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)

The central amygdaloid nucleus (ACe) is part of the amygdaloid complex that participates in adrenocorticotrophin secretion, stress-related reactions and behavioral functions. The ACe contains numerous glucocorticoid receptor (GR)-immunoreactive (IR) neurons, and in addition it has been shown to contain several neuropeptide-IR somata and nerve terminals. In order to study the relationship between the GR- and neuropeptide-IR structures we mapped the distribution of GR-like immunoreactivity (LI) in amygdaloid complex and colocalized the neuropeptide- and GR-LIs in the ACe. In the amygdaloid complex the central, medial and cortical nuclei contained a high number of GR-IR neurons, whereas a moderate number of GR-IR neurons were observed in the basolateral and basomedial nuclei. Only a few GR-IR neurons were seen in the lateral nucleus. In the ACe, the majority of corticotrophin-releasing factor (CRF)-, met-enkephalin (met-ENK)-, neurotensin (NT)- and somatostatin (SOM)-IR neurons contained also GR-IR. About half of the substance P (SP)-IR neurons were seen to contain GR-IR, whereas only some of the few vasoactive intestinal polypeptide and cholecystokinin-IR neurons showed GR-LI. Nerve terminals containing calcitonin gene-related peptide and the above mentioned peptides were seen in close contact with the GR-IR neurons. These results suggest that the glucocorticoids may modulate directly the neurotransmitter synthesis of the CRF-, met-ENK, NT-, SOM- and SP-IR cells in the ACe.
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PMID:Colocalization of peptide and glucocorticoid receptor immunoreactivities in rat central amygdaloid nucleus. 137 77

The effect and mode of action of vasoactive intestinal polypeptide (VIP), a peptidergic neuromodulator in the gastrointestinal nervous system, were investigated in isolated muscle strips of the guinea-pig ileum. VIP induced concentration-dependent (20 nM-1 microM) contractions of longitudinal ileal strips. TTX (1 microM), a mixture of atropine (3 microM) and spantide (30 microM), a mixture of atropine (3 microM) and omega-conotoxin GVIA (100 nM), somatostatin (60 nM) and dynorphin (100 nM) abolished the effect of VIP. In most cases a small relaxation became evident. Desensitization to substance P in the presence of atropine prevented VIP-induced contraction. A partial inhibition was observed in the presence of atropine (3 microM), spantide (30 microM), omega-conotoxin GVIA (100 nM), beta-endorphin (265 nM), met-enkephalin (1100 nM) and a mixture of spantide (30 microM) and omega-conotoxin GVIA (100 nM). The action of VIP was not significantly modified by guanethidine (3 microM) or hexamethonium (150 microM). In circular ileal strips VIP (10-300 nM) caused concentration-dependent relaxations through a direct myogenic effect. These results indicate that the VIP produced contractions of the guinea-pig ileum are exclusively neurally mediated and involve a cholinergic as well as a noncholinergic-nonadrenergic (NANC) pathway. It is concluded that besides acetylcholine (Ach) VIP releases the peptidergic transmitter substance P from postganglionic nerve fibers of myenteric plexus. Opioid peptides and somatostatin modulate the activity of cholinergic and peptidegic nerves in the guinea-pig ileum. The release of substance P appears to depend completely on N-type voltage sensitive calcium channels.
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PMID:Vasoactive intestinal polypeptide induces neurogenic contraction of guinea-pig ileum. Involvement of acetylcholine and substance P. 137 93

Carcinoid tumors of the lung in 10 patients were treated surgically and both the clinicopathological manifestations and immunohistochemistry were examined in detail. Five were central carcinoid tumors, located in the main, lobar or segmental bronchus and five were peripheral carcinoid tumors, located in the subsegmental bronchus or beyond. Histologically, eight of the tumors were typical carcinoid tumors, one was an atypical carcinoid tumor, and one a carcinoid tumorlet. Three growth types were also established: polypoid type, iceberg type and intrapulmonary type. The central carcinoid tumors belonged either to the polypoid type or iceberg type, while the peripheral carcinoid tumors were of the intrapulmonary type. Both the iceberg and intrapulmonary types may invade the peribronchial or parenchymal tissues more frequently than does the polypoid type. Immunohistochemically, argyrophilia and neuron-specific enolase (NSE) were detected in all the tumors examined and six stained for polypeptide hormones such as adrenocorticotropic hormone (ACTH) and/or pancreatic polypeptide (PP). Of these, five had epithelial markers such as keratin, epithelial membrane antigen (EMA) and/or carcino-embryonic antigen (CEA). These findings suggest that a carcinoid tumor of the lung originates from primitive multipotential stem cells such as those of a neuroendocrine or epithelial nature.
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PMID:Carcinoid tumor of the lung: clinicopathological and immunohistochemical studies. 137 25

