A peptide-gated ion channel from the freshwater polyp Hydra.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A peptide-gated ion channel from the freshwater polyp Hydra. / Golubovic, Andjelko; Kuhn, Anne; Williamson, Michael; Kalbacher, Hubert; Holstein, Thomas W; Grimmelikhuijzen, Cornelis J P; Gründer, Stefan.

In: Journal of Biological Chemistry, Vol. 282, No. 48, 2007, p. 35098-103.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Golubovic, A, Kuhn, A, Williamson, M, Kalbacher, H, Holstein, TW, Grimmelikhuijzen, CJP & Gründer, S 2007, 'A peptide-gated ion channel from the freshwater polyp Hydra.', Journal of Biological Chemistry, vol. 282, no. 48, pp. 35098-103. https://doi.org/10.1074/jbc.M706849200

APA

Golubovic, A., Kuhn, A., Williamson, M., Kalbacher, H., Holstein, T. W., Grimmelikhuijzen, C. J. P., & Gründer, S. (2007). A peptide-gated ion channel from the freshwater polyp Hydra. Journal of Biological Chemistry, 282(48), 35098-103. https://doi.org/10.1074/jbc.M706849200

Vancouver

Golubovic A, Kuhn A, Williamson M, Kalbacher H, Holstein TW, Grimmelikhuijzen CJP et al. A peptide-gated ion channel from the freshwater polyp Hydra. Journal of Biological Chemistry. 2007;282(48):35098-103. https://doi.org/10.1074/jbc.M706849200

Author

Golubovic, Andjelko ; Kuhn, Anne ; Williamson, Michael ; Kalbacher, Hubert ; Holstein, Thomas W ; Grimmelikhuijzen, Cornelis J P ; Gründer, Stefan. / A peptide-gated ion channel from the freshwater polyp Hydra. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 48. pp. 35098-103.

Bibtex

@article{966ce1b0ec2711dcbee902004c4f4f50,
title = "A peptide-gated ion channel from the freshwater polyp Hydra.",
abstract = "Chemical transmitters are either low molecular weight molecules or neuropeptides. As a general rule, neuropeptides activate only slow metabotropic receptors. To date, only one exception to this rule is known, the FMRFamide-activated Na(+) channel (FaNaC) from snails. Until now FaNaC has been regarded as a curiosity, and it was not known whether peptide-gated ionotropic receptors are also present in other animal groups. Nervous systems first evolved in cnidarians, which extensively use neuropeptides. Here we report cloning from the freshwater cnidarian Hydra of a novel ion channel (Hydra sodium channel, HyNaC) that is directly gated by the neuropeptides Hydra-RFamides I and II and is related to FaNaC. The cells expressing HyNaC localize to the base of the tentacles, adjacent to the neurons producing the Hydra-RFamides, suggesting that the peptides are the natural ligands for this channel. Our results suggest that neuropeptides were already used for fast transmission in ancient nervous systems.",
author = "Andjelko Golubovic and Anne Kuhn and Michael Williamson and Hubert Kalbacher and Holstein, {Thomas W} and Grimmelikhuijzen, {Cornelis J P} and Stefan Gr{\"u}nder",
note = "Keywords: Amino Acid Sequence; Animals; Cloning, Molecular; Hydra; In Situ Hybridization; Ions; Ligands; Membrane Proteins; Molecular Sequence Data; Nerve Tissue Proteins; Peptides; Phylogeny; Rats; Sequence Homology, Amino Acid; Sodium Channels",
year = "2007",
doi = "10.1074/jbc.M706849200",
language = "English",
volume = "282",
pages = "35098--103",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "48",

}

RIS

TY - JOUR

T1 - A peptide-gated ion channel from the freshwater polyp Hydra.

AU - Golubovic, Andjelko

AU - Kuhn, Anne

AU - Williamson, Michael

AU - Kalbacher, Hubert

AU - Holstein, Thomas W

AU - Grimmelikhuijzen, Cornelis J P

AU - Gründer, Stefan

N1 - Keywords: Amino Acid Sequence; Animals; Cloning, Molecular; Hydra; In Situ Hybridization; Ions; Ligands; Membrane Proteins; Molecular Sequence Data; Nerve Tissue Proteins; Peptides; Phylogeny; Rats; Sequence Homology, Amino Acid; Sodium Channels

PY - 2007

Y1 - 2007

N2 - Chemical transmitters are either low molecular weight molecules or neuropeptides. As a general rule, neuropeptides activate only slow metabotropic receptors. To date, only one exception to this rule is known, the FMRFamide-activated Na(+) channel (FaNaC) from snails. Until now FaNaC has been regarded as a curiosity, and it was not known whether peptide-gated ionotropic receptors are also present in other animal groups. Nervous systems first evolved in cnidarians, which extensively use neuropeptides. Here we report cloning from the freshwater cnidarian Hydra of a novel ion channel (Hydra sodium channel, HyNaC) that is directly gated by the neuropeptides Hydra-RFamides I and II and is related to FaNaC. The cells expressing HyNaC localize to the base of the tentacles, adjacent to the neurons producing the Hydra-RFamides, suggesting that the peptides are the natural ligands for this channel. Our results suggest that neuropeptides were already used for fast transmission in ancient nervous systems.

AB - Chemical transmitters are either low molecular weight molecules or neuropeptides. As a general rule, neuropeptides activate only slow metabotropic receptors. To date, only one exception to this rule is known, the FMRFamide-activated Na(+) channel (FaNaC) from snails. Until now FaNaC has been regarded as a curiosity, and it was not known whether peptide-gated ionotropic receptors are also present in other animal groups. Nervous systems first evolved in cnidarians, which extensively use neuropeptides. Here we report cloning from the freshwater cnidarian Hydra of a novel ion channel (Hydra sodium channel, HyNaC) that is directly gated by the neuropeptides Hydra-RFamides I and II and is related to FaNaC. The cells expressing HyNaC localize to the base of the tentacles, adjacent to the neurons producing the Hydra-RFamides, suggesting that the peptides are the natural ligands for this channel. Our results suggest that neuropeptides were already used for fast transmission in ancient nervous systems.

U2 - 10.1074/jbc.M706849200

DO - 10.1074/jbc.M706849200

M3 - Journal article

C2 - 17911098

VL - 282

SP - 35098

EP - 35103

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 48

ER -

ID: 3045658