Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To determine whether a previously reported effect of vasopressin on blood-brain transfer of leucine extends to other large neutral amino acids, we measured the regional blood-brain transfer of L-phenylalanine with the integral technique. Intravenous co-injection of L-phenylalanine and arginine vasopressin (30 nmol to 10 pmol) resulted in a decrease of the permeability-surface area (PaS) product of phenylalanine of between 11 and 39%. In addition, the peptide elicited a decrease of the cerebral blood flow of between 11 and 56% combined with a drastic decrease of the cardiac output (32-64%) and an elevation of the blood pressure to approximately 150% of control values. However, we found no changes of the cardiac output, the blood pressure, or the PaS product of phenylalanine after microdialysis (30 min, 5 microliters min-1) of arginine vasopressin (15 mumol L-1) into the dorsal hippocampus, but cerebral blood flow was decreased. The results support the hypothesis that arginine vasopressin receptors at the blood-brain barrier are involved in the regulation of large neutral amino acid transfer from blood to brain and indicate that these receptors are located at the luminal membrane of the endothelial cells.
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PMID:Blood-brain transfer of L-phenylalanine declines after peripheral but not central nervous administration of vasopressin. 223 Aug 11

Normal mammalian lungs, including human fetal lungs, contain significant amounts of a decapeptide which releases arginine-vasopressin from the neurophypophysis and therefore has antidiuretic activity. The rat peptide is: Tyr-Gly-Glu-Pro-Lys-Leu-Asp-Ala-Gly-Val-NH2. The peptide from human fetal lungs has Ala instead of Tyr. It may be a normal regulatory substance and its role in the pathogenesis of the syndrome of inappropriate antidiuresis associated with lung diseases merits investigation. In view of its source and action, the antidiuretic lung peptide may be called Pneumadin.
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PMID:Pneumadin: a new lung peptide which triggers antidiuresis. 227 81

Phe-Leu-Phe-Gln-Pro-Gln-Arg-Phe-NH2 (F-8-F-NH2), isolated from bovine brain, is an FMRF-NH2-like peptide with morphine-modulating activity. In the rat, F-8-F-NH2 immunoreactivity (IR) is highly localized in the neurohypophysis. In this study, F-8-F-NH2-IR was studied in the hypothalamo-neurohypophyseal system of an Arg8-vasopressin (AVP)-deficient animal, the Brattleboro (DI) rat, and the normal control Long-Evans (LE) strain. F-8-F-NH2-IR in the DI pituitary is below the level of detection in contrast to that in the LE (0.50 +/- 0.04 pmol/gland). Neuropeptide Y (NPY) levels are increased two-fold in the DI pituitary while AVP levels are below detection. The content of F-8-F-NH2-IR in the hypothalami and spinal cords of DI and LE rats is not statistically different, suggesting that the absence of F-8-F-NH2-IR in the Brattleboro pituitary is not due to a genetic defect in F-8-F-NH2 biosynthesis. The results of this study raise the question whether AVP could be involved in the regulation of F-8-F-NH2 immunoreactivity in the neurohypophysis.
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PMID:FMRF-NH2-like peptide is deficient in the pituitary gland of the Brattleboro rat. 235 58

