Isolation and Characterization of Toxic Polypeptides from Sea Anemones

Béress, L.; Béress, Rosemarie; Wunderer, Gert

doi:10.1007/978-1-4684-0802-7_23

Cited by 5 publications

(8 citation statements)

References 7 publications

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“…They are ATX-I (formula weight 4808 daltons), ATX-II (formula weight 4770 daltons) and ATX-III (formula weight 2933 daltons). The toxins are stable, basic polypeptides, and all are cross-linked in three places (Beress, Beress & Wunderer, 1975;Wunderer, Fritz, Wachter & Machleidt, 1976;Beress, Wunderer & Wachter, 1977;Wunderer & Eulitz, 1978).…”

Section: Introductionmentioning

confidence: 99%

MECHANICAL AND ELECTROPHYSIOLOGICAL EFFECTS OF SEA ANEMONE (Anemonia sulcata) TOXINS ON RAT INNERVATED AND DENERVATED SKELETAL MUSCLE

Alsen

Harris

Tesseraux

1981

British J Pharmacology

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1 Some effects of the sea-anemone toxin ATX-II on mammalian nerve-muscle preparations have been described. 2 When ATX-II (10 -8 10 -6M) was applied to rat hemidiaphragm preparations, both directly and indirectly generated twitch responses were potentiated and prolonged. At the same time the resting tension of the preparations increased. 3 The increase in resting tension caused by ATX-II in innervated muscles was not prevented by curarization, but was reversed by exposure to tetrodotoxin. The increase in denervated muscles was not completely reversed by tetrodotoxin.4 At concentrations exceeding 1 x 1 0-7 M, ATX-II caused a sodium-dependent depolarization of both normal and denervated muscles. The depolarization of the denervated muscles was only partially reversed by tetrodotoxin. S In the presence of ATX-II repetitive endplate potentials (e.p.ps) were evoked by single shocks to the motor nerves in many fibres, and in those in which a single e.p.p. was still observed, the quantum content (m) was increased. Miniature e.p.p. frequency was not increased by ATX-II, even when muscle fibres were depolarized by 30 mV. 6 The indirectly and directly elicited action potentials of normal and denervated muscle fibres were much prolonged by ATX-II. The action potentials remained sodium-dependent. The sodiumdependent tetrodotoxin-resistant action potential of the denervated muscle fibre was also prolonged by ATX-II. 7 It is concluded that ATX-II both activates, and delays inactivation of, sodium channels in mammalian skeletal muscle fibres, probably by interacting with the channel 'gate'.

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Section: Introductionmentioning

confidence: 99%

MECHANICAL AND ELECTROPHYSIOLOGICAL EFFECTS OF SEA ANEMONE (Anemonia sulcata) TOXINS ON RAT INNERVATED AND DENERVATED SKELETAL MUSCLE

Alsen

Harris

Tesseraux

1981

British J Pharmacology

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“…From nematocyst rich tissues, secretions as well as different parts or the whole body from sea anemones have been obtained different compounds of proteinic nature including pore-forming toxins or cytolisins [72][73][74], phospholipases [75], Na + channel toxins [76][77][78], K + channel inhibitors [79][80][81][82][83], other neurotoxins [84] and even proteinase inhibitors [85,86]. Nevertheless, the exact origin of both neurotoxins and cytolysins is not quite clear and others sources besides nematocysts seem to contribute to the toxicity of sea anemones [74].…”

Section: Channel Toxinsmentioning

confidence: 99%

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

Aneiros¹,

Garateix²

2004

Journal of Chromatography B

294

180

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Marine organisms represent a valuable source of new compounds. The biodiversity of the marine environment and the associated chemical diversity constitute a practically unlimited resource of new active substances in the field of the development of bioactive products. In this paper, the molecular diversity of different marine peptides is described as well as information about their biological properties and mechanisms of action is provided. Moreover, a short review about isolation procedures of selected bioactive marine peptides is offered. Novel peptides from sponges, ascidians, mollusks, sea anemones and seaweeds are presented in association with their pharmacological properties and obtainment methods.

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“…The sea anemone Anemonia sulcata contains a number of toxic polypeptides [1,2] which may assist it in capturing its prey. One of these polypeptides, designated toxin 11, has a molecular weight of 4940 and consists of 47 amino acids of known sequence [3].…”

mentioning

confidence: 99%

“…One of these polypeptides, designated toxin 11, has a molecular weight of 4940 and consists of 47 amino acids of known sequence [3]. It is toxic to crustaceans [1,2,4], exerting effects on neuromuscular transmission and nerve action potentials in the crayfish Astacus leptodactylus at nanomolar concentrations [4]. The effect of toxin I1 on nerve conduction in crayfish giant axons and frog (Rana esculentu) myelinated fibres appears to be due to a decrease in the rate of inactivation of the Na' channel, without any effect on the opening of this channel or on the K + channel [5,6].…”

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confidence: 99%

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Natural-Abundance 13C Nuclear-Magnetic-Resonance Study of Toxin II from Anemonia sulcata

Norton¹,

Zwick

Béress

2005

European Journal of Biochemistry

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Natural‐abundance 13C NMR spectra (at 15.04 MHz) of the polypeptide toxin II from the sea anemone Anemonia sulcata have been analysed and compared with corresponding spectra reported recently for a closely related polypeptide anthopleurin A. The spectra contain many resolved onecarbon and two‐carbon resonances from carbonyl, aromatic and methyl carbons, many of which have been assigned to individual carbons in the molecule on the basis of their chemical shifts, including their pH dependence, and by comparison with the 13C NMR spectrum of anthopleurin A. Analysis of the effects of pH on the spectrum yields estimates for the pKa values of a number of functional groups in the molecule, as follows: side‐chain carboxylates of the two aspartic acid residues 2 and 3.1; COOH‐terminal carboxylic acid, 3.5; imidazolium moieties of the two histidine residues, 6.7 and 7.6; NH2‐terminal ammonium, 8. The similarity between the pKa values of these functional groups in toxin II and those of corresponding groups in anthopleurin A, together with the close agreement between chemical shifts of conserved curbons, indicates that many local interactions are nearly identical in the two molecules, and thus supports the thesis that their overall conformations in solution are similar. However, the local interactions involving one of the aspartic acid residues are altered in toxin II. Together with other data, this leads to a proposal for the site in these two molecules which is responsible for their cardiac stimulatory activity.

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Isolation and Characterization of Toxic Polypeptides from Sea Anemones

Cited by 5 publications

References 7 publications

MECHANICAL AND ELECTROPHYSIOLOGICAL EFFECTS OF SEA ANEMONE (Anemonia sulcata) TOXINS ON RAT INNERVATED AND DENERVATED SKELETAL MUSCLE

MECHANICAL AND ELECTROPHYSIOLOGICAL EFFECTS OF SEA ANEMONE (Anemonia sulcata) TOXINS ON RAT INNERVATED AND DENERVATED SKELETAL MUSCLE

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

Natural-Abundance 13C Nuclear-Magnetic-Resonance Study of Toxin II from Anemonia sulcata

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