title: Synaptic vesicle proteins and neuronal plasticity in adrenergic neurons.
abstract: The neurons in the superior cervical ganglion are active in plasticity and re-modelling in order to adapt to requirements. However, so far, only a few studies dealing with synaptic vesicle related proteins during adaptive processes have been published. In the present paper, changes in content and expression of the synaptic vesicle related proteins in the neurons after decentralization (cutting the cervical sympathetic trunk) or axotomy (cutting the internal and external carotid nerves) were studied. Immunofluorescence studies were carried out using antibodies and antisera against integral membrane proteins, vesicle associated proteins, NPY, and the enzymes TH and PNMT. For colocalization studies, the sections were simultaneously double labelled. Confocal laser scanning microscopy was used for colocalization studies as well as for semi-quantification analysis, using the computer software. Westen blot analysis, in situ 3'-end DNA labelling, and in situ hybridization were also employed. After decentralization of the ganglia several of the synaptic vesicle proteins (synaptotagmin I, synaptophysin, SNAP-25, CLC and GAP-43) were increased in the iris nerve terminal network, but with different time patterns, while TH-immunoreactivity had clearly decreased. In the ganglia, these proteins had decreased at 1 day after decentralization, probably due to degeneration of the pre-ganglionic nerve fibres and terminals. At later intervals, these proteins, except SNAP-25, had increased in the nerve fibre bundles and re-appeared in nerve fibres outlining the principal neurons.
authors.affiliation: Inst. of Anatomy and Cell Biology, Göteborg University, Sweden.
authors.forename: X E
authors.initials: XE
authors.lastname: Hou
authors.forename: A
authors.initials: A
authors.lastname: Dahlström
mesh_terms: D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000502:physiology*; D009473:Neuronal Plasticity / Q000502:physiology*; D009474:Neurons / Q000166:cytology / Q000502:physiology*; D010625:Phenylethanolamine N-Methyltransferase / Q000378:metabolism; D017783:Superior Cervical Ganglion / Q000502:physiology*; D013572:Synaptic Vesicles / Q000502:physiology*; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D014446:Tyrosine 3-Monooxygenase; D010625:Phenylethanolamine N-Methyltransferase