Calcitonin gene-related polypeptide (CGRP) was purified from ovine hypothalamic extracts. Its amino acid sequence was determined as: Ser-(Cys)-Asn-Thr-Ala-Thr-(Cys)-Val-Thr-His-Arg-Leu-Ala-Gly-Leu-Leu-Ser- Arg-Ser - Gly-Gly-Val-Val-Lys-Ser-Asn-Phe-Val-Pro-Thr-Asn-Val-Gly-Ser-Gln-Ala-Phe- NH2. This sequence differs from rat CGRP by two amino acid substitutions (Ser for Asp25 and Gln for Glu35). Adenylate cyclase stimulating activity in rat pituitary cell cultures was monitored during the isolation. CGRP had adenylate cyclase stimulating activity comparable to corticotropin-releasing hormone, suggesting a hypophysiotropic role for CGRP. This is the first chemical characterization of CGRP in the brain (hypothalamus).
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PMID:Identification of calcitonin gene related peptide in ovine hypothalamic extract. 141 24

The purpose of the present experiment was to test the hypothesis that corticotropin-releasing factor (CRF), a polypeptide of 41 amino acids, when administered either intracerebroventricularly (i.c.v.) or subcutaneously (s.c.), has aversive properties in the conditioned place-preference paradigm. Five doses of CRF (0, 0.005, 0.05, 0.5, 5 micrograms) were tested. i.c.v. CRF induced a specific dose-dependent reduction of the amount of time spent in the environment previously paired with the administration of CRF. Furthermore, this CRF-induced place aversion was prevented by pretreatment with alpha-helical-CRF(9-41), a specific CRF antagonist, administered i.c.v. In order to test whether the aversive effects induced by i.c.v. CRF could result from the stimulation of the HPA axis accompanying i.c.v. CRF injection, the reinforcing properties of s.c. CRF were studied using the same dose range. Only the higher s.c. dose was effective in producing a place aversion suggesting that the aversive effects of CRF could not be due solely to the stimulation of the pituitary-adrenocortical system, measured by plasmatic levels of adrenocorticotropic hormone (ACTH) and corticosterone, because the lower doses consistently activate the pituitary-adrenocortical system without producing any behavioral changes. Altogether, these data indicate that the non-neurosecretory CRF neurons may mediate the aversive state occurring during stress.
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PMID:Corticotropin-releasing factor induces a place aversion independent of its neuroendocrine role. 147 1

CRH (corticotropin-releasing hormone) is a hypothalamic polypeptide that stimulates ACTH secretion by the anterior pituitary and, subsequently, cortisol secretion by the adrenal cortex. CRH test administration is indicated in the differential diagnosis of Cushing syndrome and in the assessment of corticotropic function in different pituitary conditions. Both human CRH (hCRH) and ovine CRH (oCRH) can be used by i.v. injection. Intrinsic ACTH-releasing activities of the two molecular forms are similar. Nevertheless, and contrary to hCRH, oCRH does not interact with the human CRH specific binding protein (CRH-BP) and the use of this ovine form could be useful in testing pituitary function while avoiding possible changes in peptide activity due to protein binding. The present study was conducted in 3 distinct groups of human volunteers to evaluated the ACTH and cortisol responses to i.v. oCRH (1 micrograms per kg body weight) at noon (oCRH test). 24 healthy, nonobese subjects, not under medication, participated in the study. The first group consisted of 8 young men, the second of 8 women of childbearing age and the third of 8 menopausal women. Tolerance to the oCRH test was excellent in all 3 groups. A significant increase in plasma ACTH and cortisol was observed in all the subjects, with peak occurrence for ACTH between 15 and 60 minutes after oCRH and between 20 and 120 minutes for cortisol. The responses were not sex-related among the young subjects, but the menopausal women displayed a higher cortisol increase than the other 2 groups.
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PMID:[Test with ovine corticotropin-releasing hormone (oCRH): clinical application and reference values in the young adult and the postmenopausal women]. 164 82

We have isolated from chicken embryos a novel 53-kDa protein possessing properties which are similar, but not identical to the 55-kDa PDI polypeptide from chicken embryos. The novel 53-kDa polypeptide copurifies with PDI, but is separated by ion-exchange chromatography. The novel 53-kDa polypeptide cross-reacts strongly with antibodies specific for bovine PDI and cross-reacts to varying degrees with six different preparations of antibodies specific for chicken PDI which is identical to the beta-subunit of chicken prolyl 4-hydroxylase. Anti-bovine PDI immunoglobulins selected by the purified 53-kDa polypeptide react with bovine PDI but not with the beta-subunit of prolyl 4-hydroxylase, suggesting that the 53-kDa polypeptide shares epitopes with bovine PDI but not with the chicken prolyl 4-hydroxylase beta-subunit. Amino acid compositional analysis of the purified polypeptide yielded unique data when compared to PDI and other PDI-like polypeptides. Edman degradation from the N terminus of the 53-kDa polypeptide yields a sequence very different from the N terminus of PDI. This sequence is unique when compared to all entries in available databases. A 20-residue sequence of an internal cyanogen bromide fragment of the 53-kDa polypeptide gives a nearly identical match with human beta-endorphin. The 53-kDa polypeptide is capable of cleaving the disulphides of insulin under conditions where PDI is active. The periodic acid-Schiff assay failed to detect bound carbohydrate. These observations support evidence for a family of PDI-like proteins in chicken embryo and suggest that PDI activity is not confined to only one protein.
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PMID:A novel 53-kDa polypeptide from chicken embryo. 166 Aug 84

