A Family of Acid-sensing Ion Channels from the Zebrafish

Paukert, Martin; Sidi, Samuel; Russell, Claire; Siba, Maria; Wilson, Stephen W.; Nicolson, Teresa; Gründer, Stefan

doi:10.1074/jbc.m401477200

Cited by 75 publications

(45 citation statements)

References 41 publications

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“…Moreover, and in contrast to all other zASICs, prolonged acid activation of zASIC4.1 induces a sustained current component. In contrast to zASIC4.1 but similar to rat ASIC4, zASIC4.2 is insensitive to H ϩ stimulation (22). It is not known whether zASIC4.1 and 4.2 form heteromeric channels with other zASIC subunits.…”

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confidence: 82%

“…Electrophysiology-cDNAs for zASICs have been previously described (22). Chimeric and mutant channels were generated by recombinant PCR using standard protocols with Pwo DNA polymerase (Roche Applied Science).…”

Section: Methodsmentioning

confidence: 99%

“…Like their mammalian homologs, zASICs are broadly expressed in the zebrafish central nervous system (22). We identified six ASIC subunits, zASIC1.1, 1.2, 1.3, 2, 4.1, and 4.2, that are encoded by six different genes (22).…”

mentioning

confidence: 99%

“…The amino acid sequences of zASIC4.1 and 4.2 are 68% identical; within the ectodomains identity is even 83%. Unlike rat ASIC4, zASIC4.1 forms a functional homomeric channel that is gated by extracellular H ϩ with half-maximal activation at pH ϳ5.8 (22). Moreover, and in contrast to all other zASICs, prolonged acid activation of zASIC4.1 induces a sustained current component.…”

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confidence: 99%

“…Recently, we have reported the cloning of a family of ASICs from the zebrafish (22). Like their mammalian homologs, zASICs are broadly expressed in the zebrafish central nervous system (22).…”

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confidence: 99%

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Zebrafish Acid-sensing Ion Channel (ASIC) 4, Characterization of Homo- and Heteromeric Channels, and Identification of Regions Important for Activation by H+

Chen

Polleichtner

Kadurin

et al. 2007

Journal of Biological Chemistry

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There are four genes for acid-sensing ion channels (ASICs) in the genome of mammalian species. Whereas ASIC1 to ASIC3 form functional H ؉ -gated Na ؉ channels, ASIC4 is not gated by H ؉ , and its function is unknown. Zebrafish has two ASIC4 paralogs: zASIC4.1 and zASIC4.2. Whereas zASIC4.1 is gated by extracellular H ؉ , zASIC4.2 is not. This differential response to H ؉ makes zASIC4 paralogs a good model to study the properties of this ion channel. In this study, we found that surface expression of homomeric zASIC4.2 is higher than that of zASIC4. . Upon a drop in extracellular pH, ASICs rapidly open, depolarizing the cell, and during sustained acidification they desensitize. The genome of mammals, such as mice and humans, contains four asic genes that code for at least six distinct ASIC subunits (1). ASIC subunits contain two transmembrane domains, a large extracellular loop and relatively short intracellular N and C termini (2). Functional ASICs are homo-or hetero-oligomeric assemblies of individual subunits (3-9).The ASIC1a subunit is broadly expressed throughout the central and peripheral nervous system and contributes to synaptic transmission (10, 11). ASIC1b, a splice variant of ASIC1a, is specifically expressed in the peripheral nervous system and might contribute to the perception of pain (12, 13). ASIC2a is broadly expressed in the brain and contributes to synaptic transmission by the formation of heteromeric channels with ASIC1a (3,6,8). ASIC2b, a splice variant of ASIC2a, does not generate functional channels on its own but forms heteromeric channels with other ASIC subunits, notably ASIC3 (14). ASIC3, like ASIC1b, is specifically expressed in the peripheral nervous system (15), and there is evidence for a role in the perception and processing of painful stimuli (16 -19). ASIC4 has the most restricted expression of all ASIC subunits. In humans, ASIC4 mRNA is strongly expressed only in the pituitary gland; expression in other parts of the brain is faint (20). Like ASIC2b, ASIC4 does not form a functional homomeric channel (20, 21), and unlike ASIC2b, it does apparently also not form functional heteromeric channels with other ASIC subunits (20). These properties distinguish ASIC4 from other ASIC subunits, and, whereas possible functions are emerging for all other ASIC subunits, the function of ASIC4 is still unknown.Recently, we have reported the cloning of a family of ASICs from the zebrafish (22). Like their mammalian homologs, zASICs are broadly expressed in the zebrafish central nervous system (22). We identified six ASIC subunits, zASIC1.1, 1.2, 1.3, 2, 4.1, and 4.2, that are encoded by six different genes (22). zASIC1.2 and 1.3 are paralogs of zASIC1.1, and zASIC4.2 is a paralog of zASIC4.1, respectively. The existence of paralogs in zebrafish can be at least partly explained by the fish-specific genome duplication in ray-finned fish that happened ϳ350 million years ago (23). The amino acid sequences of zASIC4.1 and 4.2 are 68% identical; within the ectodomains identity is even 83%. Unlike rat AS...

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confidence: 82%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Zebrafish Acid-sensing Ion Channel (ASIC) 4, Characterization of Homo- and Heteromeric Channels, and Identification of Regions Important for Activation by H+

Chen

Polleichtner

Kadurin

et al. 2007

Journal of Biological Chemistry

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Acid‐Sensing Ion Channels and Pain

Walder

Benson

Sluka

2009

Peripheral Receptor Targets for Analgesia

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Withanicandrin Isolated from Datura Ferox Promotes Antinociception by Modulating the Asics and TRPS Channels and Anti‐Inflammation in Adult Zebrafish

Maciel,

Liberato,

da Silva

et al. 2024

Chemistry & Biodiversity

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This is the first study to analyze the anti‐inflammatory and antinociceptive effect of withanicandrin, isolated from Datura Ferox leaves, and the possible mechanism of action involved in adult zebrafish (ZFa). To this end, the animals were treated intraperitoneally (i.p.) with withanicandrin (4; 20 and 40 mg/kg; 20 μL) and subjected to locomotor activity and acute toxicity. Nociception tests were also carried out with chemical agents, in addition to tests to evaluate inflammatory processes induced by κ‐Carrageenan 1.5% and a Molecular Docking study. As a result, withanicandrin reduced nociceptive behavior by capsaicin at a dose of 40 mg/kg and by acid saline at doses of 4 and 40 mg/kg, through neuromodulation of TRPV1 channels and ASICs, identified through blocking the antinociceptive effect of withanicandrin by the antagonists capsazepine and naloxone. Furthermore, withanicandrin caused an anti‐inflammatory effect through the reduction of abdominal edema, absence of leukocyte infiltrate in the liver tissue and reduction of ROS in thel liver tissue and presented better affinity energy compared to control morphine (TRPV1) and ibuprofen (COX‐1 and COX‐2).

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A Family of Acid-sensing Ion Channels from the Zebrafish

Cited by 75 publications

References 41 publications

Zebrafish Acid-sensing Ion Channel (ASIC) 4, Characterization of Homo- and Heteromeric Channels, and Identification of Regions Important for Activation by H+

Zebrafish Acid-sensing Ion Channel (ASIC) 4, Characterization of Homo- and Heteromeric Channels, and Identification of Regions Important for Activation by H+

Acid‐Sensing Ion Channels and Pain

Withanicandrin Isolated from Datura Ferox Promotes Antinociception by Modulating the Asics and TRPS Channels and Anti‐Inflammation in Adult Zebrafish

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