074000500_JEB230342C22 article-title: What do we know about the transient receptor potential vanilloid 2 (TRPV2) ion channel? publication-title: FEBS J. doi: 10.1111/febs.12302 contributor: fullname: Perálvarez-Marín – volume: 40 start-page: 159 year: 2001 ident: 2021042623074000500_JEB230342C43 article-title: The Gut as a barrier to drug absorption publication-title: Clin. Pharmacokinet. doi: 10.2165/00003088-200140030-00002 contributor: fullname: Zhang – volume: 10 start-page: 733 year: 2019 ident: 2021042623074000500_JEB230342C28 article-title: Transcriptomic signatures of experimental alkaloid consumption in a poison frog publication-title: Genes doi: 10.3390/genes10100733 contributor: fullname: Sanchez – volume: 42 start-page: 537 year: 2016 ident: 2021042623074000500_JEB230342C19 article-title: Ant and mite diversity drives toxin variation in the little devil poison frog publication-title: J. Chem. Ecol. doi: 10.1007/s10886-016-0715-x contributor: fullname: McGugan – volume: 11 start-page: 755 year: 1979 ident: 2021042623074000500_JEB230342C20 article-title: Morphology of the granular secretory glands in skin of poison-dart frogs (Dendrobatidae) publication-title: Tissue Cell doi: 10.1016/0040-8166(79)90029-6 contributor: fullname: Neuwirth – volume: 24 start-page: 1467 year: 2014 ident: 2021042623074000500_JEB230342C41 article-title: Deep proteomics of the Xenopus laevis egg using an mRNA-derived reference database publication-title: Curr. Biol. doi: 10.1016/j.cub.2014.05.044 contributor: fullname: Wühr – volume: 7 start-page: 9750 year: 2016 ident: 2021042623074000500_JEB230342C26 article-title: Radiation and hybridization of the Little Devil poison frog (Oophaga sylvatica) in Ecuador publication-title: Ecol. Evol. doi: 10.1002/ece3.3503 contributor: fullname: Roland – volume: 5 start-page: eaax2650 year: 2019 ident: 2021042623074000500_JEB230342C42 article-title: Structure of the saxiphilin:saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins publication-title: Sci. Adv. doi: 10.1126/sciadv.aax2650 contributor: fullname: Yen – volume: 29 start-page: 53 year: 1991 ident: 2021042623074000500_JEB230342C17 article-title: Pharmacological and biochemical properties of saxiphilin, a soluble saxitoxin-binding protein from the bullfrog (Rana catesbeiana) publication-title: Toxicon doi: 10.1016/0041-0101(91)90039-T contributor: fullname: Mahar – volume: 13 start-page: 305 year: 2016 ident: 2021042623074000500_JEB230342C31 article-title: A review of chemical defense in poison frogs (Dendrobatidae): ecology, pharmacokinetics, and autoresistance publication-title: Chem. Signal. Vertebr. doi: 10.1007/978-3-319-22026-0_21 contributor: fullname: Santos – volume: 3 start-page: 561 year: 2002 ident: 2021042623074000500_JEB230342C9 article-title: The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans publication-title: Curr. Drug Metab. doi: 10.2174/1389200023337054 contributor: fullname: Danielson – volume: 177 start-page: S46 year: 2020 ident: 2021042623074000500_JEB230342C12 article-title: The molecular basis of venom resistance in a rattlesnake-squirrel predator-prey system publication-title: Mol. Ecol. doi: 10.1016/j.toxicon.2019.12.090 contributor: fullname: Gibbs – volume: 79 start-page: 277 year: 2009 ident: 2021042623074000500_JEB230342C32 article-title: Arthropod alkaloids in poison frogs: a review of the “dietary hypothesis” publication-title: Heterocycles doi: 10.3987/REV-08-SR(D)11 contributor: fullname: Saporito – volume: 370 start-page: 153 year: 2016 ident: 2021042623074000500_JEB230342C3 article-title: Mammalian drug efflux transporters of the ATP binding cassette (ABC) family in multidrug resistance: a review of the past decade publication-title: Cancer Lett. doi: 10.1016/j.canlet.2015.10.010 contributor: fullname: Chen – volume: 61 start-page: 153 year: 2014 ident: 2021042623074000500_JEB230342C37 article-title: Animal venoms/toxins and the complement system publication-title: Mol. Immunol. doi: 10.1016/j.molimm.2014.06.020 contributor: fullname: Tambourgi – volume: 14 start-page: 543 year: 2015 ident: 2021042623074000500_JEB230342C15 article-title: SLC transporters as therapeutic targets: emerging opportunities publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd4626 contributor: fullname: Lin – volume: 95 start-page: 587 year: 2014 ident: 2021042623074000500_JEB230342C36 article-title: Evidence of maternal provisioning of alkaloid-based chemical defenses in the strawberry poison frog Oophaga pumilio publication-title: Ecology doi: 10.1890/13-0927.1 contributor: fullname: Stynoski – volume: 55 start-page: 3 year: 2003 ident: 2021042623074000500_JEB230342C35 article-title: Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: an overview publication-title: Adv. Drug Deliv. Rev. doi: 10.1016/S0169-409X(02)00169-2 contributor: fullname: Schinkel – volume: 60 start-page: 702 year: 2008 ident: 2021042623074000500_JEB230342C38 article-title: Lipid-based delivery systems and intestinal lymphatic drug transport: a mechanistic update publication-title: Adv. Drug Deliv. Rev. doi: 10.1016/j.addr.2007.09.007 contributor: fullname: Trevaskis – volume: 222 start-page: 1 year: 2019 ident: 2021042623074000500_JEB230342C2 article-title: Molecular physiology of chemical defenses in a poison frog publication-title: J. Exp. Biol. doi: 10.1242/jeb.204149 contributor: fullname: Caty – volume: 43 start-page: e47 year: 2015 ident: 2021042623074000500_JEB230342C25 article-title: limma powers differential expression analyses for RNA-sequencing and microarray studies publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv007 contributor: fullname: Ritchie |
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Snippet | Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the physiological... ABSTRACT Poison frogs sequester chemical defenses from their diet of leaf litter arthropods for defense against predation. Little is known about the... |
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SubjectTerms | Animals Anura Arthropods Poisons Predatory Behavior Short Communication Toxins, Biological - toxicity |
Title | Rapid toxin sequestration modifies poison frog physiology |
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