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J Storm-Mathisen

Publications and source records attributed to J Storm-Mathisen.

At least 55 records · Page 3Linked to original sources
PubMed1995

Differential expression of two glial glutamate transporters in the rat brain: quantitative and immunocytochemical observations.

Glutamate, the major excitatory neurotransmitter in brain, is almost exclusively intracellular due to the action of the glutamate transporters in the plasma membranes. To study the localization and properties of these proteins, we have raised antibodies specifically recognizing parts of the sequences of two cloned rat glutamate transporters, GLT-1 (Pines et al., 1992) and GLAST (Storck et al., 1992). On immunoblots the antibodies against GLT-1 label a broad heterogeneous band with maximum density at around 73 kDa, while the antibody against GLAST labels a similarly broad band at around 66 kDa in the cerebellum and a few kilodaltons lower in other brain regions. GLT-1 is expressed at the highest concentrations in the hippocampus, lateral septum, cerebral cortex, and striatum, while GLAST is preferentially expressed in the molecular layer of the cerebellum. However, both transporters are present throughout the brain, and have roughly parallel distributions in the cerebral hemispheres and brainstem. Preembedding light and electron microscopical immunocytochemistry shows that both GLT-1 and GLAST are restricted to astrocytes, which appear to express both proteins concomitantly, but in different proportions in different parts of the brain. Nerve terminal labeling was not observed. Both the amino and carboxyl terminals of GLT-1 and GLAST are located intracellularly, indicating an even number of transmembrane segments. Antibodies against a synthetic peptide corresponding to amino acid residues 2-11 of the proposed sequence of GLT-1 recognize the native rat brain GLT-1 protein, confirming that the translation initiation site is at the first ATG.

ATP-Binding Cassette Transporters↗
PubMed1994

Differential subcellular distribution of glutamate and taurine in primary olfactory neurones.

Taurine and glutamate are widely distributed amino acids in the mammalian brain, including the olfactory bulb where their functions have not been fully elucidated. This study investigated the precise cellular distribution of taurine and glutamate in the nerve layer and the glomeruli of the olfactory bulb, using semiquantitative immunocytochemistry at the electron microscopic level. The results show that both amino acids are present at higher concentrations in primary olfactory neurones than in the postsynaptic dendrites. Glutamate is also enriched in terminals vs axons of the primary olfactory neurones. This suggests that glutamate acts as a neurotransmitter at the primary synapse in the olfactory system. An opposite concentration gradient is found for taurine, with a higher level of taurine-like immunoreactivity in axons than in terminals of primary olfactory neurones. Further studies are required before conclusions can be drawn about the function of taurine in these neurones.

Animals↗
PubMed1994

Extrasynaptic localization of taurine-like immunoreactivity in the lamprey spinal cord.

Taurine is an endogenous amino acid that can occur in nerve terminals in the central nervous system and that can produce inhibitory neuronal responses. It is unclear, however, whether this amino acid can function as a synaptic transmitter. To examine the distribution of taurine at high anatomical resolution in a vertebrate, light and electron microscopic immunocytochemical postembedding techniques were applied to the lamprey spinal cord (Ichtyomyzon unicuspis and Lampetra fluviatilis), which contains many large, unmyelinated axons. The most intense immunolabeling occurred in a population of liquor-contacting cells (tanycytes), located around the central canal, which extended processes to the dorsal, lateral, and ventral margins of the spinal cord. In addition, a proportion of the taurine-immunoreactive cells contained gamma-aminobutyric acid (GABA)-like immunoreactivity. A moderate level of taurine immunoreactivity was also present in ependymal cells, located around the central canal, as well as in astrocytes throughout all regions of the spinal cord. At the ultrastructural level, the taurine immunoreactivity showed an even distribution in the cytoplasm of the labeled cells. In contrast to the glial labeling, neuronal cell bodies and axons exhibited very low levels of taurine labeling, which were similar to the level of background labeling. The synaptic vesicle clusters within the axons did not show any clear accumulation of taurine immunoreactivity. These results suggest that taurine may have metabolic roles in the lamprey spinal cord, and, as in other systems, it may take part in osmoregulation. However, the lack of immunolabeling in presynaptic elements is not consistent with a role of taurine as a synaptic transmitter.

Animals↗
PubMed1994

Differential expression of two glial glutamate transporters in the rat brain: an in situ hybridization study.

