title: Localisation of sulfakinin neuronal pathways in the blowfly Calliphora vomitoria.
abstract: The distribution of neurones immunoreactive to antisera raised against the undecapeptide C-terminal fragment of drosulfakinin II (DrmSKII), Asp-Gln-Phe-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2, has been studied in the blowfly Calliphora vomitoria. Antisera were preabsorbed with combinations of the parent antigen, the tetrapeptide Phe-Met-Arg-Phe-NH2 and cholecystokinin, the vertebrate sulfated octapeptide (CCK-8), Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2, in order to ensure specificity for the sulfakinin peptides of C. vomitoria (the nonapeptide callisulfakinin I is identical to drosulfakinin I and callisulfakinin II differs from DrmSK II only by the presence of -Glu3-Glu4- in place of -Asp3-Asp4-). Only four pairs of sulfakinin-immunoreactive neurons have been visualised in the entire nervous system. These occur in the brain: two pairs of cells situated medially in the caudo-dorsal region close to the roots of the ocellar nerve and two other pairs at the same level but positioned more laterally. Despite the small number of sulfakinin-immunoreactive cells, there are extensive projections to many areas of neuropile in the brain and the thoracic ganglion. The pathway of the medial sulfakinin cells extends into each of the three thoracic ganglia and a metameric arrangement of sulfakinin neuronal projections is also seen in the abdominal ganglia. Neither the dorsal neural sheath of the thoracic ganglion, nor the abdominal nerves contain sulfakinin-immunoreactive material. These observations suggest that the sulfakinins of the blowfly function as neurotransmitters or neuromodulators. They do not appear to have a direct role in gut physiology, as has been shown by in vitro bioassays for the sulfakinins of orthopterans and blattodeans. In addition to the neurones that display specific sulfakinin immunoreactivity, other cells within the brain and thoracic ganglion are immunoreactive to cholecystokinin/gastrin antisera. There are, therefore, at least two types of dipteran neuropeptides with amino acid sequences that are similar to the vertebrate molecules cholecystokinin and gastrin.
authors.affiliation: School of Biological Sciences, Queen Mary and Westfield College, University of London, UK.
authors.forename: H
authors.initials: H
authors.lastname: Duve
authors.forename: J F
authors.initials: JF
authors.lastname: Rehfeld
authors.forename: P
authors.initials: P
authors.lastname: East
authors.forename: A
authors.initials: A
authors.lastname: Thorpe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002490:Central Nervous System / Q000737:chemistry / Q000648:ultrastructure; D004175:Diptera / Q000033:anatomy & histology* / Q000378:metabolism; D019835:FMRFamide; D005725:Ganglia, Autonomic / Q000737:chemistry / Q000166:cytology; D007124:Immunoenzyme Techniques; D036341:Intercellular Signaling Peptides and Proteins; D007395:Interneurons / Q000737:chemistry / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009434:Neural Pathways / Q000737:chemistry / Q000648:ultrastructure*; D009474:Neurons / Q000737:chemistry*; D009479:Neuropeptides / Q000032:analysis; D010455:Peptides / Q000032:analysis*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
chemical_list: D036341:Intercellular Signaling Peptides and Proteins; D009479:Neuropeptides; D010455:Peptides; C056938:drosulfakinin II; D019835:FMRFamide