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 effects of chronic treatment with methadone, a long-acting opiate agonist, and naltrexone, a long-acting opiate antagonist on brain immunoreactive beta-endorphin (IR-beta-EP) concentrations were studied in the rat. Male rats were treated for 30 days with either methadone, 2.5 mg/kg/day; naltrexone 2 mg/kg/day, or saline. In a repeat experiment, rats were treated for 36 days with either methadone 2.5 mg/kg/day; naltrexone 4 mg/kg/day, or saline. Brain regions were homogenized in 0.2 N HCl and assayed for IR-beta-EP by RIA. No change in the IR-beta-EP content of the hypothalamus, thalamus, midbrain, or amygdala was measured in either experiment after methadone treatment. Naltrexone, however, significantly lowered brain IR-beta-EP in both experiments. In the first study hypothalamic IR-beta-EP fell from 189 +/- 17 (SEM) to 132 +/- 7.0 ng/g wet weight of tissue after naltrexone treatment (p less than 0.01). In the second experiment naltrexone lowered IR-beta-EP in the hypothalamus from 23.4 +/- 3.6 to 15.5 +/- 1.2 ng/mg protein (p less than 0.005). Similar decreases in the IR-beta-EP content of the thalamus (from 6.74 +/- 0.59 to 4.59 +/- 0.38 ng/mg protein) and amygdala (from 1.31 +/- 0.08 to 0.90 +/- 0.10) were also measured (p less than 0.01). We conclude that occupancy of opiate receptors by an opiate antagonist reduces brain levels of IR-beta-EP and suggests that chronic opiate receptor blockade may result in a compensatory increase in brain beta-EP release.
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PMID:Effect of chronic naltrexone and methadone administration on brain immunoreactive beta-endorphin in the rat. 631 67

Fractionation of the beta-endorphin-sized material from freshly dissected reptile intermediate pituitaries by ion exchange chromatography on sulfopropyl Sephadex (SP) revealed at least three distinct forms of immunoreactive beta-endorphin. These forms eluted at 0.25 M NaCl, 0.28 M NaCl, and 0.32 M NaCl and represent respectively, 6%, 65% and 29% of the total immunoreactivity. Only the 0.28 M NaCl peak and the 0.32 M NaCl peak exhibited naloxone reversible opiate bioactivity when tested in the isolated guinea pig ileum bioassay system; taking into account the molar amount of immunoreactive peptides the 0.32 M NaCl peak was 6 fold more potent than the 0.28 M NaCl peak. Intermediate pituitaries in culture were incubated with either [3H]tyrosine, [3H]arginine, or [35S]methionine for periods up to 24 hours and beta-endorphin-sized peptides were prepared by immunoprecipitation and gel filtration. Fractionation of the labeled beta-endorphin-sized peptides by ion exchange chromatography yielded profiles nearly identical to the immunoassay analyses of freshly dissected tissue. Further analysis of the major labeled forms of reptile beta-endorphin by chromatography on Sephadex G-50 equilibrated in 6 M guanidine HCl indicated that the 0.32 M NaCl peak had an apparent molecular weight of 3500 +/- 100 and the 0.28 M NaCl peak had an apparent molecular weight of 3200 +/- 100. Furthermore, pulse/chase experiments showed that the 0.32 M NaCl peak was the precursor for the 0.28 M NaCl peak. These results coupled with the relative opiate bioactivities of the major argue that the principal post-translational modification of reptile beta-endorphin is COOH-terminal proteolytic cleavage.
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PMID:Biosynthesis of multiple forms of beta-endorphin in the reptile intermediate pituitary. 632 41

The ip administration of ACTH1-24 (0.2 microgram/kg) or adrenaline-HCl (5.0 micrograms/kg) immediately after training or 6 min prior to testing facilitated retrieval of a one-trial step-down inhibitory avoidance task in rats, acquired using a low intensity footshock. Post-training administration of beta-endorphin (0.1 micrograms/kg, ip) caused retrograde amnesia, but pre-test administration facilitated retrieval. The amnesia caused by post-training administration of beta-endorphin was prevented by ACTH, adrenaline or beta-endorphin given prior to testing. Memory facilitation was most pronounced when the same drug was administered both after the training session and prior to testing. These findings suggest that ACTH, adrenaline and beta-endorphin have at least two effects on memory processing: 1) during the post-training period on the entry of recently stored information into a system that makes it available for retrieval; and 2) both after training and during the test session, that makes learning dependent on states induced by the drugs.
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PMID:Memory modulation by the administration of ACTH, adrenaline or beta-endorphin after training or prior to testing in an inhibitory avoidance task in rats. 632 41