The distributions of the mRNAs encoding the L-glutamate transporters GLT1 and GLAST were examined in the rat brain by in situ hybridization using 35S-labelled oligonucleotide probes. Probes directed to GLT1 produced dense labelling in the hippocampus, neocortex and neostriatum, and weak labelling in the cerebellum. In contrast, GLAST mRNA appeared to be greatly enriched in the cerebellum compared to other brain regions. While the intensity of the labelling for GLAST and GLT1 varied among different regions, their cellular distributions appeared to coincide inasmuch as both mRNAs were mainly expressed by glial cells. Labelling occurred, inter alia, in glial cells throughout the hippocampus, and in Golgi epithelial cells in the Purkinje cell layer of the cerebellum.

Amino Acid Transport System X-AG↗
PubMed1994

Immunohistochemical evidence for coexistence of glycine and GABA in nerve terminals on cat spinal motoneurones: an ultrastructural study.

Previous electrophysiological and pharmacological studies have suggested the involvement of both glycine and gamma-aminobutyric acid (GABA) as transmitters in the reflex pathway mediating recurrent inhibition of cat spinal motoneurones. By use of the postembedding immunogold technique and antibodies against glutaraldehyde-conjugated amino acids it is shown that glycine- and GABA-immunoreactive nerve terminals occur in contact with cell bodies of alpha motoneurone size, as well as in the surrounding neuropil in the motor nuclei of the cat spinal cord. A substantial proportion of these terminals harbours both glycine- and GABA-LI. The enrichment of immunolabelling over synaptic vesicles in such terminals strongly suggests that both of these amino acids are used as transmitter substances.

Animals↗
PubMed1994

Colocalization of glutamate and glycine in bipolar cell terminals of the human retina.

Human retinae from surgical specimens rapidly fixed in a glutaraldehyde/formaldehyde mixture were subjected to postembedding, immunogold immunocytochemistry of glutamate and glycine, and subsequently analysed in an electron microscope. The two amino acids were visualised in the same tissue sections by the use of two different gold particle sizes. All bipolar cell perikarya and terminals showed significant glutamate labelling with mean gold particle densities 3-4 times higher than those of the retinal, non-neural pigment epithelial and Müller cells. Bipolar cell terminals displayed significantly higher glutamate labelling density than the bipolar cell bodies, as would be expected of glutamatergic neurons. A subpopulation of the glutamate-immunolabelled bipolar cell bodies (18%) and terminals (32%) also exhibited strong glycine labelling (7-8 times that of pigment epithelial and Müller cells). These glutamate-glycine positive terminals established contacts with amacrine cell processes and ganglion cell dendrites and were localised almost exclusively at between 44% and 88% depth of the inner plexiform layer, indicating that they belong to the "ON" cone bipolar system. This subpopulation of terminals was endowed with significantly higher glycine labelling density than the glycine positive bipolar cell bodies. These results show that human bipolar cell terminals colocalise glutamate and glycine and provide the first direct demonstration of an enrichment of these two amino acids in the same presynaptic element.

Antibody Specificity↗
PubMed1994

Colocalization of gamma-aminobutyrate and gastrin in the rat antrum: an immunocytochemical and in situ hybridization study.

BACKGROUND/AIMS: The inhibitory neurotransmitter gamma-aminobutyrate (GABA) has been shown to coexist with insulin in pancreatic beta-cells. We have presently investigated whether GABA also colocalizes with gastrin in G cells in rat antral mucosa. METHODS: Three alternative approaches were used: (1) gastrin in situ hybridization and GABA immunocytochemistry on consecutive cryostat sections; (2) GABA immunocytochemistry and gastrin immunocytochemistry on adjacent semithin and ultrathin sections; and (3) double-immunogold labeling of GABA and gastrin in the same ultrathin section. RESULTS: Colocalization of GABA and gastrin was observed with each of the three approaches. In the double-immunogold labeled cells, the G-cell granules displayed a high gold-particle density indicating gastrin and a low particle density indicating GABA, whereas the converse was true for the extragranular cytoplasmic matrix. The gold-particle ratios between these compartments were 11 (for gastrin) and 0.36 (for GABA), respectively. GABA labeling was also observed in two other antral endocrine cell types, classified by morphological criteria as somatostatin producing D cells and serotonin producing ECn cells. CONCLUSIONS: This is the first direct demonstration of GABA in gastrointestinal G cells. Our findings suggest that GABA may have a paracrine function in the stomach mucosa, analogous to its presumed role in the pancreatic islets.

