Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.14.16.2 (tyrosine hydroxylase)
 14,760 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three neurotrophic factors associated with the nigrostriatal dopaminergic system were tested for their trophic potential to rescue degenerating substantia nigra dopaminergic neurons in adult rats with transections of the medial forebrain bundle. Axotomy of nigral dopaminergic neurons results in a retrograde degeneration of their cell bodies. Unilateral transections resulted in a partial reduction of the number of dopaminergic neurons as identified by immunocytochemistry for tyrosine hydroxylase to approximately half of the number of neurons present on the intact contralateral substantia nigra. A similar percentage loss was found for the subpopulation of nigral neurons which contain the calcium binding protein calretinin. In contrast, the small subpopulation of neurons which contain calbindin was less sensitive to the lesion and showed only mild loss in the number of cells, which was reduced to 87% of control. Neurotrophin-4/5, transforming growth factor alpha or basic fibroblast growth factor were infused supranigrally for two weeks after transection. None of the trophic factors tested reversed the loss of tyrosine hydroxylase-positive or calretinin-positive cells. In contrast, neurotrophin-4/5, but not transforming growth factor alpha or basic fibroblast growth factor, was found to reverse the axotomy-induced loss of calbindin-positive neurons and indeed increased the number of cells to 45% above control levels. In addition, neurotrophin-4/5 elevated the number of calbindin-containing neurons in intact unlesioned animals to 15% above control. These findings suggest that neurotrophin-4/5 selectively acts on nigral calbindin neurons following medial forebrain bundle transection and prevents these cells from degenerating.
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PMID:Neurotrophin-4/5 selectively protects nigral calbindin-containing neurons in rats with medial forebrain bundle transections. 873 19

The present study compares the distribution of three calcium binding proteins, calbindin-D28k, calretinin, and parvalbumin, in the midbrain tegmentum of rats and humans. In order to compare the distributions of these proteins directly, the cytoarchitecture of this region was evaluated by using immunohistochemistry for tyrosine hydroxylase and substance P in serial sections in both transverse and horizontal planes. There was a high degree of homology in the cytoarchitecture of the three main dopaminergic regions identified. The A8 group was localised in the retrorubral fields, which extended rostrally into the midbrain reticular fields in the human. The A9 group corresponded to the substantia nigra, which was delimited by its dense substance P innervation. The heterogeneous A10 group, situated along the dorsal border as well as medial to the A9 group, comprised multiple nuclei. The distribution of calcium binding proteins was similar in both species, although a larger proportion of neurons contained these proteins in the rat. Calbindin-D28k was localised in neurons within A8 and A10 nuclei and within the caudomedial A9 region (and rostrolateral A9 in the rat only). Calretinin was localised in similar regions. In contrast, neurons containing parvalbumin were concentrated in the substantia nigra pars reticulata. The results suggest that few dopaminergic neurons receiving striatal input in the substantia nigra contain calcium binding proteins; rather, the nondopaminergic nigral neurons contain parvalbumin. Interestingly, dopaminergic neurons are more numerous in humans, whereas nondopaminergic neurons predominate in rats, which suggests that functional differences may exist between rats and humans.
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PMID:Cytoarchitectural distribution of calcium binding proteins in midbrain dopaminergic regions of rats and humans. 878 81

The calcium-binding proteins Calbindin-D28k and calretinin are co-localized with dopamine in some of the midbrain dopaminergic neurons in the rat and monkey; the present study sought to examine the pattern of co-localization in the mouse. Double immunofluorescence staining procedures were used for tyrosine hydroxylase (a dopaminergic cell marker) and Calbindin-D28k or calretinin. Midbrain dopaminergic neurons were examined at four rostrocaudal levels, and the percentage of cells that contained both tyrosine hydroxylase and either of the two calcium-binding proteins was determined in nucleus A8 (retrorubral field), nucleus A9 (substantia nigra pars compacta, pars reticulata and pars lateralis) and nucleus A10 (nucleus paranigralis, ventral tegmental area, interfascicular nucleus, central linear nucleus). The two calcium-binding proteins were distributed similarly in midbrain dopaminergic neurons in the several nuclear groups that comprise nuclei A8, A9 and A10. The calcium-binding proteins were found in the majority (50-100%) of nucleus A10 neurons, whereas in nuclei A8 and A9 (except for the substantia nigra pars lateralis) less than 40% of the cells contained either calcium-binding protein. The pattern of co-localization in the mouse is similar to that reported for the rat and monkey. The calcium-binding proteins mark the population of midbrain dopaminergic neurons that are less vulnerable to degeneration in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson's disease.
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PMID:Midbrain dopaminergic neurons in the mouse: co-localization with Calbindin-D28K and calretinin. 893 Oct 15

