title: Vesicle-associated proteins and calcium in nerve terminals of chick ciliary ganglia during development of facilitation.
abstract: 1. The developmental appearance of synaptic vesicle-associated proteins and nerve terminal calcium ([Ca2+]i) sequestering processes were determined for the chick ciliary ganglia in relation to the maturation of the different phase of increased efficacy of transmitter release following nerve impulses. The maturation phases studied were from stages 34-35, at the time of synapse formation, to stage 46 at hatching. 2. Western blots and immunohistochemical localization indicated that synaptotagmin 1 and synapsin IIa were detectable at stages 34-35 and were clearly localized at the nerve terminals by stage 37. Syntaxin was clearly localized at the nerve terminals at stage 34. 3. The relative size of the postganglionic compound action potential, used to measure the transmission efficacy through the ganglion, showed that the slope of the relationship between log efficacy and log extracellular calcium concentration ([Ca2+]o) in low [Ca2+]o was about 4 by stage 46. 4. A mature facilitatory mechanism for transmission was not present at stage 34 and did not emerge until stage 38. A mature augmentation was not present at stages 34 or 38 and was not established until stages 41-42. Post-tetanic potentiation (PTP) was not present at stage 34; it was evident at stages 37-38 and only reached maturity by stages 41-42. 5. The time course of calcium changes in the nerve terminals following trains of impulses that give rise to facilitation, augmentation and PTP was determined for different stages of development using the indicator Calcium Green-1 in the nerve terminal. The mature time course of the phases of calcium decline in the nerve terminal associated with facilitation and augmentation was observed as early as stage 38, whereas that of the PTP phase did not mature until after stage 42. 6. These results are discussed in terms of the maturation of the vesicle-associated proteins and calcium influx into the terminal following trains of impulses that give rise to the different components of increased synaptic efficacy.
authors.affiliation: Department of Physiology University of Sydney, NSW, Australia.
authors.forename: Y Q
authors.initials: YQ
authors.lastname: Lin
authors.forename: K L
authors.initials: KL
authors.lastname: Brain
authors.forename: K A
authors.initials: KA
authors.lastname: Nichol
authors.forename: J J
authors.initials: JJ
authors.lastname: Morgan
authors.forename: M R
authors.initials: MR
authors.lastname: Bennett
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins; D002642:Chick Embryo; D005071:Evoked Potentials; D005726:Ganglia, Parasympathetic / Q000196:embryology / Q000502:physiology*; D008562:Membrane Glycoproteins / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D009419:Nerve Tissue Proteins / Q000502:physiology*; D050765:Qa-SNARE Proteins; D016704:Synapsins / Q000502:physiology*; D009435:Synaptic Transmission; D050863:Synaptotagmin I; D050857:Synaptotagmins
chemical_list: D002135:Calcium-Binding Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D016704:Synapsins; D050863:Synaptotagmin I; D050857:Synaptotagmins; D002118:Calcium