Evidence for a novel FMRFamide-related heptapeptide in the pulmonate snail Siphonaria pectinata

Price, David A.; Cobb, Charles G.; Doble, K. E.; Kline, John K.; Greenberg, Michael J.

doi:10.1016/0196-9781(87)90020-9

Cited by 25 publications

(5 citation statements)

References 7 publications

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“…1983;Price et al 1985Price et al , 1987Yang et al 1985;Schaeffer et al 1985;Grimmelikhuijzen & Graff, 1987;Holman, Cook & Nachman, 1986;Nachman et al 1986a, b;Ebberink et al 1987;Trimmer, Kobierski & Kravitz, 1987;Nambu et al 1988;Schneider & Taghert, 1988;Bulloch et al 1988;Li, 1990;Linacre et al 1990;Lutz et al 1990). It is clear that there is a family of FMRFamide-like peptides in Ascaris.…”

Section: Peptide Familiesmentioning

confidence: 92%

“…Besides the sequenced bioactive peptides AF1 and AF2, there are at least 3 other distinct peptides with different sequences in Ascaris; all 5 of these sequences are different from any other FMRFamidelike sequence obtained from other organisms, either directly from isolated peptides or indirectly from sequenced genes (Price & Greenberg, 1977;Dockray etal. 1983;Price et al 1985Price et al , 1987Yang et al 1985;Schaeffer et al 1985;Grimmelikhuijzen & Graff, 1987;Holman, Cook & Nachman, 1986;Nachman et al 1986a, b;Ebberink et al 1987;Trimmer, Kobierski & Kravitz, 1987;Nambu et al 1988;Schneider & Taghert, 1988;Bulloch et al 1988;Li, 1990;Linacre et al 1990;Lutz et al 1990). It is clear that there is a family of FMRFamide-like peptides in Ascaris.…”

Section: Peptide Familiesmentioning

confidence: 99%

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Neuropeptides in the nematodeAscaris suum

et al. 1991

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Most of the successful anti-nematode drugs currently available affect the nematode locomotory system. Their success is due to their interactions with molecules associated with the main neuro-transmitters of the motor nervous system, acetylcholine and GABA. These drugs tend to have a relatively broad spectrum of action, affecting a wide variety of nematodes, presumably because nematode motor nervous systems are conservative in their use of these transmitters.

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Section: Peptide Familiesmentioning

confidence: 92%

Section: Peptide Familiesmentioning

confidence: 99%

Neuropeptides in the nematodeAscaris suum

et al. 1991

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“…The details of the radioimmunoassay used to quantify the amount of FMRFamide (phenyl-alanylmethionyl-arginyl-phenylalaninylamide) in the methanol fraction of the bulbus arteriosus tissue extract are described in Price et al (1987). A 50l aliquot of the water and the methanol fractions of the tissue extract were assayed for FMRFamide.…”

Section: Radioimmunoassaymentioning

confidence: 99%

Bulbus arteriosus of the bivalve mollusc Mercenaria mercenaria: Morphology and pharmacology

Deaton

Felgenhauer

Duhon

2001

Journal of Morphology

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We examined the morphology and pharmacology of the bulbus arteriosus of the marine bivalve mollusc Mercenaria mercenaria. The bulbus arteriosus is an organ of unknown function associated with the posterior aorta and the ventricle. It is composed of connective tissue interspersed with muscle bundles. In contrast to the lumen of the ventricle, which has an extensive trabecular network, the lumen of the bulbus arteriosus has no trabeculae. No valve is present in the posterior aorta connecting the lumina of the ventricle and the bulbus arteriosus. Scattered neuronal profiles are present in the wall and the axonal processes contain vesicles that may contain neurosecretory products. We did not, however, find synapses or evidence of vesicular release into the lumen of the bulbus arteriosus. The bulbus arteriosus contains acetylcholine, 5-hydroxytryptamine (5HT), and the molluscan neuropeptides FMRFamide (phenyl-alanyl-methionyl-arginyl-phenylalaninylamide) and FLRFamide (phenylalanyl-leucinyl-arginyl-phenylalanylamide). The isolated bulbus arteriosus contracts tonically in response to mechanical stress and exposure to 5HT or FMRFamide, while acetylcholine relaxes it. We surmise that the bulbus arteriosus probably functions as a mechanism for regulating the relative amounts of hemolymph pumped into the anterior and posterior aortae by the ventricle and that the bulbus arteriosus may be a neurohemal site.

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“…RIAs were carried out as previously described (e.g., Price, 1982;Price et al, 1987Price et al, , 1990. Two antisera that had been raised in rabbits to thyroglobulin-peptide conjugates were used in these assays: antiserum S253 raised to YGGFMRFamide, and Q2 raised to pGluDPFLRFamide and AspDPFLRFamide.…”

Section: Radioimmunoassay (Ria)mentioning

confidence: 99%

The Sequences of Five Neuropeptides Isolated from Limulus using Antisera to FMRFamide

Gaus

Doble

Price

et al. 1993

The Biological Bulletin

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Five neuropeptides were isolated from CNS extracts of the horseshoe crab Limulus polyphemus by high pressure liquid chromatography (HPLC). The peptides were identified by radioimmunoassays (RIAs) based on two antisera raised to FMRFamide-related peptides (FaRPs). The purified peptides were analyzed by automated sequencing and mass spectrometry, and the following sequences were obtained: DEGHKMLYFamide, GHSLLHFamide, PDHHMMYFamide, DHGNMLYFamide, and GGRSPSLRLRFamide. The first four peptides are members of a novel family with virtually no relationship to FMRFamide. GGRSPSLRLRFamide, on the basis of structural similarity, becomes the second member of a class of FaRPs known previously only from a peptide isolated from mosquito heads. At least one member of the novel family (GHSLLHFamide) inhibits the isolated heart of Limulus.

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Evidence for a novel FMRFamide-related heptapeptide in the pulmonate snail Siphonaria pectinata

Cited by 25 publications

References 7 publications

Neuropeptides in the nematodeAscaris suum

Neuropeptides in the nematodeAscaris suum

Bulbus arteriosus of the bivalve mollusc Mercenaria mercenaria: Morphology and pharmacology

The Sequences of Five Neuropeptides Isolated from Limulus using Antisera to FMRFamide

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