Secretory granules (SGs) from rat intermediate lobes (IL) were isolated in a highly purified form by differential centrifugation, followed by sucrose density gradient centrifugation. The purified IL-SGs were lysed by freezing and thawing. The granule lysate was then centrifuged to generate membrane and soluble fractions. Proopiocortin -converting enzyme (PCE) activity was assayed by incubation of [3H]arginine- or [3H] phenylalanine-labeled toad proopiocortin with the total granule lysate, the membrane, or the soluble fraction at pH 5.0. The processed products were identified by immunoprecipitation with ACTH and beta-endorphin antisera, followed by acid-urea-gel electrophoresis. The PCE activity in rat IL-SG lysate cleaved proopiocortin to 21,000 mol wt ACTH, 21,000 mol wt ACTH/lipotropin (LPH), 13,000 mol wt ACTH, beta LPH, beta-endorphin-like peptides, and alpha MSH-like peptides, similar to those synthesized by the toad intermediate lobe in situ. Treatment of the PCE cleavage products with carboxypeptidase B resulted in the liberation of free arginine. This observation together with the nature of the products formed suggest that the PCE activity cleaved at pairs of basic residues of proopiocortin , yielding one or more products that terminated with an arginine or an arginine-lysine. PCE activity was found in membrane and soluble granule fractions, and both activities were inhibited by leupeptin, p-chloromercuribenzoate, dithiodipyridine, and pepstatin A, but not by chloroquine or N-alpha-p-tosyl-L-lysine-chloromethylketone HCl. Diisopropyl fluorophosphate and other thiol protease reagents (p-chloromercuriphenyl sulfonic acid, iodoacetic acid, and HgCl2) had a small inhibitory effect. The products formed by PCE activities in the membrane and soluble fractions were similar to those cleaved by the total granule lysate. The membrane fraction primarily cleaved proopiocortin between ACTH and beta LPH to form 21,000 (21 K) mol wt ACTH and beta-LPH, similar to the first processing step in the IL in situ. The soluble fraction, however, showed a greater tendency to cleave proopiocortin between the 16 K N-terminal glycopeptide and ACTH, to yield twice as much 21 K ACTH/LPH product as the membrane fraction. The membrane-associated PCE activity was found to be easily solubilized by extraction with high salt (1 M NaCl), suggesting that it is not an integral granule membrane protein.
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PMID:In vitro processing of proopiocortin by membrane-associated and soluble converting enzyme activities from rat intermediate lobe secretory granules. 632 33

Rats were trained in a step-down inhibitory avoidance task using a small start platform (5-cm high, 25 X 7 cm) and a low intensity footshock (0.3 mA, 60 Hz). Retrieval of this task was measured on a test session 24 hr after training. The ip administration of ACTH1-24 (25 ng/rat), epinephrine HCl (625 ng/rat), or human beta-endorphin (125 ng/rat) 5 min prior to testing enhanced retrieval. beta-Endorphin was also effective when given by the icv route at a dose of 25 ng/rat. The icv administration of ACTH (5, 25, or 125 ng/rat) or epinephrine (5, 25, 125, or 625 ng/rat) was ineffective. These findings suggest that memory modulation by beta-endorphin at the time of retrieval may be centrally mediated, whereas the influence of ACTH and epinephrine is probably mediated peripherally.
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PMID:Effect of the intraperitoneal and intracerebroventricular administration of ACTH, epinephrine, or beta-endorphin on retrieval of an inhibitory avoidance task in rats. 632 57

Interferon-alpha inducers were previously shown to cause human lymphocyte production of a corticotropin (ACTH)-like peptide. Thyrotropin (TSH) was not produced under these conditions. In contrast, this report shows that a T-cell mitogen (staphylococcal enterotoxin A), which does not induce the ACTH-like peptide, caused human lymphocyte production of an immunoreactive (ir) TSH. Lymphocyte synthesis of the ir TSH was first detectable at 24 hr, peaked at 48 hr, and thereafter declined. NaDodSO4/polyacrylamide gel electrophoresis of intrinsically radiolabeled lymphocyte-derived ir TSH showed radiolabeled peaks at 80, 50, and 26 kilodaltons. These peaks presumably correspond to trimeric, dimeric, and monomeric TSH-like proteins, respectively. Acid treatment and reduction caused the ir TSH to migrate as a 14-kilodalton peak with a 12-kilodalton shoulder in a gel filtration column run in 6 M guanidine . HCl. Thus, the ir TSH seemed to be composed of subunits with molecular masses corresponding to those of the beta and alpha chains of human TSH, respectively. The ir TSH appeared to be glycoprotein because it bound to a concanavalin A affinity column. Taken together these data suggest that in addition to ACTH, human lymphocytes can also produce a TSH-like substance.
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PMID:Human lymphocyte production of immunoreactive thyrotropin. 635 Oct 72

