Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Conditions are described for performing mitogen (Concanavalin A, Con A; lipopolysaccharide, LPS) and mixed lymphocyte reaction (MLR) cultures using serum-free medium. The effects of exogenously adding several gastrointestinal regulatory peptides (beta-endorphin, substance P, met-enkephalin, vasoactive intestinal peptide, bombesin and somatostatin) on the incorporation of 3H-methyl-thymidine was determined. It was observed that mitogen stimulation of lymph node cells with Con A was inhibited (70% of control) by vasoactive intestinal peptide (VIP) but spleen cells stimulated by LPS were insensitive to immunomodulation (98% of control). The ability of VIP to inhibit Con A induced thymidine incorporation was concentration dependent (10(-6) to 10(-18) M) and was not attributable to kinetic shifts or cell toxicity. None of the other tested neuropeptides affected Con A or LPS induced blastogenesis. MLR cultures were inhibited by VIP, beta-endorphin and somatostatin in a biphasic manner with maximal inhibition observed at 10(-8) to 10(-12) M. Both substance P and bombesin exhibited slight immunoenhancing properties at 10(-14) to 10(-18) M. Met-enkephalin was ineffective as an immunomodulator of MLR cultures. The utility of using serum-free medium in identifying neuropeptides with immunomodulatory properties are discussed.
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PMID:Gastrointestinal regulatory peptides modulate mouse lymphocyte functions under serum-free conditions in vitro. 242 44

The influence of beta-endorphin, somatostatin, substance P (SP) and vasoactive intestinal peptide (VIP) was tested on the proliferative response of peripheral blood T lymphocytes of nickel-allergic subjects to nickel sulfate. With somatostatin, 10(-6)-10(-10) M, SP, 10(-9) and VIP, 10(-7)-10(-8) M, added 1 h after nickel sulfate, there was an enhancement of the response, while a slight suppression was obtained with SP, 10(-6) M. At 3 days after nickel sulfate, beta-endorphin, 10(-6)-10(-12) M, somatostatin, 10(-7)-10(-9) M and SP, 10(-7)-10(-11) M, gave an enhancement of the response.
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PMID:Modulating effect of beta-endorphin, somatostatin, substance P and vasoactive intestinal peptide on the proliferative response of peripheral blood T lymphocytes of nickel-allergic patients to nickel sulfate. 243 Aug 96

The effect of four neuropeptides and acetylcholine on the release of leukotrienes LTC4, LTD4 and LTE4 from platelet activating factor-stimulated rat lung and ionophore A23187-stimulated guinea pig lung, as detected by the combined use of HPLC and radioimmunoassay, was studied. Both vasoactive intestinal peptide and calcitonin gene-related peptide were found to inhibit the release of leukotrienes in both preparations. This effect was most marked in platelet activating factor-stimulated rat lung, where inhibition of LTC4 release was more pronounced than either inhibition of LTD4 or LTE4 production. The effect of vasoactive intestinal peptide on LTC4 biosynthesis was dose-related in rat lung. Neither substance P nor beta-endorphin were found to inhibit leukotriene release in rat lung. Vasoactive intestinal peptide inhibition of leukotriene release is independent from its actions on the muscarinic receptor, since acetylcholine was found to have no effect in the same preparation.
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PMID:The effect of vasoactive intestinal peptide and calcitonin gene-related peptide on peptidoleukotriene release from platelet activating factor stimulated rat lungs and ionophore stimulated guinea pig lungs. 243 97

The morphological characteristics and distribution patterns of neurons immunoreactive for antisera against six biologically active peptides were examined by indirect immunofluorescence in the human brain. The peptides studied were: met-enkephalin, leu-enkephalin, substance P, somatostatin, cholecystokinin and vasoactive intestinal peptide. The tissue samples for this study were removed, dissected and placed into fixative within 4 h post-mortem. Regional differences throughout the entire neuraxis were observed in the localization of cell bodies, fibers and terminals for the various peptides. The observations reported in this article demonstrate certain distribution patterns for peptide immunoreactivities that appear to be specific to the human brain when compared to other species. These morphologic studies establish a valuable framework for the further analysis of the role of peptide-containing neuronal circuits in normal and diseased human brain.
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PMID:An immunohistochemical study of six biologically active peptides in the human brain. 243 54