Animals↗
PubMed1994

Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex.

Glutamate dehydrogenase is one of the main enzymes involved in the formation and metabolism of the neurotransmitter glutamate. In the present study we investigated the enzyme ultrastructurally in the cerebellar cortex, a region rich in well defined glutamatergic neurons, by pre-embedding immunocytochemical staining (peroxidase-antiperoxidase), as well as by post-embedding immunogold labelling employing a new system for quantitation and for specificity testing under the conditions of the immunocytochemical procedure. A new antiserum against immunologically purified bovine liver glutamate dehydrogenase or antibodies isolated from this by affinity chromatography were used in rats fixed by perfusion with aldehydes. The pre-embedding method displayed peroxidase reaction preferentially in mitochondria of astroglial cells (including the Bergmann glia). Mitochondria of neuronal tissue elements were usually free of peroxidase-reaction product. Extra-mitochondrial staining was not observed. The post-embedding immunogold method was employed to overcome penetration problems and allow semiquantitative analysis of localization and specificity. The highest densities of gold particles were found over the mitochondria in astroglial cell elements (including the Bergmann glia). Mitochondria in cell bodies of Bergmann glia had a lower particle density than those in astrocytic processes. In the latter, analysis of frequency distribution revealed no evidence of a population of mitochondria lacking glutamate dehydrogenase, but suggested the presence of populations with different levels of immunoreactivity. Comparison with the labelling of embedded bovine liver glutamate dehydrogenase indicated that the enzyme constitutes a high proportion (10%) of the total matrix protein of these mitochondria. A weaker but significant labelling was found in oligodendrocytes of the white matter. The labelling of mitochondria in neuronal elements including glutamatergic mossy fibre terminals was of the order of 15% of that in astroglial mitochondria. No difference was detected between glutamatergic neurons (mossy and parallel fibres, granular cells) and non-glutamatergic neurons (Purkinje cells). The particle density over non-mitochondrial areas was very close to background over empty resin. The results, obtained with different methods of tissue and antibody preparation, agree to show that the present form of glutamate dehydrogenase is restricted to mitochondria and preferentially localized in astrocytes.

Animals↗
PubMed1993

GABA- and glycine-immunoreactive neurons in the spinal cord of the carp, Cyprinus carpio.

gamma-Aminobutyric acid (GABA) and glycine are the two main inhibitory transmitter amino acids in the central nervous system of vertebrates. The distribution of cells containing GABA and glycine in the carp spinal cord was examined by using specific antisera raised against the two amino acids conjugated to bovine serum albumin. The immunoreaction on serial paraffin sections was visualized by a streptavidin-biotin method. Both antisera gave highly specific labelings of cells. At least three types of GABA-immunoreactive cells were found. They were small cells in the dorsal grey matter, various sized cells in the central and ventral grey, and some ependymal cells contacting the central canal. In addition, very small cells and neuropil structures in the dorsal horn were strongly immunoreactive to the GABA serum. Certain cells in the ventral horn have moderate numbers of labelled synaptic boutons on the perikarya, but very few GABA-labelled terminals were found on putative motoneurons. The immunoreactive ependymal cells appeared to have a ventrolaterally directed axon. The glycine antiserum labelled small and intermediate cells in the dorsal grey, large, elongated cells in the median region, and varying sized cells in the ventral grey. The numbers and density of immunoreactive cells and neuropil structures in the ventral horn were fewer and lower than in GABA-stained sections. The median large cells had a thick ventrolateral process. The ventral intermediate cells were often found near putative motoneurons. Labelled synaptic boutons were present on most ventral cells including putative motoneurons and interneurons. Abundant distribution of cells immunoreactive to both antisera suggest important roles of both GABA and glycine as neurotransmitters for controlling swimming movements in teleosts.

Animals↗
PubMed1993

Glutamate-like immunoreactivity in retinal terminals of the mouse suprachiasmatic nucleus.