We have localized the dopamine D1 receptor in rat retina using a subtype-specific monoclonal antibody. Immunolabelling can be detected in the inner and outer plexiform layers and in a number of cells in the inner nuclear layer. In the inner plexiform layer, labelled processes form four distinct horizontal bands and a series of patches. In order further to characterize the labelling pattern of the D1 receptor antibody, double-labelling experiments were performed with antibodies against population-specific neuronal markers in the retina. Antibodies against tyrosine hydroxylase, choline acetyltransferase, calretinin, calbindin, the glutamate transporter GLT-1, protein kinase C, recoverin and parvalbumin were co-applied with the D1 receptor antibody. With these cell markers we demonstrate that horizontal cells, at least three types of cone bipolar cells and a small number of amacrine cells are immunolabelled for the D1 receptor. In the inner plexiform layer, processes labelled by the D1 receptor antibody are co-stratified with processes labelled by the GLT-1 antibody. D1 receptor-labelled processes are not co-localized with the processes of amacrine cells and ganglion cells labelled by antibodies against tyrosine hydroxylase, choline acetyltransferase or calretinin. Our results indicate that dopamine D1 receptors are localized predominantly to horizontal cells and cone bipolar cells. Furthermore, the spatial disparity between dopaminergic processes and the site of the majority of D1 receptors supports the idea that in the retina dopamine acts as a neuromodulator that diffuses through extracellular space. The localization of D1 receptors to a number of identified cell types enables future physiological work to be directed towards specific synaptic circuits within the retina.
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PMID:Immunohistochemical localization of dopamine D1 receptors in rat retina. 895 93

In mesencephalic primary cultures derived from E14 rat embryos, calretinin- and tyrosine hydroxylase-immunoreactive neurons comprised 2% and 5% of the total cell population, respectively, at 6-7 days in vitro. The number of calretinin-immunoreactive neurons was unchanged after a 12- or 24-h exposure to 500 microM kainic acid (KA), but a 50% cell loss was detected after a 48-h exposure to KA. Tyrosine hydroxylase-immunoreactive neurons demonstrated a 50% and 67% cell loss at 24- and 48-h exposures to 500 microM KA. A 500 microM N-methyl-D-aspartic acid (NMDA) incubation for 24 h had no effect on calretinin-immunoreactive cell number, but did significantly reduce tyrosine hydroxylase-immunoreactive cell numbers by 26%. In tyrosine hydroxylase-immunoreactive cells, exposure to KA appeared to stimulate the retraction of the neuritic tree and to cause somatic swelling. In contrast, calretinin-immunoreactive neurons developed larger and more complex neuritic trees after a 24-h exposure to 500 microM KA but not NMDA. Immunohistochemical colocalization studies revealed that all tyrosine hydroxylase-immunoreactive and the majority of calretinin-immunoreactive neurons expressed the glutamate receptor subunits GluR2-R3. Very low levels of NMDAR1 receptor subunits were detected on cells in this culture and GluR4 receptor subunits were not detectable. Our experiments showed that glutamate receptors present in both calretinin- and tyrosine hydroxylase-immunoreactive cells were functional, since phosphorylated cAMP/Ca2+ response element-binding protein levels were increased in both cell types after 10 or 30 min exposures to 500 microM KA. The present results indicate that in the mesencephalic cultures tyrosine hydroxylase-immunoreactive cells are more vulnerable to KA excitotoxicity than calretinin-immunoreactive neurons.
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PMID:Differential effects of excitatory amino acids on mesencephalic neurons expressing either calretinin or tyrosine hydroxylase in primary cultures. 901 46

