G protein-coupled receptors, an unexploited animal toxin targets: Exploration of green mamba venom for novel drug candidates active against adrenoceptors

Maïga, Arhamatoulaye; Mourier, Gilles; Quinton, Loïc; Rouget, Céline; Galès, Céline; Denis, Colette; Lluel, Philippe; Sénard, Jean-Michel; Palea, Stéfano; Servent, Denis; Gilles, Nicolas

doi:10.1016/j.toxicon.2011.03.009

Cited by 37 publications

(32 citation statements)

References 42 publications

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“…The ability to sequence toxins directly by mass spectrometric analysis of venoms [3], combined with the sequencing of the genomes of venomous animals [4,5], will certainly help to increase the rate of discovered and characterized peptide toxins over the next few years. The pharmacologic activity of peptide toxins is mostly related to their binding to ion channels, such as voltage-gated and ligand-gated ionic channels, highly involved in controlling the mobility of their prey [4,[6][7][8], but also to other kinds of receptors such as G-protein coupled receptor [9], integrine receptors [10], or enzymes as acetylcholine esterase [11]. Another characteristic of animal toxins is the remarkable number and variety of post-translational modifications (PTMs).…”

Section: Introductionmentioning

confidence: 99%

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An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation

Quinton

Gilles

Smargiasso

et al. 2011

J. Am. Soc. Mass Spectrom.

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This study describes the structural characterization of a totally new family of peptides from the venom of the snake green mamba (Dendroaspis angusticeps). Interestingly, these peptides differ in several points from other already known mamba toxins. First of all, they exhibit very small molecular masses, ranging from 1.3 to 2.4 kDa. The molecular mass of classical mamba toxins is in the range of 7 to 25 kDa. Second, the new peptides do not contain disulfide bonds, a posttranslational modification commonly encountered in animal toxins. The third difference is the very high proportion of proline residues in the sequence accounting for about one-third of the sequence. Finally, these new peptides reveal a carbohydrate moiety, indicating a glycosylation in the sequence. The last two features have made the structural characterization of the new peptides by mass spectrometry a real analytical challenge. Peptides were characterized by a combined use of MALDI-TOF/TOF and nanoESI-IT-ETD experiments to determine not only the peptide sequence but also the composition and the position of the carbohydrate moiety. Anyway, such small glycosylated and proline-rich toxins are totally different from any other known snake peptide and form, as a consequence, a new family of peptides.

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Section: Introductionmentioning

confidence: 99%

“…Mamba venoms mainly consist of high mass toxins such as some neurotoxins (dendrotoxins) [24], acetyl cholinesterase inhibitors (fasciculins) [11], muscarinic toxins [25], or adrenergic toxins [9].…”

Section: Introductionmentioning

confidence: 99%

An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation

Quinton

Gilles

Smargiasso

et al. 2011

J. Am. Soc. Mass Spectrom.

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“…We also would like to mention here the recent discovery of three-finger neurotoxins which interact with another group of GPCR, namely with the adrenoreceptors [54,55]. These toxins are most similar to muscarinic toxins and were also isolated from the eastern green mamba Dendroaspis angusticeps.…”

Section: Three-finger Snake Neurotoxins Having Other Targets Than Nicmentioning

confidence: 93%

Peptide and Protein Neurotoxin Toolbox in Research on Nicotinic Acetylcholine Receptors

Tsetlin¹,

Kasheverov²

2014

Neurochemistry

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“…Nevertheless, some GPCR-based drugs show potent anti-tumor efficacy e.g. the endothelin A receptor antagonists -ZD4054 and atrasentan [157,[165][166][167]. GPCR-based drugs may also show therapeutic benefits in the regulation of apoptosis in chronic liver diseases and liver tumors.…”

Section: G-protein Coupled Receptorsmentioning

confidence: 99%

Hepatocyte Apoptosis at the Interplay of Intracellular Organelles and Membrane-Bound Receptors: Targets for Therapy

Karimian

Faber²,

Moshage³

2012

Clin Exp Pharmacol

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Hepatocyte apoptosis is ubiquitous in liver diseases. Although apoptosis is primarily a non-inflammatory process responsible for removing excess or damaged cells, un-controlled apoptosis can deteriorate organ function. E.g. if apoptotic bodies are not eliminated, their membranes become permeable, leading to the release of cellular fragments into the extracellular space and triggering an inflammatory response, a process called secondary necrosis. In massive liver injury, the ability of phagocytes to identify and clear apoptotic bodies is likely disturbed and an inflammatory response is observed despite an initial apoptotic stimulus in the liver. Therefore, understanding the cellular processes and molecular signaling pathways regulating apoptosis and/or necrosis in hepatocytes is essential to the development of new therapeutic strategies for (chronic) liver diseases. In particular, the intracellular organelles and membrane receptors that are involved in hepatocyte cell death and their interactions are of substantial interest, as a single toxic stimulus often activates several intracellular apoptotic pathways simultaneously. In this review, we discuss recent advances in organelle-mediated and membrane receptor-mediated cell death and potential targets for therapy in hepatocytes.

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G protein-coupled receptors, an unexploited animal toxin targets: Exploration of green mamba venom for novel drug candidates active against adrenoceptors

Cited by 37 publications

References 42 publications

An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation

An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation

Peptide and Protein Neurotoxin Toolbox in Research on Nicotinic Acetylcholine Receptors

Hepatocyte Apoptosis at the Interplay of Intracellular Organelles and Membrane-Bound Receptors: Targets for Therapy

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