Glycine, glycine receptor subunit and glycine transporters in the rat parabrachial and Kölliker-Fuse nuclei.
In the present study, we investigated the expression and distribution of key molecules in the parabrachial (PB) and Kölliker-Fuse nuclei (KF) that determine glycinergic signal transduction. By means of immunocytochemistry, we analyzed the amino acid glycine (Gly), the glycine transporters 1 and 2 (GlyT1, GlyT2), and the ligand binding glycine receptor-subunit alpha 1 (GlyR alpha 1). Gly-immunoreactivity (-ir) was mainly found in varicose fibers and presumed terminal boutons; Gly-ir cell bodies were only occasionally seen. Immunoreactivity for GlyT2 was located in axons while GlyT1-staining was diffuse in the neuropil. Immunolabeling for GlyR alpha 1 occurred mostly as granular staining diffusely distributed throughout the neuropil. Only in the superior lateral PB, the lateral crescent of the PB, and caudally in the KF did GlyR alpha 1-ir outline cell bodies and primary and higher-order dendrites. Furthermore, our data demonstrate a distinct codistribution of immunoreactivities for Gly, GlyT2. and GlyR alpha 1 in a specific set of PB nuclei and in the KF. Strong staining was consistently seen in the internal lateral PB, the ventral lateral PB, the lateral crescent, the medial PB adjacent to the superior cerebellar peduncle, and the rostral two-thirds of the KF. Moderate to weak immunostaining was present in the superior, central, and dorsal lateral PB, the external medial PB, the medioventral part of the medial PB, and caudally in the KF. In contrast, remaining nuclei such as the external lateral PB and the waist area were essentially devoid of Gly-ir profiles, GlyT2-ir, and GlyR alpha 1-ir. Immunoreactivity for GlyT1 was evenly distributed throughout all nuclei of the medial and lateral PB, including the external lateral PB and the waist area, while the KF was only weakly stained. Our data provide evidence that glycinergic mechanisms might play a role for neural processing in most nuclei of the PB and in the KF. Only the external lateral PB and the waist area are apparently not subject to glycinergic inhibition.
Herbert
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Department of Animal Physiology, University of Tübingen, Germany. horst.herbert@uni-tuebingen.de
Guthmann
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Zafra
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Ottersen
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D026921:Amino Acid Transport Systems, Neutral; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D005998:Glycine / Q000378:metabolism*; D050487:Glycine Plasma Membrane Transport Proteins; D007124:Immunoenzyme Techniques; D008297:Male; D009474:Neurons / Q000378:metabolism; D011149:Pons / Q000166:cytology / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D018009:Receptors, Glycine / Q000378:metabolism*; D015398:Signal Transduction
D026921:Amino Acid Transport Systems, Neutral; D002352:Carrier Proteins; D050487:Glycine Plasma Membrane Transport Proteins; D018009:Receptors, Glycine; C493269:Slc6a5 protein, rat; C493266:Slc6a9 protein, rat; D005998:Glycine