Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae.

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Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae. / Schöller, Susanne; Belmont, Martin; Cazzamali, Giuseppe; Hauser, Frank; Williamson, Michael; Grimmelikhuijzen, Cornelis J P.

In: Biochemical and Biophysical Research Communications, Vol. 327, No. 1, 2005, p. 29-34.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Schöller, S, Belmont, M, Cazzamali, G, Hauser, F, Williamson, M & Grimmelikhuijzen, CJP 2005, 'Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae.', Biochemical and Biophysical Research Communications, vol. 327, no. 1, pp. 29-34. https://doi.org/10.1016/j.bbrc.2004.11.139

APA

Schöller, S., Belmont, M., Cazzamali, G., Hauser, F., Williamson, M., & Grimmelikhuijzen, C. J. P. (2005). Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae. Biochemical and Biophysical Research Communications, 327(1), 29-34. https://doi.org/10.1016/j.bbrc.2004.11.139

Vancouver

Schöller S, Belmont M, Cazzamali G, Hauser F, Williamson M, Grimmelikhuijzen CJP. Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae. Biochemical and Biophysical Research Communications. 2005;327(1):29-34. https://doi.org/10.1016/j.bbrc.2004.11.139

Author

Schöller, Susanne ; Belmont, Martin ; Cazzamali, Giuseppe ; Hauser, Frank ; Williamson, Michael ; Grimmelikhuijzen, Cornelis J P. / Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae. In: Biochemical and Biophysical Research Communications. 2005 ; Vol. 327, No. 1. pp. 29-34.

Bibtex

@article{df3f9cc0ec2711dcbee902004c4f4f50,
title = "Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae.",
abstract = "The insect myosuppressins (X1DVX2HX3FLRFamide) are neuropeptides that generally block insect muscle activities. We have used the genomic sequence information from the malaria mosquito Anopheles gambiae Genome Project to clone a G protein-coupled receptor that was closely related to the two previously cloned and characterized myosuppressin receptors from Drosophila [Proc. Natl. Acad. Sci. USA 100 (2003) 9808]. The mosquito receptor cDNA was expressed in Chinese hamster ovary cells and was found to be activated by low concentrations of Anopheles myosuppressin (TDVDHVFLRFamide; EC50, 1.6 x 10(-8)M). The receptor was not activated by a library of 35 other insect neuropeptides and monoamines, including neuropeptides that resembled myosuppressin in their C-terminal moiety, such as PDRNFLRFamide (Anopheles FMRFamide-3), other Anopheles FMRFamide peptides, or neuropeptide F-like peptides, showing that the receptor was quite selective for myosuppressin. These results also showed that the myosuppressin receptor needs a much larger portion than the C-terminal FLRFamide sequence for its activation. The insect myosuppressins are often grouped together with the insect FMRFamides under the name FaRPs (FMRFamide-related peptides). However, this is not justified anymore, because the insect myosuppressin receptor/ligand couple is both functionally and evolutionarily fully unrelated to the insect FMRFamide receptor/ligand couple. To our knowledge, this is the first report on the molecular identification of a mosquito neuropeptide receptor.",
author = "Susanne Sch{\"o}ller and Martin Belmont and Giuseppe Cazzamali and Frank Hauser and Michael Williamson and Grimmelikhuijzen, {Cornelis J P}",
note = "Keywords: Amino Acid Sequence; Animals; Anopheles gambiae; Base Sequence; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Exons; Introns; Molecular Sequence Data; Receptors, Neuropeptide; Sequence Alignment",
year = "2005",
doi = "10.1016/j.bbrc.2004.11.139",
language = "English",
volume = "327",
pages = "29--34",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Molecular identification of a myosuppressin receptor from the malaria mosquito Anopheles gambiae.

AU - Schöller, Susanne

AU - Belmont, Martin

AU - Cazzamali, Giuseppe

AU - Hauser, Frank

AU - Williamson, Michael

AU - Grimmelikhuijzen, Cornelis J P

N1 - Keywords: Amino Acid Sequence; Animals; Anopheles gambiae; Base Sequence; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Exons; Introns; Molecular Sequence Data; Receptors, Neuropeptide; Sequence Alignment

PY - 2005

Y1 - 2005

N2 - The insect myosuppressins (X1DVX2HX3FLRFamide) are neuropeptides that generally block insect muscle activities. We have used the genomic sequence information from the malaria mosquito Anopheles gambiae Genome Project to clone a G protein-coupled receptor that was closely related to the two previously cloned and characterized myosuppressin receptors from Drosophila [Proc. Natl. Acad. Sci. USA 100 (2003) 9808]. The mosquito receptor cDNA was expressed in Chinese hamster ovary cells and was found to be activated by low concentrations of Anopheles myosuppressin (TDVDHVFLRFamide; EC50, 1.6 x 10(-8)M). The receptor was not activated by a library of 35 other insect neuropeptides and monoamines, including neuropeptides that resembled myosuppressin in their C-terminal moiety, such as PDRNFLRFamide (Anopheles FMRFamide-3), other Anopheles FMRFamide peptides, or neuropeptide F-like peptides, showing that the receptor was quite selective for myosuppressin. These results also showed that the myosuppressin receptor needs a much larger portion than the C-terminal FLRFamide sequence for its activation. The insect myosuppressins are often grouped together with the insect FMRFamides under the name FaRPs (FMRFamide-related peptides). However, this is not justified anymore, because the insect myosuppressin receptor/ligand couple is both functionally and evolutionarily fully unrelated to the insect FMRFamide receptor/ligand couple. To our knowledge, this is the first report on the molecular identification of a mosquito neuropeptide receptor.

AB - The insect myosuppressins (X1DVX2HX3FLRFamide) are neuropeptides that generally block insect muscle activities. We have used the genomic sequence information from the malaria mosquito Anopheles gambiae Genome Project to clone a G protein-coupled receptor that was closely related to the two previously cloned and characterized myosuppressin receptors from Drosophila [Proc. Natl. Acad. Sci. USA 100 (2003) 9808]. The mosquito receptor cDNA was expressed in Chinese hamster ovary cells and was found to be activated by low concentrations of Anopheles myosuppressin (TDVDHVFLRFamide; EC50, 1.6 x 10(-8)M). The receptor was not activated by a library of 35 other insect neuropeptides and monoamines, including neuropeptides that resembled myosuppressin in their C-terminal moiety, such as PDRNFLRFamide (Anopheles FMRFamide-3), other Anopheles FMRFamide peptides, or neuropeptide F-like peptides, showing that the receptor was quite selective for myosuppressin. These results also showed that the myosuppressin receptor needs a much larger portion than the C-terminal FLRFamide sequence for its activation. The insect myosuppressins are often grouped together with the insect FMRFamides under the name FaRPs (FMRFamide-related peptides). However, this is not justified anymore, because the insect myosuppressin receptor/ligand couple is both functionally and evolutionarily fully unrelated to the insect FMRFamide receptor/ligand couple. To our knowledge, this is the first report on the molecular identification of a mosquito neuropeptide receptor.

U2 - 10.1016/j.bbrc.2004.11.139

DO - 10.1016/j.bbrc.2004.11.139

M3 - Journal article

C2 - 15629425

VL - 327

SP - 29

EP - 34

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

ID: 3045835