Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae

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

Standard

Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae. / Grimmelikhuijzen, C J; Hahn, M; Rinehart, K L; Spencer, A N.

In: Brain Research, Vol. 475, No. 1, 13.12.1988, p. 198-203.

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

Harvard

Grimmelikhuijzen, CJ, Hahn, M, Rinehart, KL & Spencer, AN 1988, 'Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae', Brain Research, vol. 475, no. 1, pp. 198-203.

APA

Grimmelikhuijzen, C. J., Hahn, M., Rinehart, K. L., & Spencer, A. N. (1988). Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae. Brain Research, 475(1), 198-203.

Vancouver

Grimmelikhuijzen CJ, Hahn M, Rinehart KL, Spencer AN. Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae. Brain Research. 1988 Dec 13;475(1):198-203.

Author

Grimmelikhuijzen, C J ; Hahn, M ; Rinehart, K L ; Spencer, A N. / Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae. In: Brain Research. 1988 ; Vol. 475, No. 1. pp. 198-203.

Bibtex

@article{6a7dd1bc2ba04ae589eb7f8469d95b3b,
title = "Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae",
abstract = "The hydromedusa Polyorchis penicillatus is a good model system to study neurotransmission in coelenterates. Using a radioimmunoassay for the peptide sequence Arg-Phe-NH2 (RFamide), two peptides have now been purified from acetic acid extracts of this medusa. The structure of one of these peptides was established as pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2, and was named Pol-RFamide. This peptide belongs to the same peptide family as a recently isolated neuropeptide from sea anemones (pyroGlu-Gly-Arg-Phe-NH2). Using antisera to Pol-RFamide, the peptide was found to be exclusively localized in neurones of Polyorchis, among them neurones associated with smooth-muscle fibres. This suggests that Pol-RFamide might be a transmitter or modulator at neuromuscular junctions.",
keywords = "Amino Acid Sequence, Animals, Cnidaria, Neuropeptides, Scyphozoa",
author = "Grimmelikhuijzen, {C J} and M Hahn and Rinehart, {K L} and Spencer, {A N}",
year = "1988",
month = dec,
day = "13",
language = "English",
volume = "475",
pages = "198--203",
journal = "Brain Research",
issn = "0006-8993",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae

AU - Grimmelikhuijzen, C J

AU - Hahn, M

AU - Rinehart, K L

AU - Spencer, A N

PY - 1988/12/13

Y1 - 1988/12/13

N2 - The hydromedusa Polyorchis penicillatus is a good model system to study neurotransmission in coelenterates. Using a radioimmunoassay for the peptide sequence Arg-Phe-NH2 (RFamide), two peptides have now been purified from acetic acid extracts of this medusa. The structure of one of these peptides was established as pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2, and was named Pol-RFamide. This peptide belongs to the same peptide family as a recently isolated neuropeptide from sea anemones (pyroGlu-Gly-Arg-Phe-NH2). Using antisera to Pol-RFamide, the peptide was found to be exclusively localized in neurones of Polyorchis, among them neurones associated with smooth-muscle fibres. This suggests that Pol-RFamide might be a transmitter or modulator at neuromuscular junctions.

AB - The hydromedusa Polyorchis penicillatus is a good model system to study neurotransmission in coelenterates. Using a radioimmunoassay for the peptide sequence Arg-Phe-NH2 (RFamide), two peptides have now been purified from acetic acid extracts of this medusa. The structure of one of these peptides was established as pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2, and was named Pol-RFamide. This peptide belongs to the same peptide family as a recently isolated neuropeptide from sea anemones (pyroGlu-Gly-Arg-Phe-NH2). Using antisera to Pol-RFamide, the peptide was found to be exclusively localized in neurones of Polyorchis, among them neurones associated with smooth-muscle fibres. This suggests that Pol-RFamide might be a transmitter or modulator at neuromuscular junctions.

KW - Amino Acid Sequence

KW - Animals

KW - Cnidaria

KW - Neuropeptides

KW - Scyphozoa

M3 - Journal article

C2 - 2905621

VL - 475

SP - 198

EP - 203

JO - Brain Research

JF - Brain Research

SN - 0006-8993

IS - 1

ER -

ID: 33514388