A short neuropeptide F (sNPF) precursor and a sNPF receptor (sNPFR) were characterized for the mosquito, Anopheles gambiae. The sNPFR was expressed in CHO-K1 cells, and it exhibited high affinity binding, IC(50) approximately 3-5 nM, for specific sNPFs. sNPF1 potently inhibited forskolin-stimulated cAMP production by transfected cells, suggesting sNPFR acts via G(i/o). Transcripts for sNPF and sNPFR were present in all body regions of larvae, pupae, and adults, and immunoblots for sNPFR confirmed this distribution in females. Membranes from female heads and thoraces exhibited prototypical high affinity binding for radiolabeled sNPF, indicating sNPFR is a bona fide endogenous receptor.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
A short neuropeptide F (sNPF) precursor and a sNPF receptor (sNPFR) were characterized for the mosquito, Anopheles gambiae. The sNPFR was expressed in CHO-K1 cells, and it exhibited high affinity binding, IC(50) approximately 3-5 nM, for specific sNPFs. sNPF1 potently inhibited forskolin-stimulated cAMP production by transfected cells, suggesting sNPFR acts via G(i/o). Transcripts for sNPF and sNPFR were present in all body regions of larvae, pupae, and adults, and immunoblots for sNPFR confirmed this distribution in females. Membranes from female heads and thoraces exhibited prototypical high affinity binding for radiolabeled sNPF, indicating sNPFR is a bona fide endogenous receptor.
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| skos:exactMatch | |
| uniprot:name |
Peptides
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| uniprot:author |
Brown M.R.,
Crim J.W.,
Garczynski S.F.
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| uniprot:date |
2007
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| uniprot:pages |
109-118
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| uniprot:title |
Characterization and expression of the short neuropeptide F receptor in the African malaria mosquito, Anopheles gambiae.
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| uniprot:volume |
28
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| dc-term:identifier |
doi:10.1016/j.peptides.2006.09.019
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