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)

A 1 h immobilization stress (IS) was imposed to rats at the beginning of the dark period, i.e., when the animals start to be active. The IS was accompanied by an intense polygraphic waking and followed, over 12 h of the dark period, by a significant rebound of slow-wave sleep (SWS, +17%) and paradoxical sleep (PS, +57%). In order to estimate the IS-related changes in the endogenous concentrations of corticotropin-like intermediate lobe peptide (CLIP, ACTH18-39) and related compounds, a specific radioimmunoassay (RIA) was used. Assays performed in cerebral biopsies taken from arcuate (AN) and raphe dorsalis (nRD) nuclei led to the obtention of 2 main immunoreactive peaks, corresponding to CLIP and its phosphorylated form Ph-CLIP. Just after end of the IS and within the nRD. Ph-CLIP immunoreactivity increased by about 95%. Four hours later, i.e., when PS rebound was maximal, a 37% increase in Ph-CLIP immunoreactivity was measured in the AN. These observations have never been described before. In the blood, at the end of the restraint, CLIP/ACTH1-39 total immunoreactivity was increased by 330%. It returned to baseline level 4 h later. Blood concentration of corticosterone was also increased by 56% at the end of the IS and was close to baseline level 4 h later. Data reported here indicate that the IS first triggers an increase in Ph-CLIP within the nRD. Since the nRD contains sleep permissive components, this increase might be determinant for the SWS and PS rebound induction. The changes observed in the blood as regards CLIP/ACTH1-39 total immunoreactivity and corticosterone concentration testify to the efficacy of the IS and are part of the conventional picture accompanying such a situation. Finally, the increase in Ph-CLIP, occurring in the AN 4 h after the end of the restraint, might be part of the restorative processes necessary to compensate the stress overshoot.
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PMID:Influence of a 1 h immobilization stress on sleep states and corticotropin-like intermediate lobe peptide (CLIP or ACTH18-39, Ph-ACTH18-39) brain contents in the rat. 909 68

Substances acting upon rapid eye movement (REM) sleep or paradoxical sleep (PS) can affect the number and/or the duration of PS episodes. In the present study, we investigated the effects of the proopiomelanocortin-derived peptide CLIP (corticotropin-like intermediate lobe peptide, ACTH 18-39) and its N-terminal fragments ACTH 18-24 and ACTH 20-24 on the duration of PS episodes in rats. Intracerebroventricular injection of ACTH 20-24 caused a pronounced prolongation of PS episodes (up to 7 min duration, never seen under baseline conditions), whereas ACTH 18-24 acted in a similar way but without reaching statistical significance. We suggest that short N-terminal CLIP fragment(s) may represent endogenous hypnogenic factor(s) involved in the regulation of paradoxical sleep.
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PMID:Effects of the CLIP fragment ACTH 20-24 on the duration of REM sleep episodes. 957 36

Mytilus edulis hemolymph contains mammalian-like proopiomelanocortin (POMC). The 20 kDa protein was purified by high pressure gel permeation chromatography, anti-adrenocorticotropin (ACTH)-affinity column and reverse-phase HPLC. The amino acid sequence determination was by Edman degradation, enzymatic treatments and Western blot analysis. Of the six peptides found in this opioid precursor, methionine-enkephalin, gamma-melanocyte stimulating hormone (MSH), alpha-MSH and ACTH exhibited 100, 80, 85 and 74% sequence identity, respectively, with the mammalian counterparts. beta-Endorphin and gamma-LPH exhibited only 25 and 10% sequence identity. Dibasic amino acid residues were found at the C-terminus of MSH and ACTH, indicating cleavage sites. The alpha-MSH is flanked at the C-terminus by Gly-Lys-Lys, representing an amidation signal. ACTH and CLIP (80% sequence identity) are also C-terminally flanked by dibasic amino acid residues. Furthermore, morphine, in a dose-dependent manner, increased the hemolymph levels of alpha-MSH and ACTH (1-39) in a naloxone and phosphoramidon antagonizable manner, indicating a neutral endopeptidase (24.11; NEP) mediated cleavage. Lipopolysaccharide (10 microg/animal) stimulated the processing of ACTH (1-39) yielding ACTH (1-24) in a cleavage that is independent of NEP, but dependent on aspartyl proteases, demonstrating differential enzymatic cleavage of ACTH (1-39). Taken together, POMC is present in invertebrates and its processing can be altered depending on the signal.
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PMID:Mytilus edulis hemolymph contains pro-opiomelanocortin: LPS and morphine stimulate differential processing. 987 18