The distribution of leucine-enkephalin, methionine-enkephalin, neurotensin, somatostatin, substance P, oxytocin, vasopressin, neurophysin II, and serotonin in nerve terminals and fibers of sympathetic autonomic areas of the thoracolumbar (T-L) spinal cord was studied immunohistochemically in cats. Densities of these immunoreactive terminals and fibers were estimated in the intermediolateral nucleus pars principalis (IMLp) and pars funicularis (IMLf), the nucleus intercalatus (IC), and the central autonomic area (CA). Results for leucine- and methionine-enkephalin-like immunoreactivity (ENK) were similar and immunoreactivity for vasopressin was not observed. The greatest numbers of terminals and fibers in the IMLp region contained ENK, neurotensin-(NT), and serotonin-like immunoreactivity (5HT); terminals and fibers containing substance P-(SP) and neurophysin II-like immunoreactivity (NP2) were intermediate in number, and those containing somatostatin-(SS) and oxytocin-like immunoreactivity (OXY) were generally sparse. In the IC and CA, terminals and fibers containing ENK and NT were dense, those containing SP were moderate, and those containing OXY, NP2, and 5HT were sparsely represented. In the IMLp, where the largest proportion of sympathetic preganglionic neurons (SPN) is found, the greatest concentration of terminals and fibers containing ENK was found in segments T1-T8; for NT these segments were T1-T5 and T11-L1, for SP-C8-T2 and T11-L1, for NP2-T4-T7 and L2 to L3, and for 5HT-T1-T5. Terminals and fibers containing SS and OXY were present in segments C8-T10 and segments C8, T2-T8, T13, and L2 to L3, respectively. These results indicate that while ENK, NT, SP, NP2, and 5HT fibers and terminals are widely distributed throughout the T-L cord, they may influence to a greater degree the SPN in segments where they are present in greater numbers. As SS and OXY were not found at all levels of the IMLp, their functions may be more organ specific.
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PMID:Segmental distribution of peptide- and 5HT-like immunoreactivity in nerve terminals and fibers of the thoracolumbar sympathetic nuclei of the cat. 241 41

The distribution of leucine-enkephalin, methionine-enkephalin, neurotensin, somatostatin, substance P, oxytocin, vasopressin, and neurophysin II in cell bodies of sympathetic autonomic nuclei of the thoracolumbar (T-L) spinal cord was studied immunohistochemically in cats after intrathecal administration of colchicine. Neurons containing only enkephalin-, neurotensin-, somatostatin-, and substance P-like immunoreactivity (ENK, NT, SS, SP, respectively) were found in the intermediolateral nucleus pars principalis (IMLp) and pars funicularis (IMLf), the nucleus intercalatus (IC), and the central autonomic area (CA). The size, shape, location, and numbers of the peptide-positive neurons in the IMLp, IMLf, and IC suggested that they were sympathetic preganglionic neurons (SPN). This was confirmed by a combined retrograde tracing/immunohistochemical study showing that most of these neurons at the levels of the T-L cord known to provide preganglionic fibers to the stellate ganglion were SPN. On the other hand, the functional identification of the neurons in the CA is uncertain as neurons were not observed which were both retrogradely labelled and contained ENK, NT, SS, or SP. Immunoreactive neurons in each area were counted in ten sections from each segment from C8 to L4. In the IMLp, the SPN with ENK were greatest in number (up to 25) in segments T4-T7 and L2-L3. The maximum number of SPN containing NT was found in segments T4-T7 (45 neurons). Of the four peptides, neurons containing SS were found in the greatest number (up to 48 in segments T2-T6); neurons containing SP were found in the smallest number (15 or fewer per segment). Few SPN containing each of the four peptides were found in the IC; CA neurons with ENK and NT were also few in number. A comparison of the numbers of immunoreactive neurons in the IML with earlier estimates for the total numbers of SPN in the IML at each level showed that the proportions of IML neurons containing each of the four peptides were fairly consistent throughout the T-L cord, with some exceptions. These results suggest that the innervation of visceral organs is not obviously peptide-specific, although some organs may be innervated by a greater proportion of SPN containing one of these peptides. Finally, the presence of ENK, NT, SS, and SP in SPN suggests that these four peptides act as neurotransmitters in preganglionic pathways to sympathetic ganglia.
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PMID:Segmental distribution of peptide-like immunoreactivity in cell bodies of the thoracolumbar sympathetic nuclei of the cat. 241 42