With a view to identifying the neurotransmitter content of retinal terminals within the mouse suprachiasmatic nucleus, a highly specific antiserum to glutaraldehyde-coupled glutamate was used in a postembedding immunogold procedure at the ultrastructural level. Retinal terminals were identified by cholera toxin--horseradish peroxidase transported anterogradely from the retina and reacted with tetramethyl benzidine/tungstate/H2O2, or by their characteristically pale and distended mitochondria with irregular cristae. Controls included model ultrathin sections containing high concentrations of various amino acids. Alternate serial sections were labelled with anti-glutamate and anti-gamma-aminobutyric acid (GABA). Data were analysed by computer-assisted image analysis. Density of glutamate labelling (gold particles per micron2) on whole retinal terminals was > 3 times higher than that on postsynaptic dendrites, and > 5 times higher than that on miscellaneous non-retinal non-glutamatergic terminals in the suprachiasmatic nucleus. The overall density of gold particles over retinal terminals was approximately 3 times higher than that over GABAergic terminals, in which glutamate-like immunoreactivity was mainly mitochondrial. Labelling of vesicles in retinal terminals was almost 5 times greater than the apparent labelling of vesicles in GABAergic terminals, underscoring the location of transmitter glutamate within synaptic vesicles in retinal terminals. In the retino-recipient region of the suprachiasmatic nucleus there was also a small population of non-retinal glutamatergic terminals. Their overall immunoreactivity was similar to or exceeded that of retinal terminals, but morphological features clearly distinguished between these two types of glutamate-containing terminals. The present results indicate that the vast majority of retinal terminals may use glutamate as a transmitter, in keeping with electrophysiological and neuropharmacological data from other sources. The possibility of cotransmitters within retinal terminals, suggested by the presence of dense-core vesicles among the glutamate-containing synaptic vesicles, has still to be addressed.

Animals↗
PubMed1993

Identified hair follicle afferent boutons in the spinal cord of the cat are enriched with L-glutamate-like immunoreactivity.

Hair follicle afferent boutons in the spinal dorsal horn of the cat were examined for L-glutamate enrichment. Two hair follicle afferent axons were labelled intra-axonally with horseradish peroxidase, and post-embedding immunogold reactions of L-glutamate were performed on thin sections containing horseradish peroxidase-labelled boutons. Quantitative analysis showed that hair follicle boutons were associated with immunogold reactions for L-glutamate which were almost twice as dense as average values for dorsal horn tissue. Further analysis revealed that hair afferent boutons displayed 2.3-times the average gold particle density associated with post-synaptic dendrites and 3-times the average immunogold density for L-glutamate of structures which were known to be immunoreactive for GABA. This enrichment of L-glutamate in identified hair afferent terminals supports the idea that the amino acid is a neurotransmitter of hair follicle primary afferent axons.

Afferent Pathways↗
PubMed1993

Immunocytochemical localization of amino acid neurotransmitter candidates in the ventral horn of the cat spinal cord: a light microscopic study.

The distribution of immunoreactivities to six amino acids, possibly related to synaptic function, was investigated in the motor nucleus of the cat L7 spinal cord (laminae VII and IX) using a postembedding peroxidase-antiperoxidase technique. Consecutive 0.5 micron transverse sections of plastic-embedded tissue were incubated with antisera raised against protein-glutaraldehyde conjugates of gamma-aminobutyric acid (GABA), glycine, aspartate, glutamate, homocysteate, and taurine. This method allowed localization of the different immunoreactivities in individual cell profiles. The results showed that all these amino acids, except homocysteate, could be clearly detected in either neuronal or glial elements in the ventral horn. In cell bodies of neurons in lamina VII, immunoreactivity was observed for aspartate, glutamate, GABA, and glycine. Adjacent section analysis revealed that combinations of immunoreactivity for glycine/glutamate/aspartate, GABA/glycine/glutamate/aspartate and glutamate/aspartate, respectively, may occur in one and the same cell. In the motor nuclei (lamina IX), immunoreactivity to amino acids was observed in two types of neuron. Large cells, probably representing alpha-motoneurons, were harboring immunoreactivity to both glutamate and aspartate, while a few small neurons in this area displayed a colocalization of glycine, glutamate, and aspartate. Dendrites and axons in the motor nuclei contained glycine/glutamate/aspartate, GABA/glycine/glutamate/aspartate, and glutamate/aspartate immunoreactivities. In both laminae VII and IX, taurine-like immunoreactivity was absent in neuronal cell bodies, but highly concentrated in perivascular cells and small cells with a morphology resembling that of glial cells. A punctate immunolabeling, in all probability representing labeling of nerve terminals, could be demonstrated in the ventral horn for GABA, glycine, and glutamate, but not with certainty for aspartate or taurine. A quantitative estimate of the covering of cell bodies of alpha-motoneuron size by immunoreactive puncta revealed that glycine immunoreactive terminal-like structures were most abundant (covering 26-42% of the somatic membrane), while glutamate immunoreactive terminals were seen least frequently (5-9% covering). GABA-immunoreactive terminals covered from 10 to 24% of the soma surface.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗
PubMed1993

