Synaptic proteins in rat taste bud cells: appearance in the Golgi apparatus and relationship to alpha-gustducin and the Lewis(b) and A antigens.
Taste receptor cells are continuously replaced during the life of the animal, but many of their sensory axons respond primarily to stimuli belonging to a single taste quality. This suggests that a newly arising taste cell must form a synapse with an appropriate sensory axon, requiring cell recognition that is likely to be mediated by surface markers. As an approach to studying this process, we attempted to locate synapses by immunolabeling taste buds of rats for proteins involved in neurotransmitter release. In taste bud cells of vallate papillae and nasoincisor ducts, double-labeling experiments showed that syntaxin-1, SNAP-25, synaptobrevin, and synaptophysin colocalized with the Golgi marker beta COP in elongated cytoplasmic compartments that extended from the perinuclear region into apical and basal processes of the cells. Labeled cells were spindle-shaped, identifying them as light cells. Syntaxin-1 appeared only in taste cells, but SNAP-25, synaptobrevin, and synaptophysin were also seen in nerve fibers. The synaptic vesicle glycoprotein SV2 appeared only in nerve fibers. Taste cells of fungiform papillae did not show immunoreactivity for presynaptic proteins or Golgi markers, but axonal labeling was similar to that in other regions. Taste cells with alpha-gustducin could express either presynaptic proteins or the carbohydrate blood group antigen Lewis(b), but not both. Therefore, Lewis(b) and presynaptic proteins are not expressed during the same period in the life of a taste bud cell. Most taste cells expressing syntaxin-1 (82%) also expressed the A blood group antigen, whether or not they expressed alpha-gustducin.
Pumplin
D W
DW
Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, Maryland 21201-1509, USA. dpumplin@umaryland.edu
Getschman
E
E
D000818:Animals; D000954:Antigens, Surface / Q000378:metabolism; D002450:Cell Communication / Q000502:physiology; D002451:Cell Compartmentation / Q000502:physiology; D020756:Coatomer Protein / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D007983:Lewis Blood Group Antigens / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D050683:R-SNARE Proteins; D051381:Rats; D015398:Signal Transduction / Q000502:physiology*; D013569:Synapses / Q000378:metabolism* / Q000648:ultrastructure; D016708:Synaptophysin / Q000378:metabolism; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; D013650:Taste Buds / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure; D015293:Transducin / Q000378:metabolism*
D000954:Antigens, Surface; D020756:Coatomer Protein; D007983:Lewis Blood Group Antigens; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; C494210:Snap25 protein, rat; C494213:Stx1a protein, rat; C489618:Sv2a protein, rat; D016708:Synaptophysin; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; C075192:gustducin; D015293:Transducin