Rat brain membranes (RBM) bind beta-endorphin with high affinity and specificity. We report herein the identification of a high molecular weight beta-endorphin complex (receptor) in extracts of RBM preincubated with tritiated beta-endorphin, by using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Upon isoelectric focusing, this complex gives a single peak with an isoelectric point (+/- SEM) of 4.50 +/- 0.06. Sucrose density gradient experiments in H2O and 2H2O yield effective partial specific volume (v = 0.814 cm3/g and sedimentation constant s20,w = 15.6 S. Gel filtration yields an estimate of the hydrodynamic radius of 73 A. The corresponding frictional ratio of 1.12 is consistent with an elliptical spheroid with an axial ratio of 3.1-3.2. The molecular mass of the complex is estimated to be 690,000 daltons. The v of the complex is greater than that of CHAPS or most globular proteins.

Animals↗

PubMed1982

Beta-endorphin: replacement of tyrosine in position 27 by tryptophan increases analgesic potency--preparation and properties of the 2-nitrophenylsulfenyl derivative.

An analog of human beta-endorphin with tryptophan in position 27 has been synthetized by the solid-phase method. Bioassay of the analog showed that it had almost 4 times the analgesic potency of the parent hormone but only 68% of the opiate receptor-binding activity. The peptide is the most potent analgesic among the known synthetic analogs of beta-endorphin. The 2-nitrophenylsulfenyl derivative of the analog has been prepared and shown to have a lower analgesic potency and a higher opiate receptor-binding activity than the parent compound.

Amino Acid Sequence↗

PubMed1982

Beta-endorphin: opiate receptor binding activities of six naturally occurring beta-endorphin homologs studied by using tritiated human hormone and naloxone as primary ligands--effects of sodium ion.

Six naturally occurring homologs of beta-endorphin were tested for their potency in inhibiting the binding of [3H]naloxone and [3H]-beta h-endorphin either in the presence or in the absence of Na+. Sodium ion reduces inhibitory potency of these homologs against [3H]-beta h-endorphin and [3H]naloxone to about the same extent. The ratio of the IC50 obtained with Na+ to that obtained without Na+ is not highly correlated with analgesic potency. Very high (greater than 300) sodium ratios are observed with some homologs. A significant rank correlation was found between the ratio of the relative potency in displacing [3H]beta h-endorphin to the relative potency in analgesia and potency in inhibiting the binding of the pure antagonist naloxone.

Animals↗

PubMed1982

Beta subunits of human choriogonadotropin and ovine lutropin are biologically active.

Highly purified beta subunits of human choriogonadotropin and ovine lutropin were found to possess measurable steroidogenic activity in the in vitro rat Leydig cell assay. In addition, beta subunits of these two gonadotropins were able to inhibit the biological activity of human choriogonadotropin in the rat Leydig cell assay.

Animals↗

PubMed1982

Beta-endorphin: synthesis and properties of analogs with replacement of lysine residues by arginine.

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Amino Acid Sequence↗

PubMed1982

Synthesis and properties of equine beta-melanotropin and its naturally occurring des-Asp analog.

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Amino Acids↗

PubMed1982

Isolation and properties of beta-endorphin-(1-27)-like peptide from bovine brains.

A beta-endorphin-(1-27)-like peptide was isolated from bovine cerebral hemisphere extracts by gel filtration, ion-exchange chromatography, high performance liquid chromatography and paper electrophoresis. The peptide had tyrosine as the amino-terminal residue and its amino acid composition was nearly identical to that of equine pituitary beta-EP-(1-27). It had also the same mobility as equine pituitary beta-EP-(1-27) in paper electrophoresis. In radioimmunoassay and opiate receptor-binding assay, the brain peptide had 50% activity when compared with human beta-endorphin-(1-27). Evidence for the occurrence of NH2-acetylated form of beta-endorphin-(1-27) is also presented.

Animals↗

PubMed1982

Melanotropins: aldosterone- and corticosterone-stimulating activity in isolated rat adrenal cells.

Stimulation of corticosterone and aldosterone production in rat adrenal decapsular and capsular cells respectively by alpha- and beta-melanotropins (alpha- and beta-MSH) have been investigated. Although they are considerably less potent than corticotropin (ACTH), the dose-response curves are parallel to those for ACTH except in the case of aldosterone stimulation by beta-MSH where the dose-response curve is biphasic. The steroidogenic actions of ACTH, beta-MSH and alpha-MSH are antagonized by corticotropin-inhibiting peptide in both capsular and decapsular cells. A synthetic analog of beta-MSH ([Gly10]-betac1-MSH) inhibits both beta-MSH and ACTH in aldosterone output in capsular cells, but it does not inhibit their corticosteroidogenic actions in decapsular cells.

