title: Immunocytochemical localization of FLRFamide-, proctolin-, and CCAP-like peptides in the stomatogastric nervous system and neurohemal structures of the crayfish, Cherax destructor.
abstract: To compare the stomatogastric nervous system of the crayfish Cherax destructor with those of other decapod species, the distribution of FLRF (Phe-Leu-Arg-Phe) amide-, proctolin- and crustacean cardioactive peptide (CCAP)-like immunoreactivities was studied in the stomatogastric nervous system and in neurosecretory structures by using wholemount immunocytochemical techniques and confocal microscopy. In addition, the number of cells in the stomatogastric ganglion (19-24) and axon profiles in the stomatogastric nerve (157-165) were counted. FLRFamide-like immunoreactivity was present within numerous cell bodies and neuropil of the commissural ganglia, in the neuropil of the stomatogastric ganglion, and in one cell body of the esophageal ganglion. FLRFamide-like immunoreactivity was also found in two cell bodies at the junction of the stomatogastric nerve with the superior esophageal nerve and in two cell bodies in the inferior ventricular nerve. Proctolin-like immunoreactivity was present in numerous cell bodies and neuropil of the paired commissural ganglia and in the neuropil of the stomatogastric ganglion. CCAP-like immunoreactivity was found in the neuropil and in one to four cell bodies in the commissural ganglia. Both proctolin- and CCAP-immunoreactive varicosities occurred on the surface of the circumesophageal connectives and on the postesophageal commissure, indicating a neurohemal source within the stomatogastric nervous system, which was verified by electron microscopy. The pericardial organs showed FLRFamide-, proctolin-, and CCAP-like immunoreactivity. This staining pattern suggests that FLRFamide-like and proctolin-like peptides are used as neurohormones and as neuromodulators in the stomatogastric nervous system of the crayfish C. destructor, whereas CCAP-like peptides may only affect the stomatogastric ganglion as a neurohormone.
authors.affiliation: Institut für Neurobiologie, Freie Universität Berlin, D-14195 Berlin, Germany. skiebe@zedat-fu-berlin.de
authors.forename: P
authors.initials: P
authors.lastname: Skiebe
authors.forename: C
authors.initials: C
authors.lastname: Dietel
authors.forename: M
authors.initials: M
authors.lastname: Schmidt
mesh_terms: D000818:Animals; D003400:Astacoidea / Q000033:anatomy & histology*; D001369:Axons / Q000737:chemistry / Q000648:ultrastructure; D001710:Biotin / Q000031:analogs & derivatives; D001923:Brain Chemistry / Q000502:physiology*; D002116:Calcitonin / Q000032:analysis*; D005260:Female; D005456:Fluorescent Dyes; D017952:Ganglia, Invertebrate / Q000737:chemistry* / Q000648:ultrastructure; D007150:Immunohistochemistry; D007546:Isoquinolines; D008297:Male; D008854:Microscopy, Electron; D009474:Neurons / Q000737:chemistry* / Q000648:ultrastructure; D009479:Neuropeptides; D009842:Oligopeptides / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*
chemical_list: D005456:Fluorescent Dyes; D007546:Isoquinolines; D009479:Neuropeptides; D009842:Oligopeptides; D010446:Peptide Fragments; C070614:neurobiotin; C011536:proctolin; D001710:Biotin; C066148:phenylalanyl-leucyl-arginyl phenylalaninamide; C037553:katacalcin; D002116:Calcitonin; C017475:lucifer yellow