Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus

Papp, Ferenc; Batista, Cesar Vicente Ferreira; Varga, Zoltán; Herceg, Monika; Román-González, Sergio A.; Gáspár, R.; Possani, Lourival D.; Panyi, György

doi:10.1016/j.toxicon.2009.05.023

Cited by 28 publications

(15 citation statements)

References 34 publications

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“…Inhibit current, ShIR, Xenopus oocytes, 1 mM, (Cerni et al, 2014) Inhibit current, Rat, Xenopus oocytes, 1 mM, (Cerni et al, 2014) Inhibit current, CL1023, Kd ¼ 0.21 nM, (Werkman et al, 1993); Inhibit current, Rat, Xenopus oocytes, 1 mM, (Cerni et al, 2014) Inhibit current, Mouse, Xenopus oocytes, Kd ¼ 3.9 nM, (Rodrigues et al, 2003); Inhibit current, Mouse, L929, Kd ¼ 198 nM, (Rodrigues et al, 2003); Inhibit current, Rat, Xenopus oocytes, 1 mM, (Cerni et al, 2014) Inhibit current, Rat, Xenopus oocytes, 1 mM, (Cerni et al, 2014) Tst26 a-KTx 4.6 Tityus stigmurus Inhibit current, Human, COS7, Kd ¼ 1.9 nM, (Papp et al, 2009) Inhibit current, Human T lymphocyte, Kd ¼ 10.7 nM, (Papp et al, 2009) (Varga et al, 2012) Inhibit current, Human, COS7, Kd ¼ 5e10 nM, (Varga et al, 2012) Inhibit current, Human T lymphocytes, Kd ¼ 3 pM, (Gurrola et al, 2012); Inhibit current, Human T lymphocytes, Kd ¼ 2.9 pM, (Varga et al, 2012) a-KTx 2.14…”

Section: Tityus Serrulatusmentioning

confidence: 99%

Scorpion toxin peptide action at the ion channel subunit level

Housley

Liddell

et al. 2017

Neuropharmacology

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a b s t r a c tThis review categorizes functionally validated actions of defined scorpion toxin (SCTX) neuropeptides across ion channel subclasses, highlighting key trends in this rapidly evolving field. Scorpion envenomation is a common event in many tropical and subtropical countries, with neuropharmacological actions, particularly autonomic nervous system modulation, causing significant mortality. The primary active agents within scorpion venoms are a diverse group of small neuropeptides that elicit specific potent actions across a wide range of ion channel classes. The identification and functional characterisation of these SCTX peptides has tremendous potential for development of novel pharmaceuticals that advance knowledge of ion channels and establish lead compounds for treatment of excitable tissue disorders. This review delineates the unique specificities of 320 individual SCTX peptides that collectively act on 41 ion channel subclasses. Thus the SCTX research field has significant translational implications for pathophysiology spanning neurotransmission, neurohumoral signalling, sensori-motor systems and excitation-contraction coupling.This article is part of the Special Issue entitled 'Venom-derived Peptides as Pharmacological Tools.'

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Section: Tityus Serrulatusmentioning

confidence: 99%

Scorpion toxin peptide action at the ion channel subunit level

Housley

Liddell

et al. 2017

Neuropharmacology

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“…This approach results in often complicated names that provide broad information, but lack ease of use. To illustrate this heterogeneity, we cite alpha-conotoxin-like PuSG1.1 [29], where SG stands for Salivary Gland, or scorpion Tst26, a protein recovered from a column after a 26 minute elution [30].…”

Section: Nomenclature Issuesmentioning

confidence: 99%

Animal Toxins: How is Complexity Represented in Databases?

Jungo¹,

Estreicher

Bairoch

et al. 2010

Toxins

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Peptide toxins synthesized by venomous animals have been extensively studied in the last decades. To be useful to the scientific community, this knowledge has been stored, annotated and made easy to retrieve by several databases. The aim of this article is to present what type of information users can access from each database. ArachnoServer and ConoServer focus on spider toxins and cone snail toxins, respectively. UniProtKB, a generalist protein knowledgebase, has an animal toxin-dedicated annotation program that includes toxins from all venomous animals. Finally, the ATDB metadatabase compiles data and annotations from other databases and provides toxin ontology.

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“…O complexo toxina-canal necessita de múltiplos contatos para se efetivar, permitindo que a toxina realize sua ação bloqueadora (Papp et al, 2009). Além disso, outros trabalhos demonstram que a teoria da díade não funciona exatamente como o modelo predito (Tong et al, 2000;Batista et al, 2002;Dhawan et al, 2003).…”

Section: Discussionunclassified

“…Ainda, essas informações combinadas com técnicas de biologia molecular podem ser úteis na produção de toxinas recombinantes com alta seletividade e afinidade para canais para potássio com efeito terapêutico desejado (Papp et al, 2009).…”

Section: Discussionunclassified

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Novo método de fracionamento da peçonha do escorpião Tityus serrulatus e caracterização eletrofisiológica das toxinas Ts6 e Ts7

Cerni¹

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Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus

Cited by 28 publications

References 34 publications

Scorpion toxin peptide action at the ion channel subunit level

Scorpion toxin peptide action at the ion channel subunit level

Animal Toxins: How is Complexity Represented in Databases?

Novo método de fracionamento da peçonha do escorpião Tityus serrulatus e caracterização eletrofisiológica das toxinas Ts6 e Ts7

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