The purpose of the present study was to quantify the extent to which several peptides and serotonin coexist with substance P or somatostatin in selected lumbar dorsal root ganglia of the cat. The technique for the simultaneous visualization of two antigens by immunofluorescence was used to investigate the coexistence of neuropeptides in the lumbar dorsal root ganglia of colchicine-treated cats. Perikarya immunoreactive for calcitonin gene-related peptide, galanin, leu-enkephalin, somatostatin, and substance P were visualized in both the lumbar 5 and 6 dorsal root ganglia. In contrast, no immunoreactivity was observed for adipokinetic hormone, bombesin, dynorphin A, met-enkephalin, oxytocin, tyrosine hydroxylase, thyrotropin-releasing hormone, vasopressin, vasoactive intestinal peptide, or serotonin in either ganglion examined. Substance P coexisted with calcitonin-gene-related peptide, somatostatin, and leu-enkephalin. Somatostatin was colocalized with calcitonin gene-related peptide, leu-enkephalin, and substance P but coexisted with galanin minimally. The cell area of immunoreactive perikarya was also examined. Data concerning the cross-sectional area of immunoreactive cells indicated that somatostatin-immunoreactive perikarya were generally the largest population observed (up to approximately 6,000 microns2). Somatostatin and calcitonin gene-related peptide, as well as substance P and calcitonin gene-related peptide, coexisted in populations of cell bodies that had a smaller size (less than 2,000 microns2). These results suggest that certain peptides which coexist in the dorsal root ganglia may provide histochemical markers for functional groups of primary afferent neurons.
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PMID:Lumbar dorsal root ganglia of the cat: a quantitative study of peptide immunoreactivity and cell size. 247 1

In this study, we demonstrated that the cell content and basal secretion of vasoactive intestinal peptide (VIP) in primary rat pituitary cell cultures were increased in hypothyroidism. VIP release from hypothyroid pituitary cells in vitro was stimulated by thyrotropin releasing hormone (TRH 10(-8) to 10(-6) M) and growth hormone (GH)-releasing hormone (GHRH 10(-9) to 10(-8) M) but not by corticotropin-releasing hormone or luteinizing hormone-releasing hormone in concentrations up to 10(-6) M. In the presence of anti-VIP antisera, there was a significant decrease in basal prolactin secretion from cultured hypothyroid pituitary cells (p less than 0.005) indicating that VIP exerts a tonic stimulatory effect on prolactin (PRL) secretion. The increment in PRL secretion following TRH was not affected by exposure to anti-VIP indicating that PRL release after TRH is not mediated by VIP at the pituitary level. In contrast to changes in PRL, exposure to anti-VIP had no effect on basal GH secretion, indicating that the PRL changes are hormone specific. Similarly, GHRH-induced GH release was unaffected by VIP immunoneutralization.
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PMID:Pituitary vasoactive intestinal peptide regulates prolactin secretion in the hypothyroid rat. 251 93

Previous work has shown that corticotropin releasing factor, vasoactive intestinal peptide, phorbol ester, and forskolin cause the secretion of adrenocorticotropic hormone and beta-endorphin from the AtT-20 mouse pituitary cell line. Human recombinant interleukin 1 alpha and 1 beta also stimulated adrenocorticotropic hormone and beta-endorphin secretion from AtT-20 cells in a time- and dose-related manner. The effect appeared only after pretreatment with interleukin 1 (IL-1) for at least 18 hr and was maximum at 24 hr. After pretreatment of the cells over a period of time with IL-1, the secretion induced by corticotropin releasing factor and vasoactive intestinal peptide was increased in more than an additive manner. The enhancement of corticotropin releasing factor-induced beta-endorphin release produced by IL-1 was apparent after 12 hr and reached a maximum at 24 hr. IL-1 did not affect forskolin-induced cAMP generation but enhanced the effect of forskolin on beta-endorphin secretion. This suggests that IL-1 does not induce adenylate cyclase and that forskolin causes the secretion of beta-endorphin by a mechanism independent of cAMP. IL-1 enhanced phorbol ester-induced beta-endorphin secretion. After prolonged treatment with phorbol ester (an activator of protein kinase C), the secretion induced by phorbol ester was abolished as well as the enhancement induced by IL-1. However, prolonged treatment with phorbol ester had no effect on IL-1-induced beta-endorphin secretion. These observations suggest that IL-1 enhances peptide-generated secretion of beta-endorphin by inducing protein kinase C.
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PMID:Interleukin 1 potentiates the secretion of beta-endorphin induced by secretagogues in a mouse pituitary cell line (AtT-20). 253 29

