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

Cerebral tryptophan 5-hydroxylase and tyrosine hydroxylase are stimulated by a solution of lyophilized, protein-free 30,000g supernatant of brain homogenates (concentrate 1). This preparation can be further purified by passage through Sephadex G-75 and phosphocellulose columns to yield concentrate 2. Unlike concentrate 1, concentrate 2 is unstable after several days of storage even at -27 degrees C. Neither preparation is active without the presence of a reduced pteridine cofactor. The stimulating factor appears to be thermostable, alkali-labile, dialyzable, and light-sensitive.
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PMID:Cerebral hydroxylases: stimulation by a new factor. 440 58

The synaptic connections of amacrine cells synthesizing or accumulating serotonin in the retina of the cane toad, Bufo marinus, were studied by using preembedding double-labeling electron-microscopic immunocytochemistry. The binding sites of an anti-serotonin antibody were revealed by the diaminobenzidine reaction, whilst a colloidal gold-conjugated secondary antibody was used to detect an antibody to phenylalanine hydroxylase. Since the latter antibody recognizes tryptophan 5-hydroxylase, one of the synthesizing enzymes for serotonin, as well as tyrosine hydroxylase, the rate-limiting enzyme for catecholamine synthesis, the double labeling of the present study enabled us to identify three groups of labeled profiles at the ultrastructural level. The profiles of serotonin-synthesizing amacrine cells contained both diaminobenzidine reaction product and colloidal gold particles, whilst those of serotonin-accumulating and dopaminergic amacrine cells contained only diaminobenzidine reaction product or colloidal gold particles, respectively. The synapses of serotonin-synthesizing or serotonin-accumulating amacrine cells were distributed all through the inner plexiform layer of the retina. The profiles of serotonin-synthesizing amacrine cells predominantly received synapses from, and made synapses onto, unlabeled amacrine cell dendrites. They also received synapses from, and made synapses onto, bipolar cell terminals. They also made synapses onto presumed ganglion cell dendrites. However, the profiles of serotonin-accumulating cells made synapses only with unlabeled amacrine cell processes. There were close contacts between the profiles of serotonin-synthesizing and serotonin-accumulating amacrine cells. No synaptic relationships were observed between dopaminergic and serotonin-synthesizing or serotonin-accumulating amacrine cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Synaptic circuitry of serotonin-synthesizing and serotonin-accumulating amacrine cells in the retina of the cane toad, Bufo marinus. 771 93

Because few previous studies have shown the immunohistochemical localization of tryptophan 5-hydroxylase (TPH) in the gastrointestinal tract, we developed a specific antibody against TPH purified from mouse mastocytoma P-815 and stained human and rat gastrointestinal tracts. The specificity of the antibody was examined by Western blotting and by immunohistochemistry in brain sections. Human ileum and colon specimens, rat stomach, duodenum, jejunum, ileum and colon specimens, with and without colchicine treatment were prepared for immunohistochemistry. Immunoelectron microscopic double staining of TPH and serotonin/chromogranin A and immunofluorescence double staining of TPH and serotonin were performed to identify the cell types. Epithelial enterochromaffin (EC) cells, mast cells in the lamina propria and submucosa, and varicose fibers in the submucosa and muscle layer showed positive immunoreactivity in all segments examined from human and normal rat specimens. In colchicine-treated rat specimens, nerve cell bodies in the myenteric plexus were stained. Because the antibody does not cross react with tyrosine hydroxylase as defined in Western blotting or brain sections, these positive structures may contain TPH. The present results show evidence that EC cells, mast cells, and nerve cell bodies and fibers in the gastrointestinal tracts of both the human and the rat contain TPH and therefore may have the ability to synthesize serotonin from tryptophan.
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PMID:Immunohistochemical localization of tryptophan hydroxylase in the human and rat gastrointestinal tracts. 1042 74

Ipecac syrup, prepared from a galentical ipecac, contains the nauseant alkaloids cephaeline and emetine. The involvement of receptors and serotonin- and dopamine-metabolizing enzymes in the emesis induced by ipecac syrup and these components was investigated. 1) In ferrets, the selective 5-HT3-receptor antagonist ondansetron (0.5 mg/kg, p.o.) prevented each emesis induced by TJN-119 (0.5 mL/kg, p.o.), cephaeline (0.5 mg/kg, p.o.) and emetine (5.0 mg/kg, p.o.), but the intraperitoneal administration of the selective dopamine D2-receptor antagonist sulpiride failed to significantly suppress the TJN-119, cephaeline and emetine-induced emesis at a dose of 0.1 mg/kg that blocked apomorphine-induced emesis. 2) In the receptor binding assays, cephaeline and emetine had a distinct affinity to 5-HT4 receptor, but no or weak affinity to 5-HT1A, 5-HT3, nicotine, M3, beta1, NK1, and D2 receptors. 3) Cephaeline and emetine did not affect activities of metabolic enzymes of 5-HT and dopamine (MAO-A, MAO-B, tryptophan 5-hydroxylase and tyrosine hydroxylase) in vitro. These results suggest that 5-HT3 receptor plays an important role in the emetic action of TJN-119, cephaeline and emetine, and the 5-HT4 receptor may be involved in their mechanisms.
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PMID:Studies for the emetic mechanisms of ipecac syrup (TJN-119) and its active components in ferrets: involvement of 5-hydroxytryptamine receptors. 1212 Jul 52

The synthesis of serotonin and dopamine with purified enzymes is described. Both pathways start from an amino acid substrate and synthesize the monoamine neurotransmitter in two enzymatic steps. The enzymes human tryptophan hydroxylase isoform 2, Rattus norvegicus tyrosine hydroxylase, Chlamydia pneumoniae Cpn1046, and aromatic amino acid decarboxylase from Drosophila melanogaster are recombinantly expressed, purified, and shown to be functional in vitro. The hydroxylases efficiently convert L-DOPA (L-dihydroxy-phenylalanine) and 5-HTP (5-hydroxytryptophan) from L-tyrosine and L-tryptophan, respectively. A single aromatic amino acid decarboxylase is capable of converting both hydroxylated intermediates into the final neurotransmitter. The platform described here may facilitate future efforts to generate medically useful artificial cells and nanofactories.
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PMID:Cell-Free Synthesis of Dopamine and Serotonin in Two Steps with Purified Enzymes. 3310 24