The medial preoptic nucleus (MPN) is a sexually dimorphic complex with three major subdivisions. The cell-dense central (MPNc) and medial (MPNm) subdivisions are larger in male rats, while the cell-sparse lateral subdivision (MPNl) occupies a majority of the nucleus in females. In the present study we evaluated the distribution of possible monoaminergic and peptidergic cells and fibers within the MPN, as well as in adjacent regions of the medial preoptic area of the adult male rat. For this, we used an indirect immunohistochemical method with antisera to serotonin (5HT), dopamine beta-hydroxylase (DBH), tyrosine hydroxylase (TH), neuropeptide Y (NPY), cholecystokinin (CCK), vasoactive intestinal polypeptide (VIP), substance P (SP), neurotensin (NT), corticotropin-releasing factor (CRF), luteotropin-releasing hormone (LRH), somatostatin (SS), thyrotropin-releasing hormone (TRH), oxytocin (OXY), vasopressin (VAS), adrenocorticotropic hormone (1-24; ACTH), alpha-melanocyte-stimulating hormone (alpha-MSH), leucine-enkephalin (L-ENK), and calcitonin gene-related peptide (CGRP). The results suggest that cell bodies and/or fibers crossreacting with all of these putative neurotransmitters are differentially distributed within the MPN. Within the MPNm, the densest plexuses of fibers were stained with antisera to SP and NPY, while moderate densities of fibers were stained with anti-DBH, SS, CCK, CGRP, ACTH, and alpha-MSH, and only a few fibers were stained with anti-5HT, TH, NT, VAS, and L-ENK. Moderate numbers of SP- and L-ENK-immunoreactive cell bodies, and a few SS-, NT-, CRF-, and TRH-stained cell bodies were also found within the MPNm. The MPNc contained a dense plexus of CCK-immunoreactive fibers, as well as a few CRF-immunoreactive fibers. Both fiber types were localized almost exclusively to this subdivision, while most of the others studied here appeared to avoid it selectively. This suggests that there are relatively few inputs to the MPNc, and that they tend to avoid other parts of the nucleus, although moderate densities of DBH- and NPY-immunoreactive fibers were found in both the MPNm and MPNc. The MPNc contained several CCK-immunoreactive cell bodies as well as a moderate number of TRH-stained cell bodies. Both cell types were nearly completely localized to the MPNc. The major inputs to the MPNl studied here appear to be stained with antisera to 5HT and L-ENK, although moderate numbers of NT- and CRF- immunoreactive fibers were also found in this part of the nucleus.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Neurotransmitter specificity of cells and fibers in the medial preoptic nucleus: an immunohistochemical study in the rat. 242 28

Ecdysteroid-producing Y-organs from the crab Cancer antennarius were shown to possess enzyme activity that was stimulated in vitro by addition of Ca2+, phosphatidylserine, or the protein kinase C activator, phorbol 12-myristate 13-acetate (PMA; ED50, 4 nM). In the presence of calcium and phosphatidylserine, PMA increased protein kinase C activity dose-dependently to a maximum 4-fold increase at 100 nM PMA. Stimulated protein kinase C activity was unaffected by calmodulin (100 nM) but was inhibited by 100 nM trifluoperazine. Pretreatment of cultured Y-organ segments with PMA elevated basal protein kinase C activity, whereas molt-inhibiting hormone (MIH) and calcium ionophore A23187 did not affect activity. PMA (1-100 nM) increased Y-organ steroidogenesis dose-dependently and alleviated suppression due to MIH or lysine vasopressin; PMA effects on steroidogenesis became evident after 2 h of incubation. Another phorbol activator of protein kinase C (phorbol 12, 13-dibutyrate) and a permeable synthetic diacylglycerol (1-oleoyl-2-acetyl-glycerol) stimulated ecdysteroidogenesis while an inactive phorbol (4 alpha-phorbol 12,13-didecanoate) and diolein were ineffective. The inhibitory effects on steroidogenesis of cholera toxin, forskolin, dibutyryl cAMP, and 3-isobutyl-1-methylxanthine were countered by PMA, but PMA did not alter basal or peptide hormone-stimulated Y-organ cAMP levels. Stimulatory effects on steroidogenesis of PMA and of A23187 were not additive, and PMA did not alter inhibition caused by lanthanum (calcium channel blocker) or trifluoperazine (calmodulin inhibitor). PMA increased the incorporation of [3H]leucine into Y-organ protein by 112%, and countered the suppressive effect of MIH on protein synthesis; PMA did not affect RNA synthesis. When Y-organs were suppressed with cycloheximide, PMA was unable to stimulate steroidogenesis. Actinomycin D alone had no effect on steroidogenesis but prevented stimulation by PMA. The results indicate that Y-organs contain protein kinase C activity which stimulates ecdysteroid production and protein synthesis by a mechanism not directly interactive with the cAMP or Ca2+-calmodulin systems.
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PMID:Demonstration of protein kinase C activity in crustacean Y-organs, and partial definition of its role in regulation of ecdysteroidogenesis. 243 89

