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 specificity of antimorphine and antimeperidine antisera was measured by competitive displacement of immunizing radiolabeled haptens. Antimorphine antisera demonstrated a high degree of specificity for a conformation of the phenylpiperidine moiety contained within the structures of morphine and its congeners of the morphinan and benzomorphan series. Antimeperidine antisera demonstrated a high degree of specificity for a different conformation of the phenylpiperidine moiety represented within the structures of meperidine and its semisynthetic derivatives. The reactivity of methionine- and leucine-enkephalin, several synthetic enkephalin analogs, and alpha- and beta-endorphin with the antibodies was tested using purified immunoglobulin G in order to avoid serum-induced proteolysis. No significant cross-reactivity of antimorphine antibodies with any of the opioid peptides was detected. All of the opioid peptides tested exhibited weak but immunologically specific cross-reactivity with antimeperidine antibodies. These findings suggest that conformations analogous to the phenylpiperidine moiety in morphine as have been proposed for [Tyr1] in opioid peptides do not appear to be present as measured by immunochemical methods. A conformation with weak stereochemical similarity to the phenylpeperidine moiety in meperidine does appear to be present. The possible homologies between [Phe4] of opioid peptides, meperidine and hydrophobic side chains of certain oripavine derivatives are discussed.
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PMID:The specificity of antimorphine and antimeperidine antibodies and their reactivity with opioid peptides. 43 Mar 66

Concentrations of methionine-enkephalin- (Met-enkephalin) and beta-endorphin-like immunoreactivities were determined in 33 areas of human brain and pituitary using highly sensitive radioimmunoassays in combination with affinity chromatography for the purification of beta-endorphin. It was found that they have quite different distribution patterns, suggesting the existence of both endorphins in independent systems in the central nervous system. Determination of Met-enkephalin and beta-endorphin immunoreactivities in chronic alcoholics and opiate-dependent subjects revealed no gross changes in comparison to the normal subjects.
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PMID:Regional distribution of methionine-enkephalin- and beta-endorphin-like immunoreactivity in human brain and pituitary. 46 43

The effect of opiate peptide administration on the electrical activity of intraocular hippocampal transplants was studied. Similar to observations in situ, the administration of beta-endorphin or methionine enkephalin produces a concentration-dependent increase in the firing rate of identified pyramidal neurons within hippocampal formation transplants. In addition, these peptides elicit a profound increase in 'EEG' amplitude, which ultimately develops into epileptiform activity. The ability of naloxone to either reverse or prevent the peptide-induced changes in both single unit and EEG activity supports the hypothesis that the excitatory response of the hippocampus to opioid peptides is mediated via an opiate receptor. The results of this study also suggest that the excitatory response to the opiate peptides in hippocampus is the result of alterations in intrinsic neuronal circuitry and is not dependent upon extra-hippocampal afferents.
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PMID:Opioid peptides excite pyramidal neurons and evoke epileptiform activity in hippocampal transplants in oculo. 48 69

Mouse tumor cell beta-lipotropin (beta LPH) and gamma-lipotropin (gamma LPH) were purified from mouse pituitary tumor cell culture medium by ion exchange chromatography and gel filtration. The mouse tumor cell beta LPH was identified by immunoprecipitation with several antisera to beta-endorphin, generation of opioid bioactivity upon brief treatment with trypsin, and its identity with the molecule previously shown to serve as an intermediate in the biosynthesis of beta-endorphin. Mouse tumor cell beta LPH (Mr = 8200 +/- 250) and gamma LPH (Mr = 4600 +/- 200) are significantly smaller than known mammalian beta LPH (Mr = 10,000) and gamma LPH (Mr = 6300) molecules. The beta-endorphin region of mouse tumor cell beta LPH has the same amino acid composition as ovine, bovine, and camel beta-endorphin, and species-specific differences are thus located in the gamma LPH region of the molecule. Mouse tumor cell beta LPH and gamma LPH lack a methionine residue at what had been considered to be a highly conserved site in their beta-melanotropin-like region. A species-specific radioimmunoassay for mouse tumor cell gamma LPH was developed. Rat pituitary beta LPH and gamma LPH were shown to be similar to the corresponding mouse tumor cell molecules in size and lack of methionine in their beta-melanotropin-like segment.
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PMID:Characterization of mouse tumor cell beta-lipotropin. 48 93

The Merkel cells from sinus hair follicles of rats were investigated by immunohistochemistry using different antisera against neuropeptides and gastroenteropancreatic (GEP)-hormones. For the first time it has been demonstrated that Merkel cells exhibit an immunoreactivity towards metenkephalin (methionine-enkephalin). The met-enkephalin immunoreactivity was restricted to Merkel cells and was not found in associated nerve axons or terminals. Denervation of Merkel cells did not affect the met-enkephalin immunoreactivity. Antisera leu-enkephalin (leucine-enkephalin) and other polypeptides did not produce an immunoreaction. The demonstration of met-enkephalin-like immunoreactivity supports the concept that the Merkel cell is a member of the paraneuronal system and a potential neuroreceptor cell.
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PMID:Met enkephalin-like immunoreactivity in Merkel cells. 50 86