Changes in responsiveness for the stinging reaction of honeybees fixed in a holder after receiving 3 electrical shocks delivered with 1 min interval, was registered and used as measurement for the effect of 2 microliter of different solutions injected. Every shock consisted of a train of pulses of 1 msec each, delivered for 2 sec at a frequency of 100 Hz. Injection of morphine-HCl (50 to 200 n-moles/bee) produced a dose dependent reduction of the honeybee stinging response to the electrical shocks. The morphine dose that produced a 50% inhibition of the response (D50) was 148 n-moles/bee (927 micrograms/g), i.e., a value far greater than that reported for vertebrates in behavioral test of analgesia. Naloxone 1.1 micrograms/g produces a significant reduction of morphine D50 effect and at 4-5 micrograms/g, a full disinhibition. Thus, whereas the D50 of morphine for honeybees is far greater than that for vertebrates, the doses of naloxone that antagonize morphine are similar for bees and vertebrates. Possible explanations of this difference are mentioned. Injections of met-enkephalin, leu-enkephalin, kyotorphin and (D-Ala2) methionine-enkephalinamide, given in doses of 200 n-moles/bee, an amount greater than that of the morphine D50, exhibited no effect on the stinging response.
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PMID:The stinging response of the honeybee: effects of morphine, naloxone and some opioid peptides. 665 18

Urotensin I, purified from extracts of the urophysis of a teleost fish (Catostomus commersoni), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met-Ile-Glu- Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu -Val-NH2. Extraction with 0.1N HCl at 100 degrees C cleaves the amino-terminal tripeptide, yeilding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.
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PMID:Complete amino acid sequence of urotensin I, a hypotensive and corticotropin-releasing neuropeptide from Catostomus. 698 44

We have used radioimmunoassays with carboxyl-specific antisera to study the development of met- and leu-enkephalin in rat brain and gut from 13-days of fetal age through adulthood. Fractionation of HCl extracts of fetal and neonatal brain tissues by HPLC revealed the presence of immunoreactive forms other than met- and leu-enkephalin. For example, HPLC separation of extracts of 16-day fetal brain yielded two peaks of leu-enkephalin-like immunoreactivity. One emerged at the position of leu-enkephalin, the other eluted with about one-third the retention time. There were four peaks of met-enkephalin-like immunoreactivity, one with the retention time characteristic of met-enkephalin, the others with shorter retention times. In contrast, all of the met-enkephalin-like immunoreactivity in adult brain eluted with the retention time characteristic of authentic met-enkephalin and all of the leu-enkephalin-like immunoreactivity eluted in the position of authentic leu-enkephalin. Multiple immunoreactive forms of met- and leu-enkephalin were found in extracts of both fetal and adult gut tissues.
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PMID:Multiple immunoreactive forms of met- and leu-enkephalin in fetal and neonatal rat brain and in rat gut. 715 39

The immunoactive beta-endorphin-related material in extracts of rat anterior and intermediate/posterior pituitary was separated by ion exchange chromatography on sulfopropyl-Sephadex (Zakarian, S., and Smyth, D. G. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5972-5976). The profile of beta-endorphin immunoactivity in rat anterior pituitary was distinctly different from that found in intermediate/posterior pituitary. In the rat anterior pituitary, most of the immunoactivity co-migrated with synthetic camel beta-endorphin(1-31); in the intermediate/posterior pituitary, only about 10% of the immunoactivity co-migrated with camel beta-endorphin(1-31). In rat anterior pituitary cell suspensions incubated with [3H]tyrosine for 6 h or 48 h, material co-migrating with camel beta-endorphin(1-31) was the major final posttranslational product related to beta-endorphin. This material was reanalyzed by chromatography on sulfopropyl-Sephadex, analyzed by gel filtration on Sephadex G-50 in 6 M guanidine HCl, and digested with pronase and trypsin. In every analysis, the major peak of [3H]tyrosine-labeled anterior pituitary beta-endorphin was indistinguishable from camel beta-endorphin(1-31).
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PMID:Differences in the post-translational processing of beta-endorphin in rat anterior and intermediate pituitary. 724 Jan 65


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