Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2

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

Standard

Isolation of two novel neuropeptides from sea anemones : The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2. / Nothacker, Hans Peter; Rinehart, Kenneth L.; McFarlane, Ian D.; Grimmelikhuijzen, Cornelis J.P.

In: Peptides, Vol. 12, No. 6, 1991, p. 1165-1173.

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

Harvard

Nothacker, HP, Rinehart, KL, McFarlane, ID & Grimmelikhuijzen, CJP 1991, 'Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2', Peptides, vol. 12, no. 6, pp. 1165-1173. https://doi.org/10.1016/0196-9781(91)90190-Z

APA

Nothacker, H. P., Rinehart, K. L., McFarlane, I. D., & Grimmelikhuijzen, C. J. P. (1991). Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2. Peptides, 12(6), 1165-1173. https://doi.org/10.1016/0196-9781(91)90190-Z

Vancouver

Nothacker HP, Rinehart KL, McFarlane ID, Grimmelikhuijzen CJP. Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2. Peptides. 1991;12(6):1165-1173. https://doi.org/10.1016/0196-9781(91)90190-Z

Author

Nothacker, Hans Peter ; Rinehart, Kenneth L. ; McFarlane, Ian D. ; Grimmelikhuijzen, Cornelis J.P. / Isolation of two novel neuropeptides from sea anemones : The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2. In: Peptides. 1991 ; Vol. 12, No. 6. pp. 1165-1173.

Bibtex

@article{91bf0f8e523b4f39be477eb7c234beeb,
title = "Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2",
abstract = "Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Val-NH2, two novel peptides were purified from extracts of the sea anemone Anthopleura elegantissima. These peptides were L-3-phenyllactyl-Tyr-Arg-Ile-NH2 (name: Antho-RIamide I) and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2 (Antho-RIamide II). Immunocytochemical staining showed that these peptides were localized in neurons of sea anemones. Application of low concentrations (10-8 M) of Antho-RIamide I inhibited spontaneous contractions in several muscle groups of sea anemones, whereas Antho-RIamide II was inactive. Antho-RIamide I is the second neuropeptide from sea anemones that bears the unusual, amino-terminal L-3-phenyllactyl blocking group. We suggest that this group renders the peptide resistant against degradation by nonspecific aminopeptidases. In addition, the L-3-phenyllactyl residue might also play a role in receptor binding.",
keywords = "Coelenterate, Mass spectrometry, Neurohormone, Neuropeptide blocking group, Neurotransmitter, Peptide structure, Posttranslational modification",
author = "Nothacker, {Hans Peter} and Rinehart, {Kenneth L.} and McFarlane, {Ian D.} and Grimmelikhuijzen, {Cornelis J.P.}",
note = "Funding Information: We thank SusanneR aabe for typing the manuscripat nd the Bundesministeriufmor Forschung und Technologic and the Deutsche Forschungsgemeinschaft (Gr 76f2o/r7 fi-n3a) ncial support.",
year = "1991",
doi = "10.1016/0196-9781(91)90190-Z",
language = "English",
volume = "12",
pages = "1165--1173",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier",
number = "6",

}

RIS

TY - JOUR

T1 - Isolation of two novel neuropeptides from sea anemones

T2 - The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2

AU - Nothacker, Hans Peter

AU - Rinehart, Kenneth L.

AU - McFarlane, Ian D.

AU - Grimmelikhuijzen, Cornelis J.P.

N1 - Funding Information: We thank SusanneR aabe for typing the manuscripat nd the Bundesministeriufmor Forschung und Technologic and the Deutsche Forschungsgemeinschaft (Gr 76f2o/r7 fi-n3a) ncial support.

PY - 1991

Y1 - 1991

N2 - Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Val-NH2, two novel peptides were purified from extracts of the sea anemone Anthopleura elegantissima. These peptides were L-3-phenyllactyl-Tyr-Arg-Ile-NH2 (name: Antho-RIamide I) and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2 (Antho-RIamide II). Immunocytochemical staining showed that these peptides were localized in neurons of sea anemones. Application of low concentrations (10-8 M) of Antho-RIamide I inhibited spontaneous contractions in several muscle groups of sea anemones, whereas Antho-RIamide II was inactive. Antho-RIamide I is the second neuropeptide from sea anemones that bears the unusual, amino-terminal L-3-phenyllactyl blocking group. We suggest that this group renders the peptide resistant against degradation by nonspecific aminopeptidases. In addition, the L-3-phenyllactyl residue might also play a role in receptor binding.

AB - Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Val-NH2, two novel peptides were purified from extracts of the sea anemone Anthopleura elegantissima. These peptides were L-3-phenyllactyl-Tyr-Arg-Ile-NH2 (name: Antho-RIamide I) and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2 (Antho-RIamide II). Immunocytochemical staining showed that these peptides were localized in neurons of sea anemones. Application of low concentrations (10-8 M) of Antho-RIamide I inhibited spontaneous contractions in several muscle groups of sea anemones, whereas Antho-RIamide II was inactive. Antho-RIamide I is the second neuropeptide from sea anemones that bears the unusual, amino-terminal L-3-phenyllactyl blocking group. We suggest that this group renders the peptide resistant against degradation by nonspecific aminopeptidases. In addition, the L-3-phenyllactyl residue might also play a role in receptor binding.

KW - Coelenterate

KW - Mass spectrometry

KW - Neurohormone

KW - Neuropeptide blocking group

KW - Neurotransmitter

KW - Peptide structure

KW - Posttranslational modification

UR - http://www.scopus.com/inward/record.url?scp=0026342252&partnerID=8YFLogxK

U2 - 10.1016/0196-9781(91)90190-Z

DO - 10.1016/0196-9781(91)90190-Z

M3 - Journal article

C2 - 1821096

AN - SCOPUS:0026342252

VL - 12

SP - 1165

EP - 1173

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 6

ER -

ID: 370740262