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  • 1
    Electronic Resource
    Electronic Resource
    Alterations in Catecholamine System Enzymes (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 771 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb44677.x
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of N-terminus-deleted human tyrosine hydroxylase type 1 by end products of catecholamine biosynthetic pathway (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 1415-1428 
    Details
    ISSN: 1435-1463
    Keywords: Tyrosine hydroxylase ; deletion mutagenesis ; catecholamine ; tetrahydrobiopterin ; expression inEscherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The N-terminal 52-, 70-, and 157-amino acids-deleted mutants and wild-type tyrosine hydroxylases were expressed inEscherichia coli and utilized to investigate the roles of the N-terminus in the catecholamine inhibition on enzyme activity. Their lysate's supernatants were used as enzyme samples. Three catecholamines, namely dopamine, norepinephrine, and epinephrine, affected both wild-type and mutant enzymes after preincubation in the mode of mixed inhibition, and the most marked alteration among the kinetic parameters produced by the deletion was the increase in the inhibition constants. The deletions also abolished the catecholamine-induced shift of the pH profile of the enzyme activity toward a more acidic pH optimum. All three mutants responded to catecholamines almost in the same way. These results suggest that the three catecholamine end products exert their inhibition on tyrosine hydroxylase to the same extent and that the N-terminal 52 amino acid residues contain the key sequence in mediating the inhibitory action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01271255
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  • 3
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of GTP cyclohydrolase I in the brain, adrenal gland, and liver of mice (1995)
    Springer
    Journal of neural transmission 102 (1995), S. 175-188 
    Details
    ISSN: 1435-1463
    Keywords: GTP cyclohydrolase I ; tyrosine hydroxylase ; tryptophan hydroxylase ; phenylalanine hydroxylase ; tetrahydrobiopterin ; liver ; adrenal medulla ; brain ; mouse ; immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary GTP cyclohydrolase I (GCH) is the first and rate-limiting enzyme for the biosynthesis of tetrahydrobiopterin (BH4), the cofactor of phenylalanine, tyrosine, and tryptophan hydroxylases, the enzymes that synthesize tyrosine, catecholamines (dopamine, noradrenaline, and adrenaline), and serotonin, respectively. We produced for the first time polyclonal antibody with highly sensitive immunoreactivity against an oligopeptide of rat enzyme, GFPERELPRPGA, by immunization of rabbits with the peptide conjugated to hemocyanin by glutaraldehyde. The specificity of the antibody was confirmed by Western blot analysis. Using this antibody specific for GCH, we observed strong GCH immunostaining in the liver cells, in the dopamine-, noradrenaline-, adrenaline-, or serotonin-containing cells of the brain, and in the adrenal gland of mice. Immunocytochemical studies revealed GCH to be localized in monoamine-containing perikarya in the periglomerular cells of the olfactory bulb, zona incerta, arcuate nucleus, ventral tegmental area, substantia nigra pars compacta, locus ceruleus, nucleus tractus solitarius, area postrema, and ventrolateral area of the medulla oblongata. GCH immunostaining was particularly strong in serotoninergic nuclei, such as dorsal and median raphe nuclei, nucleus raphe pallidus, and nucleus raphe magnus. By immunoelectron micoscopy, GCH-labeled cytoplasm and microtubules in the processes were observed ultrastructurally, but no staining was found in the mitochondria, and Golgi apparatus. Immunostaining was observed neither in the group D neurons that contain only aromatic amino acid decarboxylase without tyrosine hydroxylase, nor in glial cells and endothelial cells. These results indicate the abundant presence of GCH in catecholaminergic and serotoninergic neurons as well as in the adrenal medulla and liver, where BH4 is synthesized as the cofactor of tyrosine, tryptophan, and phenylalanine hydroxylases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01281153
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  • 4
    Electronic Resource
    Electronic Resource
    Immunocytochemical study of catecholaminergic neurons in the senescence-accelerated mouse (SAM-P8) brain (1997)
    Springer
    Journal of neural transmission 104 (1997), S. 1267-1275 
    Details
    ISSN: 1435-1463