The characteristics of atrial natriuretic factor (ANF) receptors where studied in rat retinal particulate preparations. Specific 125I-ANF binding to retinal particulate preparations was greater than 90% of total binding and saturable at a density (Bmax) of 40 +/- 8 fmol/mg protein with an apparent dissociation constant (Kd) of 6.0 +/- 2.0 pM (n = 3). Apparent equilibrium conditions were established within 30 min. The Kd value of 125I-ANF binding calculated by kinetic analysis was 4.0 pM. The Bmax of 60 +/- 10 fmol/mg protein and the Kd of 5 +/- 2 pM, calculated by competition analysis, were in close agreement with the values obtained from Scatchard plots or kinetic analysis. The 125I-ANF binding to retinal particulate preparations was not inhibited by 1 microM concentration of somatostatin, vasopressin, vasoactive intestinal peptide, adrenocorticotropin, thyrotropin releasing hormone, or leu-enkephalin. The rank order of potency of the unlabelled atrial natriuretic peptides for competing with specific 125I-ANF (101-126) binding sites was rANF (92-126) greater than rANF (101-126) greater than rANF (99-126) greater than rANF (103-126) greater than Tyro-Atriopeptin I greater than hANF (105-126) greater than rANF (1-126). Similar results have been obtained in peripheral tissues and mammalian brain, indicating that central and peripheral ANF-binding sites have somewhat similar structural requirements. Affinity cross-linking of 125I-ANF to retinal particulate preparations resulted in the labelling of two sites of molecular weight 140 and 66 kDa, respectively. This demonstration of specific high-affinity ANF receptors suggests that the peptide may act as a neurotransmitter or neuromodulator in the retina.
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PMID:Identification and characterization of atrial natriuretic factor receptors in the rat retina. 254 74

Immediate hypersensitivity responses, as acute urticaria, produce a release of neuropeptides by nerve endings, which present specificity of recognition by mast cells, basophils and other target cells. We have measured vasoactive intestinal peptide (VIP), somatostatin, bombesin, neurotensin and beta-endorphin by radioimmunoassay in plasma extracts of 20 patients with acute idiopathic urticaria and of 20 healthy subjects. VIP- and beta-endorphin-like immunoreactivities were found to be significantly decreased with respect to controls (p less than 0.001 and p less than 0.01, respectively). On the contrary, somatostatin- and bombesin-like immunoreactivities were significantly increased (p less than 0.001 and p less than 0.05, respectively). These findings could be a reflection in blood of a raised release of somatostatin and bombesin by nerve endings in the urticaria process. Moreover, the decreased plasma levels of VIP- and beta-endorphin-like immunoreactivities could be explained by a raised specific metabolism of these peptides in the urticaria process.
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PMID:Plasma neuropeptide pattern in acute idiopathic urticaria. 257 76

Current investigations on the immunohistochemical occurrence and co-occurrence of biogenic polypeptides in the mammalian carotid body were reviewed and extended by our own recent findings. The family of chromogranins and related peptides in glomus cells appears to have a widespread interspecies distribution, whereas other peptides investigated occur in a species-specific pattern. Immunoreactivity to antisera against opioids, which derive from the proenkephalin sequence, appears to be present in glomus cells of the rabbit, cat, dog, and a shrew. Conversely, glomus cells of pig and guinea pig predominantly are immunoreactive to cleavage products of prodynorphin, which co-occur in some cells with substance P and met-enkephalin-arg-phe, respectively. In the rat and Callithrix jacchus, opioid immunoreactivity is present in nerve fibres but not in glomus cells. Immunoreactivity to other peptides, such as neurotensin, cholecystokinin, neuropeptide Y, and galanin, is found only in one or two particular species. Neurotensin immunolabelling occurs in beagle dog glomus cells, which are known to lack substance P. Cholecystokinin immunoreactivity is present in glomus cells of dog and Callithrix, and co-exists with chromogranin A, neuropeptide Y, and substance P. Substance P appears to exist in both carotid body glomus cells and nerve fibres. Substance P immunoreactivity is present in glomus cells of all species investigated, except dog. Coexistence of substance P and calcitonin gene-related peptide (CGRP) is demonstrated in nerve fibres of the guinea pig carotid body, which originate in the petrosal and jugular ganglia. Other peptides visualized immunohistochemically in mammalian carotid body nerve fibres are vasoactive intestinal peptide and neuropeptide Y. The functional significance of the various peptides present in the carotid body is discussed.
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PMID:Immunohistochemical distribution and colocalization of regulatory peptides in the carotid body. 267 3


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