Acid-sensing ion channel (ASIC) structure and function: insights from spider, snake and sea anemone venoms

Cristofori-Armstrong, Ben and Rash, Lachlan D. (2017) Acid-sensing ion channel (ASIC) structure and function: insights from spider, snake and sea anemone venoms. Neuropharmacology, 127 173-184. doi:10.1016/j.neuropharm.2017.04.042

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Author Cristofori-Armstrong, Ben
Rash, Lachlan D.
Title Acid-sensing ion channel (ASIC) structure and function: insights from spider, snake and sea anemone venoms
Journal name Neuropharmacology   Check publisher's open access policy
ISSN 0028-3908
1873-7064
Publication date 2017-04-27
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.neuropharm.2017.04.042
Open Access Status File (Author Post-print)
Volume 127
Start page 173
End page 184
Total pages 12
Place of publication Kidlington, Oxford, United Kingdom
Publisher Pergamon Press
Language eng
Subject 3004 Pharmacology
2804 Cellular and Molecular Neuroscience
Abstract Acid-sensing ion channels (ASICs) are proton-activated cation channels that are expressed in a variety of neuronal and non-neuronal tissues. As proton-gated channels, they have been implicated in many pathophysiological conditions where pH is perturbed. Venom derived compounds represent the most potent and selective modulators of ASICs described to date, and thus have been invaluable as pharmacological tools to study ASIC structure, function, and biological roles. There are now ten ASIC modulators described from animal venoms, with those from snakes and spiders favouring ASIC1, while the sea anemones preferentially target ASIC3. Some modulators, such as the prototypical ASIC1 modulator PcTx1 have been studied in great detail, while some of the newer members of the club remain largely unstudied. Here we review the current state of knowledge on venom derived ASIC modulators, with a particular focus on their molecular interaction with ASICs, what they have taught us about channel structure, and what they might still reveal about ASIC function and pathophysiological roles.
Keyword Acid-sensing ion channel
ASIC
Venom
Peptide
Pharmacology
Ion channel
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID APP1067940
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: HERDC Pre-Audit
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
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Created: Fri, 02 Jun 2017, 12:19:08 EST by Dr Lachlan Rash on behalf of School of Biomedical Sciences