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)

The uterus and vagina of the guinea pig have been examined, region by region, for acetylcholinesterase, tyrosine hydroxylase, dopamine beta-hydroxylase and aromatic amino acid decarboxylase activity, as well as for the neuropeptides, neuropeptide Y, vasoactive intestinal peptide, substance P, enkephalin and somatostatin. No acetylcholinesterase activity was localized in the uterus, though it was present in associated paracervical ganglion tissues. Of the catecholamine-synthesizing enzymes, tyrosine hydroxylase and dopamine beta-hydroxylase activity was found virtually throughout the reproductive tract, whereas aromatic amino acid decarboxylase activity was restricted in its distribution. Neuropeptide distribution was quite varied. Neuropeptide Y was found throughout the endometrium/submucosa but only in the muscularis of the vagina and not in the myometrium. Substance P was localized in the vagina and uterine horn, though not the body of the uterus. Vasoactive intestinal peptide was present in all regions of the endometrium/submucosa, but not in the myometrium of the uterine horn. Enkephalin and somatostatin were not localized in any part of the reproductive tract examined, apart from paracervical ganglion tissues. The types and significance of the nerves supplying the reproductive tract are discussed.
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PMID:An immunohistochemical study of the catecholamine synthesizing enzymes and neuropeptides in the female guinea-pig uterus and vagina. 135 70

Vasoactive intestinal peptide (VIP) has been suggested to be a mediator of vagal inhibition of airway tone and it has been assumed that VIP-containing nerve fibres in the airway arise from intrinsic ganglia. We have used a combination of double- and triple-labelling immunohistochemistry, retrograde axonal tracing, organotypic culture and nerve lesion studies, to identify the origin and distribution of neurons containing immunoreactivity (IR) to VIP in guinea pig airway smooth muscle. We also investigated whether immunoreactivity to other neuropeptides coexisted with VIP-IR within these neurons. We found that all VIP-IR nerve fibres in guinea pig tracheal smooth muscle also contained IR to neuropeptide Y (NPY) but not to tyrosine hydroxylase (TH), a marker for noradrenergic neurons. Both VIP-IR and NPY-IR were absent from nerve cell bodies in the tracheal plexus. After maintenance of isolated trachea in organotypic culture for 4 days, to allow degeneration of extrinsic nerve fibres, nerve fibres containing VIP-IR or NPY-IR were almost completely absent from tracheal smooth muscle. Of ganglia known to supply the trachea, coexistence of VIP-IR and NPY-IR was found only in cell bodies of the stellate ganglion. Retrograde tracing studies using the fluorescent tracer, DiI, confirmed that the stellate ganglion was the site of origin of neurons containing VIP-IR and NPY-IR supplying the airways. These neurons projected to the airways from the stellate ganglion both directly through the mediastinum, and via the cervical sympathetic trunk and vagus nerves. These results suggest that nerve fibres containing both VIP-IR and NPY-IR in the tracheal smooth muscle of the guinea pig are derived from non-noradrenergic cell bodies in the stellate ganglion. The absence of VIP-IR from vagal post-ganglionic neurons suggests that VIP cannot be a mediator of vagal inhibitory transmission in tracheal smooth muscle of this species.
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PMID:Vasoactive intestinal peptide and neuropeptide Y coexist in non-noradrenergic sympathetic neurons to guinea pig trachea. 158 1

Vasoactive intestinal peptide (VIP) increased catecholamine biosynthesis in bovine adrenal chromaffin cells by 50-200%. Six related peptides produced no effects. In addition, VIP increased tyrosine hydroxylase (TH) activity measured in gel-filtered supernatants prepared from homogenates of treated cells. The hypothesis that cyclic AMP is the second messenger involved in these effects of VIP was also evaluated. VIP led to an elevation of cyclic AMP levels, and this increase occurred over a similar concentration range and time course as the activation of TH and the increase in catecholamine biosynthesis. Each measure reached maximal levels at 10-20 microM VIP within 1 min and remained elevated for at least 16 min. These changes produced by VIP were paralleled by enhanced phosphorylation of TH, and this phosphorylation occurred on a single tryptic peptide that was the same peptide whose phosphorylation has been previously shown to be stimulated by forskolin. In contrast to VIP and forskolin, 12-O-tetradecanoylphorbol 13-acetate, a phorbol ester known to activate protein kinase C, increased the phosphorylation on a total of three tryptic peptides of TH. Our results indicate that VIP stimulates catecholamine biosynthesis in chromaffin cells through the phosphorylation and activation of TH and support the conclusion that a cyclic AMP-dependent phosphorylation of TH is responsible for these effects.
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PMID:Vasoactive intestinal peptide stimulates catecholamine biosynthesis in isolated adrenal chromaffin cells: evidence for a cyclic AMP-dependent phosphorylation and activation of tyrosine hydroxylase. 168 Jan 63