High-affinity binding sites for endothelin have been found in a human placenta membrane preparation. 125I-endothelin bound to placenta membranes at 20 degrees C with an association half-time of 30 min, whereas the binding was only slowly reversed with a dissociation half-time of 250 min. In saturation experiments, a single class of high-affinity binding sites was identified with an apparent dissociation constant (KD) of 24 pM and a maximal density of 240 fmol per mg of protein. The binding of 125I-endothelin was half-maximally inhibited by cold endothelin at a concentration (IC50) of 140 pM. In contrast, no inhibition was found at 10(-4) M for a variety of vasoactive peptides such as angiotensin II, vasopressin, neuropeptide Y, substance P, CGRP, bradykinin, leucine enkephalin or dynorphin A. Similarly, the binding was modulated neither by the calcium channel blockers nifedipine, verapamil or diltiazem, nor by the calcium channel agonist Bay k 8644. There was also no effect with the structurally-related bee venom apamin. Using this membrane preparation, endothelin-like activity could be measured in the medium of cultured human endothelial cells by competition binding technique.
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PMID:Specific receptors for endothelin on membranes from human placenta. Characterization and use in a binding assay. 254 8

Everted sacs of the rat jejunum change the accumulation of [3H]leucine when beta-casomorphins (BCMs) or synthetic analogs, in a concentration range of 10(-8) mol/l, are coincubated with the amino acid. BCM5 (BCM fragment 1-5, Tyr-Pro-Phe-Pro-Gly) and [D-Ala2]-BCM5-NH2 (Tyr-D-Ala-Phe-Pro-Gly) increase, whereas [D-Pro4]-BCM5 (Tyr-Pro-Phe-D-Pro-Gly) decreases the leucine accumulation and [Arg8]-vasopressin has no effect. No effect of BCM5 could be observed on the accumulation of the space marker [14C]inulin. Specific binding sites for casomorphins were detected microautoradiographically, exclusively at the epithelial cell layer using [3H][D-Pro4]-BCM5 in competition studies as a model. HPLC analysis revealed that under the experimental conditions about 50% of the studied [D-Pro4]-BCM5 was enzymatically degraded and no intact peptide is accumulated within the samples of everted sacs. From the results we postulate a brush-border receptor contact of the BCMs which induces an alteration of the amino acid uptake. A contraluminal binding of the chemical signals is not likely, because there is no evidence for a transepithelial transport of intact BCMs. The observed effects of the BCMs demonstrate as yet unknown peptide-receptor interactions, probably at the brush-border membrane, with subsequent effects on the nutrient supply. Furthermore, the results support the general hypothesis of distinct peptide-receptor interactions in those types of epithelia in which the cells are connected by tight junctions.
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PMID:beta-Casomorphins alter the intestinal accumulation of L-leucine. 254 74

Several neuropeptides were immunohistologically studied in normal human spinal cords. Substance P, methionine-enkephalin, leucine-enkephalin, and cholecystokinin positive fibers were found in all cytoarchitectonic layers, with a specific distribution pattern for each peptide. Somatostatin, oxytocin, and vasopressin immunoreactivities were restricted to particular spinal layers. Perikarya and proximal dendrites were visualized and classified by comparison with previous Golgi analyses. Substance P was contained in "radiate cells" of layer III, methionine-enkephalin in marginal neurons as well as in layer II "stellate cells," and somatostatin in layer II "islet cells." Several results differed from those reported in other species. Chemical neuroanatomy may provide new insights into the neuronal organization of the human spinal cord.
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PMID:Substance P, enkephalins, somatostatin, cholecystokinin, oxytocin, and vasopressin in human spinal cord. 258 9


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