Calbindin-D28k (calbindin) is an intracellular calcium binding protein of unknown in vivo function. It is abundantly expressed in many populations of neurons, and it can, presumably by buffering calcium overload, protect cells against excitotoxic damage. In the midbrain, calbindin is preferentially expressed in those dopamine neurons which are spared from degeneration in Parkinson's disease and its animal models. Whether calbindin itself determines neuronal vulnerability is questioned in other lesion models where calbindin expression is not positively correlated with neuronal resistance. To study the possible neuroprotective role of calbindin in vivo, we generated calbindin-deficient mice by gene targeting and assessed the viability of midbrain dopamine neurons in both a chemical and a genetic lesion paradigm. Tyrosine hydroxylase-immunoreactive neurons were counted in calbindin null-mutant mice treated with the neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and in a calbindin-deficient weaver strain (homozygous for weaver and the calbindin null mutation). The extent and pattern of neuron loss observed in MPTP-treated wild-type and homozygous weaver mice were as previously described. Surprisingly, no significant differences were observed between MPTP-treated calbindin null mutants and their wild-type littermates, or between calbindin-weaver double mutant mice and weaver mice. Thus, in all four groups the same subpopulation of tyrosine hydroxylase-positive midbrain neurons (i.e. those normally containing calbindin) were preferentially spared. Calretinin, a closely related calcium-binding protein, which is also expressed in some midbrain dopamine neurons, was not up-regulated in these surviving neurons. These findings indicate that the resistance of calbindin-containing neurons in the MPTP and weaver models is not causally related to the expression of calbindin, and that endogenous calbindin is not required for protection of these neurons.
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PMID:Vulnerability of midbrain dopaminergic neurons in calbindin-D28k-deficient mice: lack of evidence for a neuroprotective role of endogenous calbindin in MPTP-treated and weaver mice. 904 76

The purpose of this study was to examine the distribution of calretinin immunoreactivity (CR) in the male rat pituitary gland by immunofluorescence microscopy. CR was found in cells of the anterior pituitary and in granules in the posterior pituitary. In the intermediate lobe, nerve fibers in close proximity to the melanotropes were CR-immunoreactive (CR-ir). Fine CR-ir varicose fibers were also observed in the anterior and posterior pituitary. Colocalization studies revealed that the majority of the CR-containing cells of the anterior pituitary also contained thyroid-stimulating hormone (TSH). These CR/TSH cells represented about 32% of the thyrotrope population. Following thyroidectomy, a massive increase in both the number of CR-ir cells and in the expression of CR mRNA was observed in the anterior pituitary. Thyroxine treatment, however, resulted in a reduction in the number and size of the CR-ir cells in the same lobe. In the intermediate lobe, CR-ir was colocalized with tyrosine hydroxylase (TH) immunoreactive dopaminergic fibers. These intermediate lobe fibers disappeared following pituitary stalk section, as did the CR/TH fibers and the CR-ir granular material in the posterior pituitary. The findings in the anterior pituitary suggest that consideration be given to the idea that CR might function in the synthesis and/or release mechanism of TSH in thyrotropes and that its expression is modulated by the hypothalamo-pituitary-thyroid axis.
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PMID:Calretinin in the rat pituitary: colocalization with thyroid-stimulating hormone. 908 99

