title: PRQFVamide, a novel pentapeptide identified from the CNS and gut of Aplysia.
abstract: We have purified a novel pentapeptide from the Aplysia nervous system using bioassay on gut contractions. The structure of the peptide is Pro-Arg-Gln-Phe-Val-amide (PRQFVa). The precursor for PRQFVa was found to code for 33 copies of PRQFVamide and four related pentapeptides. Peaks corresponding to the predicted masses of all five pentapeptides were detected in Aplysia neurons by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Northern analysis revealed that expression of the precursor is abundant in the abdominal ganglion, much less in the pedal and cerebral ganglia, and rarely seen in the buccal and pleural ganglia. PRQFVa-positive neurons, mapped by immunohistochemistry and in situ hybridization, were present in all the central ganglia. PRQFVa immunopositive processes were observed in the gut, particularly in association with the vasculature. Some arteries and other highly vascularized tissues, such as the gill and the kidney, also contain numerous PRQFVa immunopositive processes. Application of synthetic PRQFVa suppresses not only contractions of the gut but also contractions of vasculature. PRQFVa is expressed in some of the neurons within the feeding circuitry and application of synthetic PRQFVa was found to decrease the excitability of some (B4/5 and B31/32) but not all (B8) neurons of the buccal feeding circuit. Our findings suggest that PRQFVa may act as a modulator within the feeding system as well as in other systems of Aplysia.
authors.affiliation: Graduate School of Science, Department of Biological Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Furukawa
authors.forename: K
authors.initials: K
authors.lastname: Nakamaru
authors.forename: K
authors.initials: K
authors.lastname: Sasaki
authors.forename: Y
authors.initials: Y
authors.lastname: Fujisawa
authors.forename: H
authors.initials: H
authors.lastname: Minakata
authors.forename: S
authors.initials: S
authors.lastname: Ohta
authors.forename: F
authors.initials: F
authors.lastname: Morishita
authors.forename: O
authors.initials: O
authors.lastname: Matsushima
authors.forename: L
authors.initials: L
authors.lastname: Li
authors.forename: V
authors.initials: V
authors.lastname: Alexeeva
authors.forename: T A
authors.initials: TA
authors.lastname: Ellis
authors.forename: N C
authors.initials: NC
authors.lastname: Dembrow
authors.forename: J
authors.initials: J
authors.lastname: Jing
authors.forename: J V
authors.initials: JV
authors.lastname: Sweedler
authors.forename: K R
authors.initials: KR
authors.lastname: Weiss
authors.forename: F S
authors.initials: FS
authors.lastname: Vilim
mesh_terms: D000577:Amides / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia; D001120:Arginine; D001808:Blood Vessels / Q000502:physiology; D015152:Blotting, Northern; D002490:Central Nervous System / Q000737:chemistry* / Q000502:physiology*; D003001:Cloning, Molecular; D004064:Digestive System / Q000737:chemistry*; D004068:Digestive System Physiological Phenomena; D004594:Electrophysiology; D005724:Ganglia / Q000737:chemistry / Q000502:physiology; D005998:Glycine; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D013058:Mass Spectrometry; D009119:Muscle Contraction / Q000502:physiology; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification* / Q000502:physiology*; D010649:Phenylalanine; D011392:Proline; D014633:Valine
chemical_list: D000577:Amides; D010455:Peptides; D010649:Phenylalanine; D001120:Arginine; D011392:Proline; D014633:Valine; D005998:Glycine