Vasoactive intestinal peptide (VIP)-like immunoreactivity is present at low levels in the superior cervical ganglion of the adult rat, where immunostained neural processes, but only an occasional immunostained cell body, are found. However, when ganglia are maintained for 24 or 48 hr in organ culture, their content of VIP-like immunoreactivity increases 6- or 31-fold, respectively. When examined at 24 hr, the increase in VIP-like immunoreactivity is totally blocked by an inhibitor of RNA or protein synthesis. Many neuronal cell bodies and processes with immunoreactivity for VIP and the related peptide histidine isoleucine amide (PHI) are seen in cultured ganglia. In addition, VIP/PHI mRNA is abundant in cultured ganglia but only barely detectable in ganglia prior to culture. Under the same culture conditions, neuropeptide Y-like immunoreactivity increases to a small extent, and tyrosine hydroxylase activity and total ganglion protein remain unchanged. These results support the idea that adult sympathetic neurons exhibit plasticity in neuropeptide expression and that this plasticity, in the case of VIP, depends on changes in gene expression.
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PMID:Phenotypic plasticity in adult sympathetic neurons: changes in neuropeptide expression in organ culture. 174 5

Vasoactive intestinal peptide immunoreactive (VIP-IR) nerve fibres and terminals, neurons and small granule containing cells were observed in human lumbal sympathetic ganglia. Electron-microscopically VIP-IR was localized in the large dense-cored vesicles in nerve terminals and on the membranes of the Golgi complexes in the neurons. A small population of principal ganglion cells was surrounded by VIP-IR nerve terminals. Most of these neurons contained acetylcholinesterase (AChE) enzyme but were not tyrosine hydroxylase-immunoreactive (TH-IR). All VIP-IR ganglion cells and most of the nerve fibres contained AChE but not TH-IR. It appears that in human sympathetic ganglia VIP is localized in the cholinergic neurons and nerve fibres and that the VIP-IR nerve terminals innervate mainly the cholinergic subpopulation of the sympathetic neurons.
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PMID:Vasoactive intestinal peptide (VIP)-like immunoreactivity in the human sympathetic ganglia. 256 93

Vasoactive intestinal peptide (VIP) acutely increases tyrosine hydroxylase (TH) activity in cultures of dispersed normal adult rat chromaffin cells and of PC12 rat pheochromocytoma cells. High concentrations of VIP (10 microM) produce about 3-fold increases in TH activity in both cell types. VIP also increases the content of cyclic adenosine 3':5'-monophosphate (cAMP) in PC12 cells. VIP may increase TH activity by promoting the cAMP-dependent phosphorylation of the enzyme. Nerve fibers containing VIP-like immunoreactive material have been reported in the adrenal medulla and in other catecholamine (CA)- storing tissues. This VIPergic innervation may regulate CA synthesis and other cAMP-dependent processes in these tissues.
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PMID:Vasoactive intestinal peptide increases tyrosine hydroxylase activity in normal and neoplastic rat chromaffin cell cultures. 286 99

Peptide, 5-hydroxytryptamine (5-HT)-, tyrosine hydroxylase (TOH)-, and glial fibrillary acidic protein (GFAP)-like immunoreactivity was studied in the optic tectum of Rana pipiens. Peroxidase-antiperoxidase and indirect immunofluorescence single- and double-labeling methods were used to compare differential laminar distribution of each of these substances. Substance P (SP), leucine-enkephalin (LENK), cholecystokinin octapeptide (CCK8), bombesin (BOM), avian pancreatic polypeptide (APP), and possibly neurotensin display unique individual patterns of laminar distribution of processes and cell bodies throughout the tectum. A correlative analysis of the topographical distribution of SP, LENK, BOM, and APP on the basis of double-labeled sections shows a precise laminar segregation of these substances. Vasoactive intestinal peptide-, beta-endorphin-, and ranatensinlike immunoreactivity is consistently absent from our material. 5HT- and TOH-like immunoreactivity discloses a reticular array of fibers without clear evidence of laminar organization. This peptide-like laminar organization is particularly elaborate throughout the superficial neuropil of the optic tectum, the major retinorecipient zone. The pattern of lamination demonstrated in the present study differs in several important features from that previously described on the basis of several histological methods. The cells of origin of processes (axons and/or dendrites) in the superficial tectal neuropil may be either intrinsic or extrinsic to the tectum. Special reference is made to conflicting evidence regarding the possibility of a retinal contribution to peptide-like tectal lamination.
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PMID:Laminar organization of peptide-like immunoreactivity in the anuran optic tectum. 619 80