We have previously shown that the melanotrope population of the pituitary intermediate lobe of Rana ridibunda is composed of two subpopulations, of low (LD) and high density (HD), that show distinct ultrastructural features and display different synthetic and secretory rates. To investigate whether LD and HD melanotrope cells also differ in proopiomelanocortin (POMC) processing, we have analyzed the POMC-end products in single cells from both subpopulations by means of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). The mass spectra revealed the presence of 8 POMC-derived peptides in HD and LD melanotrope cells, indicating a similar processing of the precursor in both subpopulations. However, the relative abundance of three POMC-end products (i.e. lys-gamma1-MSH, acetyl-alpha-MSH, and CLIP fragment) was higher in the HD subset. Moreover, two peptides with molecular weights of 1030 and 1818 Da, respectively, were detected that could not be assigned to any product deduced from the frog POMC sequence. The relative amount of the 1030 Da peptide was higher in LD melanotrope cells. Taken together, our results suggest that POMC processing is differentially regulated in the two melanotrope cell subsets.
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PMID:Analysis by mass spectrometry of POMC-derived peptides in amphibian melanotrope subpopulations. 1020 41

The proopiomelanocortin (POMC) gene, which encodes the common precursor for MSH-related and beta-endorphin-related end products, appeared early in chordate evolution and features a variety of lineage-specific modifications. Key among these has been the apparent degeneration and subsequent deletion of the gamma-MSH region during the evolution of POMC in the ray-finned fish. A second area of increasing focus has been the role of gene duplication in the evolution of POMC in particular and the opioid/orphanin gene family in general. The cloning and phylogenetic analysis of two POMC cDNAs from the paddlefish (Polyodon spathula) is reported here and biochemical data on their processed end products are presented. Based on conceptual amino acid translations, the paddlefish cDNAs encode all functional domains and, in most cases, the flanking paired-basic amino acid cleavage sites characteristic of gnathostome POMCs (i.e., signal sequence, gamma-MSH-like region, ACTH (alpha-MSH and CLIP), gamma-LPH, beta-MSH, and beta-endorphin). Phylogenetic analysis of the paddlefish POMC sequences in the context of the duplicated POMCs of sturgeon and salmonids suggests that degeneration of the gamma-MSH core sequence and its amino-terminal proteolytic cleavage site was initiated prior to divergence of the sturgeon and paddlefish lineages over 150 mya. Finally, a comparison of the relative rates of evolutionary divergence between paralogously related POMC genes within chondrostean and salmonid lineages provides potential support for the hypothesis that some taxa (e.g., the Chondrosteii) represent relic species as a result of an exceptionally slow rate of evolutionary change.
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PMID:Duplication of the POMC gene in the paddlefish (Polyodon spathula): analysis of gamma-MSH, ACTH, and beta-endorphin regions of ray-finned fish POMC. 1056 47

Basal sleep amounts in adrenalectomized rats (AdX), as compared to intact animals, exhibit a significant increase in slow-wave sleep (SWS), a tendency towards an increase in paradoxical sleep (PS), and circadian rhythms (SWS and PS) flattened in amplitude. An immobilization stress (IS) of 1 h, imposed on AdX rats at the beginning of the dark period, is accompanied by an intense polygraphic waking. Just after the IS, SWS amount become significantly higher than in control rats (+44%/11 h of darkness) whereas significant increases of PS occur only 5-10 h after the IS (+24%/11 h of darkness). A specific radioimmunoassay for CLIP (corticotropin-like intermediate lobe peptide or ACTH(18-39)) was performed in biopsies taken either from the nucleus raphe dorsalis (nRD) or the arcuate nucleus (AN). In the nRD, just after the IS, phosphorylated CLIP (Ph-CLIP) concentration exhibits a decreasing tendency, but 4 h later, it increases significantly (+22%, p<0.05). In the AN, Ph-CLIP concentration remains unchanged after the IS as well as 4 h later. These results differ from those previously reported in intact animals also submitted to a 1-h IS, that is, a SWS rebound less marked (+27%/11 h of darkness), a PS rebound more important starting immediately after the IS (+46%/11 h of darkness) and a significant increase in Ph-CLIP occurring just after the end of the restraint. In conclusion, data obtained after a restraint stress either in AdX or in control rats point out the dependence of the PS rebound on the nRD Ph-CLIP concentration.
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PMID:Influence of a 1-h immobilization stress on sleep and CLIP (ACTH(18-39)) brain contents in adrenalectomized rats. 1064 Jun 30

Our previous study on the distribution of adrenocorticotropin (ACTH)-like substances in the neural complex (cerebral ganglion, dorsal strand, and neural gland) of an ascidian Halocynthia roretzi revealed that some of the cells in the cerebral ganglion and the cells scattered along the dorsal strand were immunopositive with antiserum against ACTH. In order to ascertain whether these cells are equipped with prohormone convertases, we performed immunohistochemical studies on the neural complex by using antisera against PC1 and PC2. A considerable number of cells around the dorsal strand and a few cells in the neural ganglion were immunopositive with PC1 and/or PC2 antibodies. Immunoelectron microscopic study demonstrated that some granulated cells situated in the cerebral ganglion and along the dorsal strand contained PC1- or PC2-like substances within their secretory granules. Western blot analysis revealed the presence of 66-kDa PC1-like and 70-kDa PC2-like substances in the neural complex. Moreover, immunostaining of consecutive sections showed that the majority of the cells containing PC1- and/or PC2-like substances corresponded to the cells immunoreactive with antisera against ACTH and CLIP but not to those immunoreactive with an antiserum against PRL. Cells belonging to the neural gland neither contained electron-dense granules nor showed immunoreactivity with any antisera employed in this experiment. The possibility that some of the cells situated in the cerebral ganglion and along the dorsal strand are progenitors of vertebrate adenohypophyseal cells is discussed.
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PMID:Occurrence of prohormone convertase-like substances in the neural complex cells of the ascidian Halocynthia roretzi. 1262 Feb 44