    Keywords: Catecholamine ; senescence-accelerated mouse (SAM-P8) ; immunocytochemistry ; aging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The catecholaminergic neurons of senescence-accelerated mice (SAM-P8) were analyzed by immunohistochemical microphotometry in terms of immunoreactivities to aromatic L-amino acid decarboxylase (AADC), dopamine (DA), or noradrenaline (NA). Accelerated senescence-resistant mice (SAM-R1) were used as control mice. The immunoreactivities to AADC, DA, and NA of the catecholaminergic neurons of the SAM-P8 mice were weaker than those of the SAM-R1 mice in all the brain regions. Immunoelectron microscopy revealed progressive degeneration of dopaminergic neurons and their terminal fibers in the substantia nigra as well as in noradrenergic neurons and their proximal dendrites in the locus coeruleus of the SAM-P8 mice. In contrast, there was no difference between the SAM-P8 and SAM-R1 mice in the distribution of AADC-only positive neurons (designated as D neurons in the rat brain by Jaeger et al.) nor in their immunoreactivities. These results may indicate that DA neurons in the substantia nigra and NA neurons in the locus coeruleus degenarate more rapidly during aging in SAM-P8 mice than in control SAM-R1 mice and that D neurons may function as a part of a compensatory system for the decreases in catecholaminergic neurons during aging.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01294727
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  • 5
    Electronic Resource
    Electronic Resource
    Expression of human tyrosine hydroxylase type I in Escherichia coli as a protease-cleavable fusion protein (1999)
    Springer
    Journal of neural transmission 106 (1999), S. 819-824 
    Details
    ISSN: 1435-1463
    Keywords: Keywords: Human tyrosine hydroxylase type 1 ; N-terminal amino acid-deleted mutant ; maltose-binding protein fusion.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary. Wild-type and N-terminal 35-, 38-, and 44-amino acid-deleted mutants of human tyrosine hydroxylase type 1 (hTH1) fused to maltose-binding protein via the target sequence for a restriction protease were expressed in Escherichia coli and purified. The fused protein was treated with the restriction protease factor Xa or enterokinase to isolate hTH1 from the fused form. The treatment of fused wild-type and 35-amino acid-deleted mutant with factor Xa and enterokinase caused non-specific cleavages in the vicinity of the phosphorylation sites, Ser19 and Ser40, due to the flexible conformation of the N-terminus of hTH1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007020050202
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  • 6
    Electronic Resource
    Electronic Resource
    Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain (1999)
    Springer
    Journal of neural transmission 106 (1999), S. 607-617 
    Details
    ISSN: 1435-1463
    Keywords: Keywords: Aromatic L-amino acid decarboxylase ; brain ; colocalization ; GTP cyclohydrolase I ; human ; immunohistochemistry ; tetrahydrobiopterin ; tyrosine hydroxylase.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary. Guanosine triphosphate (GTP) cyclohydrolase I (GCH) is the first and rate-limiting enzyme for biosynthesis of tetrahydrobiopterin, the cofactor of tyrosine hydroxylase (TH). Our previous study reported the presence of GCH in several neuronal groups in animal brains using a newly raised anti-GCH antibody. The present study aims at elucidating whether GCH and TH coexist in the same neurons of the human brain with the aid of immunohistochemical dual labeling. GCH-immunoreactivity was observed in the cell bodies and fibers of monoaminergic neurons of the human brain. Neurons which contain both enzymes are seen in the human substantia nigra, ventral tegmental area, locus coeruleus, dorsal raphe, and zona incerta. In these regions, almost all the cells also show immunoreactivity for aromatic L-amino acid decarboxylase (AADC), the second step enzyme for catecholamine synthesis, indicating that these neurons are catecholaminergic. However, some neurons in the dorsal and dorsomedial hypothalamic nuclei are stained only for GCH or TH. They appear to constitute an independent cell group in the human brain. The present observation suggests that L-dopa is not produced in the cells immunoreactive for TH but not for GCH, and that TH in these cells which lack GCH may have an unidentified role other than dopa synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007020050183
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of an alternative promoter that regulates tissue-specific expression of the human aromatic L-amino acid decarboxylase gene in cultured cell lines (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 1-15 
    Details
    ISSN: 1435-1463
    Keywords: Aromatic L-amino acid decarboxylase ; alternative promoter ; tissue-specific expression ; transfection experiment ; DNase I hypersensitive site