Demonstration of glutamate/aspartate uptake activity in nerve endings by use of antibodies recognizing exogenous D-aspartate.

Nerve terminals as well as glial cells are thought to possess high-affinity Na(+)-dependent transport sites for excitatory amino acids. However, recent immunocytochemical results with antibodies against such a transporter isolated from rat brain showed a selective labelling of glial cells [Danbolt et al. (1992) Neuroscience 51, 295-310]. Critical evaluation of the literature indicates that previous evidence for nerve terminal uptake of acidic amino acids might possibly be attributed to glia. To find out whether there is indeed a glutamate transporter in nerve endings, we incubated hippocampal slices with D-aspartate (10 and 50 microM), a metabolically inert substrate for the high-affinity glutamate transport system. After fixation by glutaraldehyde/formaldehyde the slices were processed immunocytochemically with specific polyclonal antibodies raised against D-aspartate coupled to albumin by glutaraldehyde/formaldehyde. The electron-microscopic postembedding immunogold technique demonstrated a large accumulation of gold particles in nerve terminals making asymmetrical synapses, compared to their postsynaptic dendritic spines, as well as in glial cell processes. The labelled terminals include those of the glutamatergic Schaffer collaterals. Axosomatic boutons appeared unlabelled. Comparison with a test conjugate with known concentration of fixed D-aspartate (94 mM) suggests that the concentration attained in the terminals after incubation with 50 microM D-aspartate was in the lower millimolar range. The uptake was totally dependent on Na+, blocked by L-threo-3-hydroxyaspartate, and had a high affinity for D-aspartate (apparent Km about 20 microM). There was no labelling in slices incubated without D-aspartate. Compared to glia, the nerve terminals had a higher D-aspartate density and accounted for a much higher proportion of the total tissue uptake, but this relationship may be different in vivo. At the light-microscopic level the D-aspartate-like immunoreactivity showed a distinct laminar distribution, identical to that shown autoradiographically for D-[3H]aspartate and L-[3H]glutamate uptake sites [Taxt and Storm-Mathisen (1984) Neuroscience 11, 79-100], and corresponding to the terminal fields of the major excitatory fibre systems in the hippocampal formation. The novel approach described here establishes that glutamatergic nerve terminals as well as glia do sustain sodium-dependent high-affinity transport of excitatory amino acids, implying that more than one glutamate transporter must be present in the brain. Immunogold detection of D-aspartate gives a much higher anatomical resolution than electron microscopic autoradiography of D-[3H]aspartate or L-[3H]glutamate uptake, the only method that has been available previously for ultrastructural demonstration of uptake activity.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1993

In vitro binding of [3H]bilirubin to neurons in rat brain sections.

Slide-mounted 12-microns cryostat sections of rat brain were incubated with [3H]bilirubin, washed, dried, and apposed to emulsion-coated coverslips for autoradiography. The binding appeared to be nonsaturable. Within the gray matter, binding was concentrated over neuronal cell bodies (particularly evident over hippocampal pyramidal and granular cells, and over cerebellar Purkinje cells), suggesting that the preferential neuronal toxicity of bilirubin may be related to neuronal binding. Regional differences in bilirubin binding were not demonstrated.

Animals↗
PubMed1992

Direct observations of synapses between L-glutamate-immunoreactive boutons and identified spinocervical tract neurones in the spinal cord of the cat.