Beta-Leu5-endorphin, a relative of "normal" beta-endorphin in which leucine is substituted for methionine at position 5 of the latter, has previously been found in high concentrations in the dialysate of schizophrenics. Its removal from plasma by means of hemodialysis has been claimed to relive the symptoms of schizophrenia. Using a highly sensitive radioimmunoassay of equal sensitivity to beta-endorphin and beta-leu5-endorphin, we have compared the plasma immunoreactivity of three schizophrenic patients befofe and after performance of their first session of membrane hemoperfusion. As compared to normal subjects, plasma beta-endorphin-like immunoreactivity was not greatly elevated in the schizophrenic patients before hemoperfusion.However, instead of the expected decrease, a consistent increase in the plasma levels of immunoreactive beta-endorphin was detected after hemoperfusion. In vitro experiments in which two different membranes and hemodialysis as well as hemoperfusion were used, revealed that synthetic beta-leu5-endorphin (and beta-endorphin) from human plasma was not cleared with any of these methods. This finding is inconsistent with the hypothesis that the claimed therapeutic effects of hemodialysis in schizophrenics are due to the removal of a beta-endorphin-like material from the plasma. Consequently, it seems to be unprobable that high concentrations of beta-leu5-endorphin occur in the dialysate or ultrafiltrate of schizophrenics.
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PMID:Endorphins in schizophrenia: hemodialysis/hemoperfusion are ineffective in clearing beta-Leu5-endorphin and beta-endorphin from human plasma. 53 84

1 A method is described for the rapid extraction of opioid peptides from the brain and other tissues. The method is based on acid extraction of tissues followed by adsorption of the extract onto Amberlite XAD-2 resin. Elution with methanol separates the enkephalins and alpha-endorphin from beta-endorphin.2 Over 90% of the opioid peptide activity isolated from brain and gut of several species by our method was due to methionine- and leucine-enkephalin. In contrast, the major opioid peptide activity recovered from the pituitary was due to peptides of much greater mol. wt. than the enkephalins.3 An opioid peptide with properties unlike those of the known endorphins or enkephalins was present in brain extracts. This peptide, termed epsilon-endorphin, has an apparent mol. wt. of 700 to 1200; it constituted between 5 to 10% of the total opioid activity in our extracts.4 A differential assay of methionine- and leucine-enkephalin was made either by destroying methionine-enkephalin activity with cyanogen bromide or by separating the peptides by thin layer chromatography.5 The ratio of methionine-enkephalin to leucine-enkephalin varied greatly in different brain regions. The highest proportions of leucine-enkephalin were found in the cerebral cortex and hippocampus.6 Formaldehyde perfusion and fixation of the brain in vivo had no significant effect on the brain content of enkephalin, indicating that proteolytic breakdown is not a major problem in the extraction of these peptides.7 It is suggested that the enkephalins may have a neurotransmitter role in both brain and peripheral tissues and that methionine- and leucine-enkephalin may subserve separate neuronal functions.
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PMID:The distribution of methionine-enkephalin and leucine-enkephalin in the brain and peripheral tissues. 59 68

The opiate agonist potency of thirteen synthetic enkephalin pentapeptides has been examined on the electrically stimulated guinea pig ileum and mouse vas deferens preparations in comparison with methionine and leucine enkephalins, beta-endorphin and normorphine. Their antagonism by naloxone (Ke) was also assessed on each preparation. Our findings are compatible with, and are discussed in the context of, the hypothesis that these preparations possess at least two populations of receptors.
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PMID:In vitro profile of some opioid pentapeptide analogues. 65 47

A sensitive radioimmunoassay for beta-endorphin is described. Antibodies against human beta-endorphin which exhibit a high avidity for the C-terminal of the peptide were raised in rabbits following the injection of thyroglobulin-coupled human beta-endorphin (betah-E) as immunogen. Methionine-enkephalin, alpha-, gamma-endorphine, as well as ACTH peptides did not cause interference in the radioimmunoassay. beta-Lipotropin, however, showed a 50% cross-reactivity. The sensitivity of the assay is 25 pg/0.5 ml tube volume for beta-endorphin. beta-Endorphin was extracted with a high recovery from the rat plasma using silicic acid and beta-endorphin levels as low as 100 pg/ml could be measured. Basal levels of beta-endorphin-like immunoreactivity in plasma of rats were about 400 pg/ml. beta-Endorphin levels in adrenalectomized rats and in animals chronically treated with the cortisol synthesis blocker metyrapone were found to be markedly increased (about 7-fold). Exposure of the rats to electrically induced footshocks caused a similar increase of immunoreactive beta-endorphin in plasma. A significant increase was also seen after insulin injection.
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PMID:Radioimmunoassay of beta-endorphin basal and stimulated levels in extracted rat plasma. 67 22

Using naloxone as the antagonist, a comparison of pA2 values obtained from the guinea pig ileal longitudinal muscle preparation revealed that both leucine (leu-) enkephalin and methionine (met-) enkephalin can be classified as pure narcotic agonists with pA2 values similar to that of morphine but different from that of nalorphine. In addition, cross tolerance to both met- and leu-enkephal in could be demonstrated on an ileal strip made tolerant to morphine by implantation of morphine pellets to a guinea pig for 72 hours. Pretreatment of a naive muscle strip to three increasing concentrations of leu-enkephalin was found to markedly decrease the IC50 of morphine and to sensitize the ileal strip to naloxone as was evidenced by an increase in the morphine-naloxone pA2 value. Met-enkephalin or morphine pretreatment had no effect on subsequent morphine IC50 determinations but similarly increased the morphine-naloxone pA2 value. These results suggest that although both leu- and met-enkephalin may be classified as pure narcotic agonists, their interaction with morphine on the ileal strip is markedly different. Leu-enkephalin may be an important physiological modulator of narcotic efficacy.
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PMID:Characterization of leucine and methionine enkephalin and their interaction with morphine on the guinea pig ileal longitudinal muscle. 70 20


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