In the glomerular layer of the rat main olfactory bulb, we previously reported three chemically defined interneuron groups: GABA-like immunoreactive, calretinin-immunoreactive and Calbindin-D28k-immunoreactive groups [Kosaka K. et al. (1995) Neurosci. Res. 23, 73-88]. In the present study, we analysed the structural features of these three neuron groups using confocal laser scanning light microscopy, focusing on their dendritic arborization pattern, especially on their close apposition to olfactory receptor terminals labeled by olfactory marker protein. Each glomerulus consisted of two zones, the olfactory nerve zone and the non-olfactory nerve zone. The former was mainly occupied by olfactory nerve preterminals and terminals as well as their targets, postsynaptic fine dendritic portions of intrinsic neurons. The latter non-olfactory nerve zone was occupied mainly by olfactory marker protein-negative profiles. Processes of GABAergic neurons and those of one of their subpopulations, tyrosine hydroxylase-immunoreactive neurons, were numerous both in the olfactory nerve and non-olfactory nerve zones, resulting in their frequent close apposition to olfactory marker protein-immunoreactive elements. Combined confocal laser scanning light microscopic electron microscopic examination revealed synaptic contacts from olfactory nerve terminals on tyrosine hydroxylase-immunoreactive processes at these sites of close apposition. In contrast, calretinin-immunoreactive and Calbindin-D28k-immunoreactive processes, particularly Calbindin-D28k-immunoreactive ones, were distributed almost exclusively in the non-olfactory nerve zone, as if they avoided the olfactory nerve zone, showing a net or honeycomb pattern. Thus, calretinin-immunoreactive and Calbindin-D28k-immunoreactive processes were not or very rarely closely apposed to olfactory nerve terminals. These findings suggested that there might be some differences among chemically defined interneuronal groups in their synaptic contacts from olfactory nerves. Further quantitative image analysis clearly exhibited the prominent differences among these neuron groups in their intraglomerular dendritic arborization in relation with the olfactory nerve zone, i.e. the percentages of the area in the olfactory nerve zone occupied by GABAergic and tyrosine hydroxylase-immunoreactive processes were about 10%, respectively, whereas those of calretinin-immunoreactive and Calbindin-D28k-immunoreactive processes were only about 1% and 0.3%, respectively. These findings suggested that so-called periglomerular cells in glomeruli might be heterogeneous not only in their chemical nature, but also in their dendritic arborization pattern and synaptic contacts from olfactory nerve terminals.
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PMID:Chemically defined neuron groups and their subpopulations in the glomerular layer of the rat main olfactory bulb--II. Prominent differences in the intraglomerular dendritic arborization and their relationship to olfactory nerve terminals. 913 50

Olfactory bulbs (OBs) from embryonic day 15 and 17 and postnatal day 1 mice were transplanted into the lateral ventricle of juvenile host mice without bulbectomy, and fine structural and chemical features of neurons and glia in the OB transplants were investigated immunocytochemically and electron microscopically. In the OB transplants there were neither clearly defined glomeruli nor layers, nor olfactory marker protein immunoreactive elements. However, chemically defined neuronal populations resembling those in the normal OBs such as those immunoreactive for gamma-aminobutyric acid (GABA), tyrosine hydroxylase and Ca(2+)-binding proteins (calbindin-D28K, calretinin, parvalbumin) were observed. Electron microscopically, dendrodendritic and somatodendritic reciprocal synapses, that is, synapses characteristic of the OB, were occasionally observed in the OB transplants. These results indicated that at least some embryonic or newborn mouse OB neurons and/or precursor cells could exhibit chemical properties and form typical synaptic contacts observed in normal OB, even when they received no inputs from olfactory receptor cells.
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PMID:Differentiation of chemically defined neuronal populations in the transplanted olfactory bulb without olfactory receptor innervation. 917 76

In the rabbit retina, parvalbumin has been localized selectively to AII amacrine cells, while 28 kDa calbindin could be detected in horizontal cells, in one type of depolarizing cone bipolar cell and a population of wide-field amacrine cells. The distribution of the third neuronal calcium binding protein, calretinin, however, has not been studied to date in detail in the rabbit retina. Therefore in this study we aimed to describe the overall distribution of calretinin in the different retinal layers and the possible colocalization pattern with other neurochemical marker molecules. A few cone photoreceptor cells were found to be labeled, whereas the outer plexiform layer was free from immunoreactive elements. In the most proximal row of the inner nuclear layer amacrine cells were labeled, while more distally a few cells emitted beaded axon-like processes toward the outer retina. There were large (18-28 microm in diameter) cells labeled in the ganglion cell layer, of which many apparently had their axon stained. Some of the calretinin immunoreactive amacrine cells (the AII neurons) also contained parvalbumin. Colocalization of calretinin and 28 kDa calbindin could not be ascertained in the same amacrine cell populations, nor was tyrosine hydroxylase present in calretinin-containing cells. There was partial colocalization of calretinin in the gamma-aminobutyric acid-positive amacrine cell population. Parvalbumin containing ganglion cells were also positive for calretinin; however, the calretinin-positive ganglion cells were more numerous. gamma-Aminobutyric acid could be colocalized in some calretinin-positive neurons of the ganglion cell layer.
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PMID:Calretinin in neurochemically well-defined cell populations of rabbit retina. 927 31


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