Four spinocervical tract cells in lumbosacral spinal cords of adult cats were physiologically characterized and intracellularly labelled with horseradish peroxidase. The neurones were examined with a light microscope and reconstructed. Selected regions were chosen for ultrastructural analysis. Thin sections were treated to reveal the presence of L-glutamate by using the postembedding immunogold method. Two antisera, which specifically recognise the presence of fixed glutamate in tissue, were used in the study. Somata, proximal, and distal dendrites of all four neurones received synaptic contacts from boutons which displayed an obvious immunogold reaction. These boutons formed between 35% and 48% of all synaptic contacts onto spinocervical tract cells. Glutamate-enriched boutons were associated with gold particle densities which were 2-3 times greater than the average densities associated with the surrounding neuropil. Their profiles had a mean diameter of 1.68 microns, contained round agranular synaptic vesicles, and formed asymmetrical synaptic junctions. However, not all boutons displaying these characteristics were enriched with glutamate. Immunogold studies of alternate thin sections, which were incubated with glutamate or GABA antiserum, demonstrated that synaptic boutons on spinocervical tract cells were either enriched with GABA or with glutamate and formed two separate populations which had distinct morphological characteristics. GABA-containing boutons contained irregularly shaped agranular vesicles and formed symmetrical synaptic junctions, whereas glutamate-enriched boutons corresponded to those described above. A further population of boutons, containing highly flattened vesicles, was not immunoreactive for GABA or glutamate. The evidence supports the idea that much of the excitatory transmission into the SCT is mediated by L-glutamate.

Animals↗
PubMed1992

Cloning and expression of a rat brain L-glutamate transporter.

Synaptic transmission of most vertebrate synapses is thought to be terminated by rapid transport of the neurotransmitter into presynaptic nerve terminals or neuroglia. L-Glutamate is the major excitatory transmitter in brain and its transport represents the mechanism by which it is removed from the synaptic cleft and kept below toxic levels. Here we use an antibody against a glial L-glutamate transporter from rat brain to isolate a complementary DNA clone encoding this transporter. Expression of this cDNA in transfected HeLa cells indicates that L-glutamate accumulation requires external sodium and internal potassium and transport shows the expected stereospecificity. The cDNA sequence predicts a protein of 573 amino acids with 8-9 putative transmembrane alpha-helices. Database searches indicate that this protein is not homologous to any identified protein of mammalian origin, including the recently described superfamily of neurotransmitter transporters. This protein therefore seems to be a member of a new family of transport molecules.

Amino Acid Sequence↗
PubMed1992

The termination pattern and postsynaptic targets of rubrospinal fibers in the rat spinal cord: a light and electron microscopic study.

The spinal course, termination pattern, and postsynaptic targets of the rubrospinal tract, which is known to contribute to the initiation and execution of movements, were studied in the rat at the light and electron microscopic levels by using the anterograde tracer Phaseolus vulgaris-leucoagglutinin (PHA-L) in combination with calbindin-D28k (CaBP), gamma-aminobutyric acid (GABA), and glycine immunocytochemistry. After injections of PHA-L unilaterally into the red nucleus, labelled fibers and terminals were detected at cervical, thoracic, and lumbar segments of the spinal cord. Most of the descending fibers were located in the dorsolateral funiculus contralateral to the injection site, but axons descending ipsilaterally were also revealed. Rubrospinal axon terminals were predominantly found in laminae V-VI and in the dorsal part of lamina VII at all levels and on both sides of the spinal cord, but stained collaterals were also seen in the ventrolateral aspect of Clark's column and in the ventral regions of lamina VII on both sides. The proportion of axonal varicosities revealed on the ipsilateral side varied at different segments and represented 10-28% of the total number of labelled boutons. Most of the labelled boutons were engaged in synaptic contacts with dendrites. Of the 137 rubrospinal boutons investigated, only 2 were found to establish axosomatic synaptic junctions in the lumbar spinal cord contralateral to the PHA-L injection. With the postembedding immunogold method, 80.8% of dendrites establishing synaptic contacts with rubrospinal terminals did not show immunoreactivity for either GABA or glycine, whereas 19.2% of them were immunoreactive for both amino acids. Rubrospinal axons made multiple contacts with CaBP-immunoreactive neurons in laminae V-VI. Synaptic contacts between rubrospinal terminals and CaBP-immunoreactive dendrites were identified at the electron microscopic level, and all CaBP-containing postsynaptic dendrites investigated were negative for both GABA and glycine. The results suggest that rubrospinal terminals establish synaptic contacts with both excitatory and inhibitory interneurons in the rat spinal cord, and a population of excitatory interneurons receiving monosynaptic rubrospinal input is located in laminae V-VI.

Animals↗