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The human aromatic L-amino acid decarboxylase (AADC) gene is transcribed in a tissue-specific manner by an alternative promoter. In this study using human cultured cell lines, we analyzed the alternative promoter that regulates tissue-specific expression of AADC. Neither neuronalnor nonneuronal-type mRNA of AADC was detected in HeLa cells, nonneuronal-type mRNA of AADC was expressed in HepG2 cells, and the neuronal-type was expressed in the SK-N-SH cell line. We examined the promoter activities located in 5′- and 3′-flanking regions of exon N1 and exon L1 by transfection experiments. Plasmids containing 5′-flanking regions of exon L1, the shortest of which was 0.3kb, could promote specifically high expression of the reporter gene in HepG2 cells. On the other hand, plasmids containing 5′-flanking regions of exon N1 (3.6 kb to 0.5 kb) could promote the reporter gene expression not only in SK-N-SH cells but also in HeLa and HepG2. More enhanced expression were observed by transfection of plasmids containing parts of the first intron in these cell lines. Thus, these results suggest that the basal liver-specific promoter activity is located in the 5′-flanking region of exon L1 and that the first intron may also be needed for enhanced expression rather than determination of cell-specificity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01292612
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation of a full-length cDNA clone for human GTP cyclohydrolase I type 1 from pheochromocytoma (1995)
    Springer
    Journal of neural transmission 101 (1995), S. 237-242 
    Details
    ISSN: 1435-1463
    Keywords: GTP cyclohydrolase I ; tetrahydrobiopterin ; cDNA ; mRNA ; pheochromocytoma ; (Human)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Although the existence of three different cDNA forms of human GTP cyclohydrolase I (GCH I) have been reported (Togari et al., 1992), the full-length sequence of any human GCH I cDNA involving poly (A) tail has not yet been documented. In the present study, we first isolated a full-length cDNA clone encoding human GCH I type 1 from human pheochromocytoma cDNA library. The length of the cDNA insert was 2,921 base pairs including poly (A) tail. RNA blot analysis showed a single niRNA species of 4.0kb in human pheochromocytoma tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01271561
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  • 9
    Electronic Resource
    Electronic Resource
    Interleukin-2 but not basic fibroblast growth factor is elevated in parkinsonian brain (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 1077-1081 
    Details
    ISSN: 1435-1463
    Keywords: Interleukin-2 ; basic fibroblast growth factor ; Parkinson's disease ; brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The contents of interleukin (IL)-2 and basic fibroblast growth factor (bFGF) were measured in the brain (caudate nucleus, putamen, and cerebral cortex) from control and parkinsonian patients by highly sensitive enzyme-linked immunosorbent assay (ELISA). The concentrations of IL-2 in the brain were in the order of pg/mg protein, and the values were significantly higher in the caudate and putamen from parkinsonian patients than those from control patients. However, the levels of IL-2 in the cerebral cortex showed no significant difference between parkinsonian and control patients. In contrast to IL-2, the bFGF levels in the brain were high and in the order of ng/mg protein, and there was no significant difference in the caudate and putamen between parkinsonian and control patients. Although both IL-2 and bFGF may play important roles in dopaminergic neurons as neurotrophic factors, IL-2 but not bFGF may relate to the compensatory response in the nigrostriatal dopaminergic regions in parkinsonian brain during progress of neurodegeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01291792
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  • 10
    Electronic Resource
    Electronic Resource
    Brain β2-microglobulin levels are elevated in the striatum in Parkinson's diseaselevels are elevated in the striatum in Parkinson's disease (1995)
    Springer
    Journal of neural transmission 9 (1995), S. 87-92 
    Details
    ISSN: 1435-1463
    Keywords: β2-Microglobulin ; tumor necrosis factor-α ; Parkinson's disease ; brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary β2-Microglobulin (B2-MG) content was measured for the first time in the brain (caudate nucleus, putamen, and cerebral cortex) from control and parkinsonian patients by a highly sensitive sandwich enzyme immunoassay. The concentrations of B2-MG in dopaminergic striatal regions were significantly higher in parkinsonian patients than those in controls, whereas those in the cerebral cortex showed no significant difference between parkinsonian and control subjects. Tumor necrosis factor-α (TNF-α) concentrations were also increased in the striatum, confirming our previous findings, but not in the cerebral cortex. Since TNF-α may induce B2-MG expression, these results suggest that an immunological response may occur in the nigrostriatal dopaminergic regions in Parkinson's disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02252965
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