title: Vesicular glutamate transporter 2 is expressed in different nerve fibre populations that selectively contact pulmonary neuroepithelial bodies.
abstract: Pulmonary neuroepithelial body (NEB) receptors in rats receive at least four different nerve fibre populations. In addition to a spinal sensory innervation that contacts NEBs at their basal side, extensive vagal nodose sensory terminals and separate nitrergic and cholinergic nerve endings protrude between NEB cells. In the present study, antibodies against the vesicular glutamate transporter 2 (VGLUT2), a transmembrane protein responsible for loading glutamate into synaptic vesicles, were used to investigate whether some of the nerve terminals contacting NEBs in rat lungs might use glutamate as a neurotransmitter. VGLUT2 immunoreactivity (IR) was detected in extensive intraepithelial arborising nerve terminals that appeared to contact most of the NEBs. Multiple immunostaining showed VGLUT2 IR in the vagal nodose and spinal sensory nerve terminals contacting NEBs, and in another, most likely sensory, intraepithelial nerve fibre population, the origin and further characteristics of which remain to be elucidated. At least part of the VGLUT2-immunoreactive nerve fibres that contact NEBs were shown to be myelinated. The expression of VGLUT2 indicates that glutamate is stored and released as a neurotransmitter in terminals of several pulmonary (sensory) nerve fibre populations that selectively relate to the complex NEB receptors. The present study strongly suggests an involvement of glutamatergic mechanisms in the peripheral transduction of sensory stimuli from the lungs, via the release of glutamate from nerve terminals, thereby modulating the activity of NEB receptor cells or the excitability of afferent nerves.
authors.affiliation: Laboratory of Cell Biology and Histology, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.
authors.forename: Inge
authors.initials: I
authors.lastname: Brouns
authors.forename: Isabel
authors.initials: I
authors.lastname: Pintelon
authors.forename: Jeroen
authors.initials: J
authors.lastname: Van Genechten
authors.forename: Ian
authors.initials: I
authors.lastname: De Proost
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Timmermans
authors.forename: Dirk
authors.initials: D
authors.lastname: Adriaensen
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D004847:Epithelial Cells / Q000166:cytology* / Q000502:physiology; D018698:Glutamic Acid / Q000378:metabolism / Q000502:physiology; D006651:Histocytochemistry; D008168:Lung / Q000166:cytology* / Q000294:innervation* / Q000502:physiology; D026901:Membrane Transport Proteins; D009412:Nerve Fibers / Q000737:chemistry / Q000378:metabolism*; D009490:Neurosecretory Systems / Q000166:cytology* / Q000502:physiology; D009620:Nodose Ganglion / Q000166:cytology / Q000502:physiology; D017729:Presynaptic Terminals / Q000378:metabolism / Q000648:ultrastructure; D051381:Rats; D017208:Rats, Wistar; D014630:Vagus Nerve / Q000166:cytology / Q000502:physiology; D050599:Vesicular Glutamate Transport Protein 2; D033921:Vesicular Transport Proteins
chemical_list: D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C493475:Slc17a6 protein, rat; D050599:Vesicular Glutamate Transport Protein 2; D033921:Vesicular Transport Proteins; D018698:Glutamic Acid