title: Immunocytochemical localization of the glutamate transporter GLT-1 in goldfish (Carassius auratus) retina.
abstract: Glutamate is the major excitatory neurotransmitter in the retina of vertebrates. Electrophysiological experiments in goldfish and salamander have shown that neuronal glutamate transporters play an important role in the clearance of glutamate from cone synaptic clefts. In this study, the localization of the glutamate transporter GLT-1 has been investigated immunocytochemically at the light and electron microscopical levels in the goldfish retina using a GLT-1-specific antibody. GLT immunoreactivity (IR) was observed at the light microscopical level in Müller cells, bipolar cells, the outer plexiform layer (OPL), and the inner plexiform layer (IPL). At the electron microscopical level, membrane-bound and cytoplasmic GLT-IR in the OPL was located in finger-like protrusions of the cone terminal located near the invaginating postsynaptic processes of bipolar and horizontal cells. GLT-IR was not observed in the vicinity of synaptic ribbons. This location of GLT-1 allows modulation of the glutamate concentration in the synaptic cleft, thereby shaping the dynamics of synaptic transmission between cones and second-order neurons. In the inner IPL, GLT-IR was observed in the cytoplasm and was membrane bound in mixed rod/cone bipolar cell terminals and cone bipolar cell terminals. The membrane-bound GLT-1 was generally observed at some distance from the synaptic ribbon. The morphology of the bipolar cell terminal together with the localization of GLT-1 suggests that at least these glutamate transporters are not primarily involved in rapid uptake of glutamate release by the bipolar cells. The GLT-IR in the cytoplasm of Müller cells was located throughout the entire goldfish retina from the outer limiting membrane to the inner limiting membrane. The location of GLT-1 in Müller cells is consistent with the role of Müller cells in converting glutamate to glutamine.
authors.affiliation: Research Unit, Retinal Signal Processing, The Netherlands Ophthalmic Research Institute, Amsterdam.
authors.forename: C A
authors.initials: CA
authors.lastname: Vandenbranden
authors.forename: S
authors.initials: S
authors.lastname: Yazulla
authors.forename: K M
authors.initials: KM
authors.lastname: Studholme
authors.forename: W
authors.initials: W
authors.lastname: Kamphuis
authors.forename: M
authors.initials: M
authors.lastname: Kamermans
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D000595:Amino Acid Sequence; D027322:Amino Acid Transport System X-AG; D000818:Animals; D000918:Antibody Specificity; D006054:Goldfish / Q000502:physiology*; D007150:Immunohistochemistry; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D017949:Retinal Cone Photoreceptor Cells / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D018528:ATP-Binding Cassette Transporters; D027322:Amino Acid Transport System X-AG