Transepithelial pathways of macromolecule transport have been studied in vitro in rabbit nasal respiratory mucosa, maintained at 27 degrees C. Transepithelial electrical potential difference, short-circuit current and resistance were 3.4 +/- 0.5 mV (submucosa positive), 65.0 +/- 6.7 microA cm-2 and 52.1 +/- 5.6 omega cm-2 respectively (n = 15). These electrical characteristics are those of a leaky epithelium allowing macromolecules to permeate paracellularly. A detailed permeation study of a polypeptide (elcatonin, Mw = 3362) was also undertaken. Elcatonin mucosa-submucosa (Jms) and submucosa-mucosa (Jsm) fluxes were measured by radioimmunoassay. With 10 micrograms/ml elcatonin, Jms was significantly larger than Jsm for the whole 120-min period of observation; net flux showed a maximum in the first 30 min (Jms = 13.6 +/- 1.0 ng cm-2 h-1, Jsm = 1.4 +/- 0.1 ng cm-2 h-1, n = 10). Jms fell towards the value of Jsm if the temperature was reduced to 4 degrees C or if the mucosa was simultaneously treated with 0.1 mM dinitrophenol and 3 mM monoiodoacetate. Jms and Jnet followed saturation kinetics with increasing elcatonin concentrations. Adrenocorticotropic hormone (Mr = 4500) produced a similar pattern to elcatonin. However, Jms and Jsm were not significantly different from each other at any time either for [3H]sucrose (Mw = 342) or for [14C]polyethyleneglycol-4000 (Mw = 4000) when present in the bathing medium at 500 microM concentration. The results show active transport of polypeptides in parallel with passive permeation (possibly through leaky intercellular junctions). Active transport does not appear to be related to nonspecific pinocytosis but to receptor-mediated endocytosis.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Active transport of polypeptides in rabbit nasal mucosa: possible role in the sampling of potential antigens. 166 8

The concentrations of somatostatin (SRIF), vasoactive intestinal polypeptide (VIP), beta-endorphin (beta-EP), adrenocorticotropin (ACTH) and corticotropin-releasing factor (CRF) immunoreactivity were measured in cerebrospinal fluid (CSF) of patients with Alzheimer's disease (AD), patients with Parkinson's disease (PD) and controls. In order to study the mechanisms that regulate peptide levels in CSF and peptide interactions, correlations between CSF peptides were determined. Within all patient groups a number of significant correlations were shown to exist between CSF peptides. The correlations were apparently not coincidental, since there was no such relation between the concentrations of CSF peptides and CSF protein content. Neither age, sex, severity of dementia nor the presence of extrapyramidal signs could explain the number of significant correlations. These results indicate, that the correlations found between CSF peptides may be due to common regulatory mechanisms or general physiological behaviour of peptides in the CSF.
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PMID:A correlation study of CSF neuropeptides in Alzheimer's and Parkinson's disease. 168 48

The purpose of the present study was to determine whether neurochemicals normally found within neuron somata, fibers, and terminals of the hippocampal formation would also be present in transplanted hippocampal tissue that had developed in lesion cavities made in adult rat brains by aspiration of the hippocampus and overlying dorsolateral neocortex. Embryonic Day 15 or 16 rat brian tissue containing hippocampus with some medial pallial anlage was transplanted into the site of hippocampal aspiration lesions in adult male rats. One hundred ten to one hundred thirty-five days later the brains of these rats were sectioned and processed using the avidin-biotin-horseradish peroxidase immunocytochemical procedure to visualize choline acetyltransferase, met-enkephalin (MENK), neurotensin (NT), somatostatin, substance P, tyrosine hydroxylase (TH), or vasoactive intestinal polypeptide. Sections from two brains were stained using the thiocholine technique for visualization of acetylcholinesterase. All of these substances were found within cell bodies and/or fibers in the transplants. However, several abnormalities were noted. In addition to TH-immunoreactive fibers, TH-immunoreactive cell bodies were found in the transplants. Since TH is not expressed in mature hippocampal or cortical neurons this suggests that mechanisms for suppression of manufacture of this enzyme are lacking or inhibited in the transplants. Further, although all of the peptides were present either in fibers or in both cell bodies and fibers, the density of staining for NT and MENK was less than would be expected for normal hippocampus, and none of the cell bodies or fibers reacting for the peptides exhibited any apparent organization resembling that normally observed in hippocampus or cortex. However, some histological organization was present and the cholinergic markers were associated with this organization. These data suggest that some tropic and/or trophic factor such as nerve growth factor is present in the transplants to guide cholinergic innervation.
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PMID:Neurochemical anatomy of fetal hippocampus transplanted into large lesion cavities made in the adult rat brain. 170 34


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