PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “gamma-Endorphin”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources

Improvement of schizophrenic patients treated with [des-Tyr1]-gamma-endorphin (DTgammaE).

It was postulated from animal experiments that gamma-endorphin and, in particular, the nonopiate-like peptide [des-Tyr1]-gamma-endorphin (DTgammaE, beta-lipotropin [beta-LPH]62-77) have neurolepic-like activity. To test this, 14 patients with long-lasting, relapsing schizophrenic or schizoaffective psychosis resistant to conventional neuroleptics were treated with DTgammaE. An open design was used first for six patients (study 1) and a double-blind, crossover design for the other eight (study 2). In study 1, all neuroleptic medication was discontinued and 1 mg of DTgammaE zinc phosphate was given daily intramuscularly for about seven days. In study 2, six patients were maintained with neuroleptic therapy and two patients were drug free; all eight received daily intramuscular injections of 1 mg of nonlasting DTgammaE in saline and solution for eight days. There was transient or semipermanent improvement in both studies in which the psychotic symptoms diminished or even disappeared. In study 2, there was a slight but significant improvement with the first treatment. Improvement continued and by day 4, the psychotic symptoms had almost disappeared. No toxic side effects were noted. These effects of DTgammaE may be a consequence of the normalization of beta-endorphin homeostasis in the brain.

Adult↗

Isolation, primary structure, and synthesis of alpha-endorphin and gamma-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity.

The isolation and primary structure of two peptides with morphinomimetic activity, obtained from an extract of porcine hypothalamus-neurohypophysis, are described. The amino acid sequence of the two peptides, named alpha-endorphin and gamma-endophin, was determined by mass spectrometry and danxyl-Edman methods to be H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH and H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-OH, respectively. These correspond to the amino acid sequences present between residues 61 and 76 and residues 61 and 77 of the various beta-lipotropins. A third peptide also obtained in pure form in these studies was found to be an unstable salt of alpha-endorphin.

Amino Acid Sequence↗

Endorphins: profound behavioral effects in rats suggest new etiological factors in mental illness.

The endogenous morphinomimetic brain peptides Met5-enkephalin and alpha-, beta-, and gamma-endorphins have been evaluated in rats after intracerebrospinal fluid injection. beta-Endorphin produces marked, prolonged muscular rigidity and immobility similar to a catatonic state, counteracted by the opiate antagonist naloxone; this effect occurs at molar doses 1/100 to 1/400 that at which the other peptides or morphine block the response to painful stimuli. All peptides evoked dose-related, naloxone-reversible, wet-dog shakes in rats that had not been exposed to drugs. beta-Endorphin produced hypothermia, whereas gamma-endorphin produced hyperthermia. Such potent and divergent responses to naturally occurring subtances suggest that alterations in their homeostatic regulation could have etiological significance in mental illness.

Animals↗

[Comparative activity of endorphins on the opiate receptors].

Displacement of naloxone from membranes of Rat brain by alpha, beta and gamma-endorphins with and without Na+ in the incubating medium has been studied. beta-endorphin shows a higher affinity for the opiate receptors and a stronger agonist property than morphine. alpha and gamma-endorphins have a much lower affinity than morphine and a marked antagonist characteristic. This study suggests the possibility of naturally occurring antagonists of the opiate receptors.

Animals↗

Radioimmunoassay of beta-endorphin basal and stimulated levels in extracted rat plasma.

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.

Animals↗

Regional distribution of beta-lipotropin converting enzymes in rat pituitary and brain.

Among the brain areas studied only pars distalis and pars intermedia are found to contain beta-lipotropin activating enzyme indicating the these may be the exclusive organs for a physiologically significant conversion of beta-lipotropin into beta-endorphin. beta-Endorphin inactivating enzyme is found to be rather uniformly distributed in all the pituitary and brain regions. alpha-and gamma-endorphins are presumably formed by the action of the enzyme on beta-endorphin.

Animals↗

Reduction of distress vocalization in chicks by opiate-like peptides.

All the opiate-like peptides we tested (Met-enkephalin, (D-Ala2)-Met-enkephalin-NH2, beta-endorphin, (D-Ala2)-beta-endorphin, (D-Ala2)-alpha-endorphin, (D-Ala2)-gamma-endorphin) were capable of reducing distress vocalizations (DV's) in socially-isolated chicks when injected into the vicinity of the fourth ventricle in doses as low as 100 picomoles. All of these substances were at least as potent as equimolar doses of morphine sulfate. In general, DV's were a more sensitive measure of opiate-like peptide effects than reductions in body temperature. In a more limited study using peripheral injections, it was determined that (D-Ala2)-Met-enkephalin at doses of 400 nanomoles/kg, like morphine sulfate, was more effective in reducing DV's, than an equimolar dose of beta-endorphin. beta-endorphin was not as effective via a peripheral route as it was via central administration.

Animals↗

Metabolism of potent enkephalin analogs (FK 33-824, D-Ala2, pentafluorophenylalanine-4-enkephalinamide and a dimer of D-Ala2-enkephalin) and D-amino acid substituted derivatives of human beta-endorphin.

New analogs of the opiate peptides containing novel substitutions were compared in terms of their metabolic stability in the presence of an ultrafiltrate of mouse brain. The enkephalin analog FK 33-824 was more stable at short incubation periods (30 min) than Met-enkephalin but less stable than D-Ala2-enkephalinamide at longer periods (180 min) as shown by the complete release of N-terminal Tyr. In contrast, D-Ala2-enkephalinamide substituted in position 4 with pentafluorophenylalanine was completely stable at the time periods tested. A dimer of D-Ala2-enkephalin was relatively stable at short periods but subject to a 30% hydrolysis (vs. 100% for FK 33-824) in terms of Tyr release at longer periods of incubation. A doubly substituted human beta-endorphin (D-Leu17, D-Lys29-beta-endorphin) showed greater stability than the native peptide based on release of internal residues after incubation with the ultrafiltrate of brain. The presence of D-Leu17 blocked release of intermediate sized endorphins but did not affect liberation of Tyr. The additional presence of D-Thr in position 6 of a triply substituted beta-endorphin (D-Thr6, D-Leu17, D-Lys29-beta-endorphin) did not affect liberation of Tyr, indicating that formation of gamma-endorphin (cleavage of Leu17-Phe) and of enkephalin (cleavage of Met5-Thr) need not occur before the action of brain peptidases. The results demonstrate the feasibility of altering the resistance of analogs of enkephalin and endorphin to degradation by brain enzymes.

Amino Acids↗