Proopiomelanocortin (POMC) cDNA was cloned from sea bass (Dicentrarchus labrax) pituitary gland. A 743 nucleotide sequence was obtained coding for the following sequences flanked by sets of proteolytic cleavage sites: ACTH (Ser(88)-Met(127)), alpha-MSH (Ser(88)-Gly(102)), CLIP (Pro(106)-Met(127)), beta-LPH (Glu(131)-Gln(208)), gamma-LPH (Glu(131)-Ser(175)), beta-MSH (Asp(159)-Ser(175)), and beta-endorphin (Tyr(178)-Gln(208)). No region homologous to gamma-MSH/joining peptide (a tetrapod POMC feature) was found. Amino acid sequence identity was high with other teleostean species considered (tilapia: 73%) and lower with elasmobranchs (dogfish: 42%). However, the presumed biologically active peptides were highly conserved within all species considered: alpha-MSH (93-100%), ACTH (80-95%) and beta-endorphin (54-90%). Real-time PCR allowed us to quantify the expression of the POMC in different tIssues of the sea bass: pituitary gland, liver, gonad and head kidney. No significant POMC expression was found in the integument. In pituitary gland, gonads, head kidney and liver, POMC expression was respectively, 1.26x10(10), 2.67x10(5), 2.06x10(4) and 1.67x10(4) copies/ micro g mRNA.
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PMID:Cloning of a proopiomelanocortin cDNA from the pituitary gland of the sea bass (Dicentrarchus labrax) and assessment of mRNA expression in different tissues by means of real-time PCR. 1263 Sep 25

Channel catfish (Ictalurus punctatus) proopiomelanocortin (POMC) cDNA was cloned to investigate its structure, evolution, and expression in different tissues. POMC is an important gene in the hypothalamus-pituitary-adrenal axis, the main mediator of the stress response. POMC gene was isolated from a pituitary cDNA library and nucleotide sequence was determined. POMC cDNA is composed of 1164 nucleotides with a 639 nucleotide open reading frame encoding a protein of 212 amino acids. Catfish POMC protein contains a signal peptide (SP, Met(1)-Ala(28)), N-terminal peptide (Gln(29)-Glu(101)), adrenocorticotropic hormone (ACTH, Ser(104)-Met(142)), alpha-melanocyte stimulating hormone (alpha-MSH, Ser(104)-Val(116)), corticotropin-like intermediate lobe peptide (CLIP, Arg(121)-Met(142)), beta-lipotropin (beta-LPH, Glu(145)-His(212)), gamma-lipotropin (gamma-LPH, Glu(145)- Ser(177)), beta-MSH (Asp(161)-Ser(177)), and beta-endorphin (beta-EP, Tyr(180)-His(212)). Catfish POMC protein does not contain a gamma-MSH region and most of the joining peptide and part of the gamma-LPH are deleted. Protein sequence alignment showed the highest similarity with the carp (Cyprinus carpio) POMC I (66.5%) and POMC II (67%), while the sea lamprey (Petromyzon marinus) POC (17.9%) and POM (18.8%) were the most divergent. The average similarity was 46.95% among the 44 POMC proteins from 36 different species analyzed. Compared to the POMC mRNA levels in the pituitary, the concentration of the POMC mRNA was 0.0594% in the anterior kidney and 0.0012-0.0045% in all the other tissues except in the skin where the lowest expression (0.0005%) was observed. Overall architecture of channel catfish POMC is highly similar to those from other teleosts.
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PMID:Molecular cloning of proopiomelanocortin cDNA and multi-tissue mRNA expression in channel catfish. 1520 Oct 69

The POMC gene is perhaps the most extensively studied member of the opioid/orphanin gene family. In Phylum Chordata this gene has been characterized in representatives of every class within the Gnathostomata, as well as in one representative agnathan vertebrate, the marine lamprey. This review provides a systematic overview of trends in the evolution of the melanocortins (ACTH/alpha-MSH, beta-MSH, gamma-MSH, and delta-MSH) and beta-endorphin in gnathostomes, and advances the hypothesis that the appearance of gamma-MSH occurred early in the radiation of the gnathostomes. A summary of the extensive work on POMC genes in the marine lamprey is also provided, as well as a reevaluation of the conserved regions in the sequence of CLIP (corticotropin-like-intermediate lobe peptide) in the POMC sequences of the various groups of gnathostomes.
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PMID:Trends in the evolution of the proopiomelanocortin gene. 1586 52


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