title: Ultracytochemical distribution of ouabain-sensitive, K+-dependent, p-nitrophenylphosphatase in the synaptic layers of goldfish retina.
abstract: Ouabain-sensitive, K+-dependent p-nitrophenylphosphatase (K+-pNPPase) activity, which represents the second dephosphorylation step of Na+,K+-ATPase, was localized histochemically at the light and electron microscopical levels in the goldfish retina. K+-pNPPase staining was most intense in the outer and inner plexiform layers and less intense over the photoreceptor inner segments. K+-pNPPase staining was observed on the membranes of horizontal cell dendrites and presynaptic membrane of all cone pedicles but only rarely over rod spherules. Bipolar cell dendrites in the outer plexiform layer were not stained for K+-pNPPase. In the inner plexiform layer (IPL), K+-pNPPase staining was observed at 90% of the bipolar cell ribbon synapses but only at 40% of amacrine cell synapses. The proportion of K+-pNPPase staining at amacrine cell synapses increased from 26 to 49% as one progressed from the outer to inner layers of the IPL, while staining at bipolar cell synapses showed no such trend. Only 16% of the amacrine synapses onto mixed, rod-cone (mb) bipolar cell synaptic terminals were positive for K+-pNPPase. We suggest that the differential distribution of K+-pNPPase staining at retinal synapses can be explained, in part, by the ionic conductances gated at the postsynaptic sites. In addition, the presence of K+-pNPPase on lateral horizontal cell dendrites in cone pedicles is consistent with the hypothesis that the sodium pump is involved in the release of GABA at feedback synapses from horizontal cells to cone photoreceptors.
mesh_terms: D009597:4-Nitrophenylphosphatase / Q000032:analysis* / Q000378:metabolism; D000818:Animals; D003530:Cyprinidae / Q000378:metabolism*; D006054:Goldfish / Q000378:metabolism*; D006651:Histocytochemistry; D008854:Microscopy, Electron; D010042:Ouabain / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D011188:Potassium / Q000502:physiology; D012160:Retina / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D013569:Synapses / Q000201:enzymology* / Q000648:ultrastructure
chemical_list: D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium