New APETx-like peptides from sea anemone Heteractis crispa modulate ASIC1a channels

Kalina, Rimma; Leychenko, Elena; Dmitrenok, Pavel S.; Chernikov, Oleg V.; Koshelev, Sergey G.; Kvetkina, Aleksandra; Козлов, С. А.; Kozlovskaya, É. P.; Monastyrnaya, Margarita

doi:10.1016/j.peptides.2018.04.013

Cited by 34 publications

(64 citation statements)

References 38 publications

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“…In this work we conducted an in-depth investigation of two known type II Heteractis toxins-RTX-III [10] and δ-SHTX-Hcr1f (=RpII [21])-as well as a new one, RTX-VI. All of them were isolated from 20% aqueous-ethanolic fraction by hydrophobic chromatography on a Polychrome-1 [20] and purified using two-step cation exchange chromatography followed by RP-HPLC.…”

Section: Discussionmentioning

confidence: 99%

“…After extraction, peptides were eluted with 20% aqueous ethanol from a Polychrome-1 [20] and separated by cation-exchange chromatography on a Bio-Rex 70 column (Figure 1a), resulting in three distinct fractions. Fraction 2 (Figure 1a), enriched with peptides of molecular masses about 5200 Da according to the mass spectrometry data, was then fractionated on a SP-Sephadex C-25 column (Figure 1b).…”

Section: Isolation Of the Toxinsmentioning

confidence: 99%

“…Peptides were extracted from the sea anemone H. crispa using 70% ethanol and separated by hydrophobic chromatography on a Polychrome-1 (powdered Teflon, Biolar, Olaine, Latvia) column (4.8 × 95 cm) using a step gradient of ethanol concentration at a flow rate of 120 mL/h and fraction size of 20 mL [20]. The hydrophobic 20% aqueous-ethanolic fraction was further separated by cation-exchange chromatography on Bio-Rex 70 column (2.5 × 60 cm) (Bio-Rad, Richmodn, CA, USA) equilibrated with an ammonium acetate buffer (pH 4.5) at a flow rate of 22 mL/60 min and a fraction size of 5.8 mL, followed by cation-exchange chromatography on Sephadex C-25 (2.5 × 40 cm) (Amersham Biosciences, Piscataway, NJ, USA) at a flow rate of 70 mL/60 min and a fraction size of 7 mL.…”

Section: Extraction and Chromatographic Proceduresmentioning

confidence: 99%

“…The molecular mass of another peptide, RTX-VI (5240.21 Da), isolated by RP-HPLC from fraction 3 (Figure 1c), did not correspond to the mass of any previously described toxin from the Heteractis genus (Figure 1e). [20] was carried out on Bio-Rex 70 column (2.5 × 60 cm); (b) Ion-exchange chromatography of fraction 2 was carried out on SP-Sephadex C-25 column (2.5 × 50 cm). (c-e) RP-HPLC of fractions 1 and 3 on Luna C18 (10 × 250 mm) column.…”

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confidence: 99%

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New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa

Kalina

Peigneur

Zelepuga

et al. 2020

Toxins

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Toxins modulating NaV channels are the most abundant and studied peptide components of sea anemone venom. Three type-II toxins, δ-SHTX-Hcr1f (= RpII), RTX-III, and RTX-VI, were isolated from the sea anemone Heteractis crispa. RTX-VI has been found to be an unusual analog of RTX-III. The electrophysiological effects of Heteractis toxins on nine NaV subtypes were investigated for the first time. Heteractis toxins mainly affect the inactivation of the mammalian NaV channels expressed in the central nervous system (NaV1.1–NaV1.3, NaV1.6) as well as insect and arachnid channels (BgNaV1, VdNaV1). The absence of Arg13 in the RTX-VI structure does not prevent toxin binding with the channel but it has changed its pharmacological profile and potency. According to computer modeling data, the δ-SHTX-Hcr1f binds within the extracellular region of the rNaV1.2 voltage-sensing domain IV and pore-forming domain I through a network of strong interactions, and an additional fixation of the toxin at the channel binding site is carried out through the phospholipid environment. Our data suggest that Heteractis toxins could be used as molecular tools for NaV channel studies or insecticides rather than as pharmacological agents.

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Section: Discussionmentioning

confidence: 99%

Section: Isolation Of the Toxinsmentioning

confidence: 99%

Section: Extraction and Chromatographic Proceduresmentioning

confidence: 99%

mentioning

confidence: 99%

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New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa

Kalina

Peigneur

Zelepuga

et al. 2020

Toxins

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“…In addition, Hcr 1b-1, Hcr 1b-2, Hcr 1b-3 and Hcr 1b-4 have been also identified from the sea anemone Heteractis crispa and have shown neurotoxic activity by inhibiting the ASIC channels. In particular, Hcr 1b-1 is a specific ASIC3 inhibitor and Hcr 1b-2 is able to inhibit both ASIC1a and ASIC3 channels; the others are specific for the ASIC1a channel [ 123 ].…”

Section: Venoms Of Cnidariamentioning

confidence: 99%

A Review of Toxins from Cnidaria

D’Ambra

Lauritano

2020

Marine Drugs

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Cnidarians have been known since ancient times for the painful stings they induce to humans. The effects of the stings range from skin irritation to cardiotoxicity and can result in death of human beings. The noxious effects of cnidarian venoms have stimulated the definition of their composition and their activity. Despite this interest, only a limited number of compounds extracted from cnidarian venoms have been identified and defined in detail. Venoms extracted from Anthozoa are likely the most studied, while venoms from Cubozoa attract research interests due to their lethal effects on humans. The investigation of cnidarian venoms has benefited in very recent times by the application of omics approaches. In this review, we propose an updated synopsis of the toxins identified in the venoms of the main classes of Cnidaria (Hydrozoa, Scyphozoa, Cubozoa, Staurozoa and Anthozoa). We have attempted to consider most of the available information, including a summary of the most recent results from omics and biotechnological studies, with the aim to define the state of the art in the field and provide a background for future research.

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Synaptic signals mediated by protons and acid‐sensing ion channels

Uchitel

Inchauspe

Weissmann

2019

Synapse

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Extracellular pH changes may constitute significant signals for neuronal communication. During synaptic transmission, changes in pH in the synaptic cleft take place. Its role in the regulation of presynaptic Ca2+ currents through multivesicular release in ribbon‐type synapses is a proven phenomenon. In recent years, protons have been recognized as neurotransmitters that participate in neuronal communication in synapses of several regions of the CNS such as amygdala, nucleus accumbens, and brainstem. Protons are released by nerve stimulation and activate postsynaptic acid‐sensing ion channels (ASICs). Several types of ASIC channels are expressed in the peripheral and central nervous system. The influx of Ca2+ through some subtypes of ASICs, as a result of synaptic transmission, agrees with the participation of ASICs in synaptic plasticity. Pharmacological and genetical inhibition of ASIC1a results in alterations in learning, memory, and phenomena like fear and cocaine‐seeking behavior. The recognition of endogenous molecules, such as arachidonic acid, cytokines, histamine, spermine, lactate, and neuropeptides, capable of inhibiting or potentiating ASICs suggests the existence of mechanisms of synaptic modulation that have not yet been fully identified and that could be tuned by new emerging pharmacological compounds with potential therapeutic benefits.

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New APETx-like peptides from sea anemone Heteractis crispa modulate ASIC1a channels

Cited by 34 publications

References 38 publications

New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa

New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa

A Review of Toxins from Cnidaria

Synaptic signals mediated by protons and acid‐sensing ion channels

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