Disease relevance of Alpha Neo Endorphin

• Expression in Escherichia coli of chemically synthesized gene for a novel opiate peptide alpha-neo-endorphin [1].

High impact information on Alpha Neo Endorphin

• This exon codes for the majority of the translated region of prodynorphin mRNA including the opioid peptides alpha-neo-endorphin, dynorphin A, and dynorphin B [2].
• In brains from colchicine-treated animals, numerous alpha-neo-endorphin/dynorphin-immunoreactive neuronal cell bodies were seen in the supraoptic, retrochiasmatic supraoptic, paraventricular, and magnocellular accessory nuclei of the hypothalamus [3].
• The following brain regions contained alpha-neo-endorphin/dynorphin-immunoreactive fibers and terminals: the median forebrain bundle, the internal capsule, the substantia nigra, the hypothalamus, the nucleus accumbens, the hippocampus, and the medulla oblongata [3].
• Isolation and characterization of an endogenous C-terminal fragment of the alpha-neo-endorphin/dynorphin precursor from bovine caudate nucleus [4].
• Using a specific radioimmunoassay, we have found that immunoreactive (ir) alpha-neo-endorphin has a widespread and unique distribution in the rat brain and spinal cord [5].

Biological context of Alpha Neo Endorphin

• Chemically synthesized alpha-neo-endorphin gene was fused to the Escherichia coli beta-galactosidase gene on the plasmid pKO13 [1].
• Dynorphin A and the kappa-selective compounds D-Pro10-dynorphin(1-11) and U-50,488H were the most potent agonists, with IC50 values of 0.03-0.05 microM, whereas other dynorphin gene products like dynorphin B and alpha-neo-endorphin were approximately 10-fold less potent [6].
• The high affinity of this site for alpha-neo-endorphin and U50,488 suggests that this kappa opioid binding site resembles the kappa 1b subtype [7].
• Alpha-Neo-endorphin (alpha Neo-End), dynorphin B (DynB), DynA(1-13) and DynA(6-17) enhanced phagocytosis less effectively than DynA [8].
• The complete amino acid sequence of alpha-neo-endorphin [9].

Anatomical context of Alpha Neo Endorphin

• The distribution of immunoreactive alpha-neo-endorphin in the central nervous system of the rat [5].
• Distribution of immunoreactive beta-neo-endorphin in discrete areas of the rat brain and pituitary gland: comparison with alpha-neo-endorphin [10].
• In contrast, in all brain tissues alpha-neo-endorphin was found to be the predominant peptide, with tissue levels in striatum and thalamus almost 20 times higher than those of beta-neo-endorphin [11].
• Dynorphin-(1-8), alpha-neo-endorphin, and beta-neo-endorphin are rapidly hydrolyzed to form leu-enkephalin, whereas bovine adrenal medulla dodecapeptide is hydrolyzed to form met-enkephalin [12].
• The opioid peptides are present in very low concentrations in prenatal hippocampus, with only dynorphin B and alpha-neo-endorphin being present in significant amounts [13].

Associations of Alpha Neo Endorphin with other chemical compounds

• Chromatographic and radioimmunological studies showed that pro-Dyn mRNA was translated and fully processed into opioid peptides with leucine-enkephalin (Leu-Enk)-extended sequences [dynorphin-A-(1-8), dynorphin-B-(1-13), and alpha-neo-endorphin] [14].
• Non-cholinergic secretomotor neurons in the submucous ganglia have been shown to be immunoreactive for dynorphin A 1-8, dynorphin A 1-17, dynorphin B and alpha neo-endorphin while cholinergic neurons have been shown to be immunoreactive for dynorphin A 1-8 only [15].
• Characterization and localization of immunoreactive dynorphin, alpha-neo-endorphin, Met-enkephalin and substance P in human spinal cord [16].
• In addition to changes in individual prodynorphin peptides, AMPH treatment caused alterations in the relationships between intermediate peptides (dynorphin A(1-17) and alpha-neo-endorphin) and their immediate products (dynorphin A(1-8) and beta-neo-endorphin) [17].
• Both the native, iodinated and tritiated alpha-neo-endorphin analogs were shown to be homogenous by chromatography on carboxymethylcellulose, paper chromatography, paper electrophoresis, high performance liquid chromatography and amino acid analysis [18].

Gene context of Alpha Neo Endorphin

• PC2 cleaved proDyn to produce dynorphin (Dyn) A 1-17, Dyn B 1-13, and alpha-neo-endorphin, without a previous requirement for PC1/PC3 [19].
• Proenkephalin B-derived opioid peptides, such as dynorphin1-17, dynorphin1-8, dynorphin B, alpha-neo-endorphin and beta-neo-endorphin in the human hypothalamo-neurohypophyseal tract were quantitated and characterized by the combined use of various radioimmunoassays, gel filtration, high performance liquid chromatography and enzymatic cleavage [20].
• Expression of chemically synthesized alpha-neo-endorphin gene fused to E. coli alkaline phosphatase [21].
• In addition to Dyn A1-13-IR, alpha-neo-endorphin-like immunoreactivity was released by LHRH [22].
• Our findings indicate that EC-cells of the investigated species contain pro-dynorphin-related peptides, i.e. dynorphin A and alpha-neo-endorphin, but no derivatives from pro-opiomelanocortin or pro-enkephalin [23].

Analytical, diagnostic and therapeutic context of Alpha Neo Endorphin

• In immunohistochemical staining experiments on frozen sections through rat brains from normal and colchicine-treated animals, the antiserum labeled the same neuronal fiber systems previously described as containing both dynorphin A and alpha-neo-endorphin immunoreactive material [24].
• Purification, sequence analysis, and cellular localization of a prodynorphin-derived peptide related to the alpha-neo-endorphin in the rhynchobdellid leech Theromyzon tessulatum [25].
• In all three species, an immunoreactive form of alpha-neo-endorphin was detected with the same retention time as synthetic mammalian alpha-neo-endorphin following reversed-phase HPLC analysis [26].
• This paper examines the distribution of fibers and cell bodies containing alpha-neo-endorphin in the cat brain stem by using an indirect immunoperoxidase technique [27].
• The newly synthesized polypeptides were analyzed through electrophoresis of immunoprecipitated products or the Western blotting technique using polyclonal antibodies raised against mammalian dynorphin 1-17 and mammalian alpha-neo-endorphin [28].

References