Secretin is a 27-amino acid neuroendocrine peptide that stimulates fluid and electrolyte secretion in the gastrointestinal tract, activates tyrosine hydroxylase activity in the central nervous system, and affects cardiac and renal function. Specific receptors for secretin have been previously characterized on neuroblastoma cells, pancreatic acini, gastric glands, and liver cholangiocytes. We report here the isolation of a 1616-base pair cDNA from human lung tissue that encodes a 440-amino acid, 50-kDa, G protein-coupled human secretin receptor (HSR), with homology of 80% with the rat secretin receptor and 37% with the human type I vasoactive intestinal peptide receptor. Northern blot analysis of human tissue mRNA revealed that the relative intensity for expression of a 2.1-kilobase HSR transcript was pancreas > kidney > small intestine > lung > liver, with trace levels in brain, heart, and ovary. Stable transfectants of HSR in human embryonic kidney 293 cells, termed 293S12, expressed 10(5) binding sites/cell for 125I-secretin, with an apparent Kd of 3.2 nM. Vasoactive intestinal peptide, pituitary adenylyl cyclase-activating peptide-38, and glucagon were less potent (by 3 orders of magnitude) than secretin in competitively inhibiting 125I-secretin binding to 293S12 cells. Secretin evoked concurrent dose-dependent increases in intracellular cAMP and calcium levels in 293S12 cells and stimulated a 4-fold increase in phosphatidylinositol hydrolysis. Thus, the HSR expressed by stable transfectants can couple to two distinct intracellular signaling pathways.
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PMID:Molecular cloning and expression of a human secretin receptor. 770 Feb 44

Vasoactive intestinal peptide (VIP) is widely recognized as a regulator of tyrosine hydroxylase via a mechanism of trans-synaptic activation. Subsets of adrenal medullary cells and postganglionic sympathetic nerves coexpress the peptide neurotransmitter neuropeptide Y (NPY) with catecholamines. Using PC12 cells transiently expressing a fusion gene in which the bacterial enzyme chloramphenicol acetyltransferase (CAT) is under the control of 700 base pairs of the 5' flanking region of the NPY gene, we have studied the role of VIP and the related peptide pituitary adenylate cyclase activating peptide (PACAP) in regulating NPY gene transcription. Both VIP and PACAP stimulated expression of the NPY gene through activation of cAMP-dependent protein kinase. PACAP was 1000-fold more potent in eliciting this response compared to VIP and activity resided in its N-terminal 27 amino acids. Both VIP and PACAP caused a subpopulation (approximately 50%) of PC12 cells to undergo profound morphological changes in that the cells extended long, slender neurites with prominent growth cones. This change in morphology was unaffected by preincubating cells with inhibitors of either cAMP-dependent protein kinase or calcium/phospholipid-dependent protein kinase. A trophic role for either VIP or PACAP in regulating sympathetic nerve function is proposed.
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PMID:Vasoactive intestinal peptide stimulates neuropeptide Y gene expression and causes neurite extension in PC12 cells through independent mechanisms. 796 4

Electrical stimulation of the preganglionic fibers innervating the rat superior cervical ganglion (SCG) produces both short-term and long-term increases in tyrosine hydroxylase (TH) activity that are not completely blocked by nicotinic antagonists. Vasoactive intestinal peptide (VIP) and secretin, two neuropeptides known to produce short-term increases in TH activity, were examined for their ability to produce long-term increases in this enzyme activity. Culturing the SCG in the presence of either peptide produced a 30-50% increase in TH activity measured 2 days later. The results raise the possibility that one of these peptides or a related molecule participates in the transsynaptic induction of ganglionic TH.
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PMID:Vasoactive intestinal peptide and secretin produce long-term increases in tyrosine hydroxylase activity in the rat superior cervical ganglion. 809 67


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