Adrenal Glands↗

PubMed1982

Synthesis and properties of human beta-endorphin-(1-17) and its analogs.

Four analogs of human beta-endorphin (beta h-EP) were synthesized by the solid-phase method: beta h-EP-(1-17) (I), [D-Ala2]beta h-EP-(1-17) (II), [Gln8]-beta h-EP-(1-17) (III) and [D-Ala2, Gln8]-beta h-EP-(1-17) (IV). Measurement in a radio-receptor binding assay with use of tritiated beta h-EP as primary ligand gave relative potencies as follows: Met-enkephalin, 100; I, 33; II, 47; III, 889; IV, 123; beta h-endorphin, 2253.

Amino Acids↗

PubMed1982

beta-Endorphin: analgesic and receptor binding activity of non-mammalian homologs.

Analgesic potencies of turkey, ostrich and des-acetyl salmon beta-endorphins have been measured in the tail-flick test and binding affinities determined by radio-receptor assay. The duration of analgesia and the slope of the dose-response curves generated by these peptides are similar to those elicited by mammalian beta-endorphins. This suggests that they act in vivo and in vitro on the same population of opiate receptors. The ratio of binding to analgesic potencies observed for these peptides varies nearly sixfold. Structure-activity analysis suggests that a basic side-chain at position 9 is required in order to produce a high opiate activity both in vivo and in vitro. A reexamination of the biological activities of camel beta-endorphin shows that the analgesic potency and binding affinity of this peptide are respectively 171 and 2.7 times higher than human beta-endorphin. His-27 and/or Gln-31 may contribute to this increased potency. The dissociation of radioreceptor binding affinity from analgesic potency in these naturally occurring beta-endorphin homologs suggests that either the conditions under which the binding assay is performed mask the true binding potency in the brain or that, once bound to the appropriate receptor, these homologs do not possess equal ability to produce biological effects.

Amino Acid Sequence↗

PubMed1982

Corticotropin inhibiting peptide and a synthetic beta-melanotropin analog inhabit the lipolytic activity of corticotropin and melanotropins.

Lipolysis in isolated rabbit fat cells induced by beta-melanotropin, alpha-melanotropin and corticotropin was inhibited by both corticotropin inhibiting peptide and [Gly10]-beta-melanotropin. Corticotropin inhibiting peptide was a more potent antagonist than [Gly10]-beta-melanotropin.

Adipose Tissue↗

PubMed1982

beta-Endorphin: synthesis and properties of analogs modified in positions 8 and 31.

Four analogs of human beta-endorphin (beta h-EP) were synthesized by the solid-phase method: [Gln8,31]-beta h-EP(I), [Arg8,Gln31]-beta h-EP(II), [Ala8,Gln31]-beta h-EP (III), and [Val8, Gln31]-beta h-EP(IV). Radioreceptor binding assay with use of tritiated beta h-EP as primary ligand gave relative potencies as follows: beta h-EP, 100; I, 200;II, 150;III, 150;IV, 120. Relative potencies in an analgesic assay were: beta h-EP, 100; I,236;II, 254;III, 116;IV, 121. The side-chain of Glu-8 in beta h-EP can be replaced by a variety of structures without diminishing biological activity.

Amino Acid Sequence↗

PubMed1982

Synthesis and properties of human gamma-lipotropin.

The synthesis of human gamma-lipotropin by the solid-phase method is described. The synthetic product was characterized by Rf in partition chromatography on Sephadex G-50, paper electrophoresis, polyacrylamide gel electrophoresis, thin-layer chromatography, HPLC, end group determination, peptide mapping of a tryptic digest, and amino acid analyses of acid and enzymic digests. The synthetic material is identical to natural human gamma-lipotropin when assayed against natural human beta-lipotropin for lipolytic activity.

Amino Acid Sequence↗

PubMed1982

Synthesis and properties of human beta-endorphin-(1-9) and its analogs.

Four analogs of human beta-endorphin (beta h-EP) were synthesized by the solid-phase method: beta h-EP-(1-9) (I), [D-Ala2]-beta h-EP-(1-9) (II), [Gln8]-beta h-EP-(1-9) (III), and [D-Ala2, Gln8]-beta h-EP-(1-9) (IV). Measurement in a radioreceptor binding assay with use of tritiated beta h-EP as primary ligand gave relative potencies as follows: Met-enkephalin, 100; I, 76; II, 100; III, 200; IV, 200. Two new amino acid derivatives were prepared and used for synthesis of the analogs: N alpha-t-butyloxycarbonyl-O-(cyclopentyl)-tyrosine and N alpha-t-butyloxycarbonyl-gamma-(cyclopentyl)-glutamic acid.

Amino Acid Sequence↗