Novel Opioid Peptide Amidorphin: Characterization and Distribution of Amidorphin‐Like Immunoreactivity in Bovine, Ovine, and Porcine Brain, Pituitary, and Adrenal Medulla

  title={Novel Opioid Peptide Amidorphin: Characterization and Distribution of Amidorphin‐Like Immunoreactivity in Bovine, Ovine, and Porcine Brain, Pituitary, and Adrenal Medulla},
  author={D. C. Liebisch and Bernd R. Seizinger and Gregory J Michael and Albert Herz},
  journal={Journal of Neurochemistry},
Abstract: We have recently isolated from bovine adrenal medulla a novel C‐terminally amidated opioid peptide, amidorphin, which derives from proenkephalin A. Amidorphin revealed a widespread distribution in bovine, ovine, and porcine tissue. Particularly high concentrations of amidorphin immunoreactivity were detected in adrenal medulla, posterior pituitary, and striatum, similar to the major gene products of proenkephalin A. In the adrenal medulla of each species. authentic amidorphin was the… 
Differential posttranslational processing of proenkephalin in rat bone marrow and spleen mononuclear cells: evidence for synenkephalin cleavage.
The results show that PENK was processed in mononuclear cells of the primary and secondary organs of the rat hematopoietic system, as occurs in neural and endocrine tissues, and the precursor was cleaved only in the latter tissue to low molecular weight peptides.
Synenkephalin processing in embryonic rat brain.
Adrenal proenkephalin-derived peptides during postnatal development in spontaneously hypertensive rats.
The results presented suggest that the basic alteration of the adrenal proenkephalin system of SHR may be due to a genetic reduction of proencephalin levels, and the free enkephaline decrease could be related to changes in nervous input to the Adrenal gland.
Characterization of Opioid Binding Sites in the Neural and Intermediate Lobe of the Rat Pituitary Gland by Quantitative Receptor Autoradiography
This work studied the binding characteristics of larger pro‐enkephalin derived peptides for opioid binding sites in the neural lobe by means of light microscopic receptor autoradiography and compared with those in other parts of the pituitary.
Essential metalloelement metabolism and radiation protection and recovery.
This review presents the roles of some essential metalloelement-dependent enzymes in the maintenance and function of tissues and their responses to radiation injury and gives an account of the observed effects of nontoxic doses of essential metaloelement compounds on protection against radiation damage and its recovery.
Radiation Protection and Radiation Recovery with Essential Metalloelement Chelates
  • J. Sorenson, L. Soderberg, L. Chang
  • Biology
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine
  • 1995
The pharmacological effects of essential metalloelement chelates offer a physiological approach to prevention and/or treatment of radiation injury can be understood as due to facilitation of de novo synthesis ofessential metallOElement-dependent enzymes which have roles in preventing the accumulation of pathological concentrations of oxygen radicals or repairing biochemical damage caused by radiation-induced bond homolysis.


Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla
Very high concentrations of amidorphin were detected in bovine adrenal medulla and in a further endocrinological system, the hypothalamic–neurohypophyseal axis, and may be considered to be a major gene product of the opioid peptide precursor proenkephalin A in these endocrine tissues.
Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour
The first identification of a novel opioid octapeptide with a C-terminal amide structure, henceforth designated as ‘adrenorphin’, in human phaeochromocytoma tumour derived from adrenal medulla is presented.
Metorphamide: isolation, structure, and biologic activity of an amidated opioid octapeptide from bovine brain.
  • E. Weber, F. Esch, C. Evans
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1983
A synthetic replicate of metorphamide as well as several synthetic analogs were tested for opioid activity in several bioassays and binding assays, and metorphamia was found to have a high mu-binding activity.
Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid.
An enzymatic activity capable of producing an alpha-amidated peptide product from its glycine-extended precursor has been identified in secretory granules of rat anterior, intermediate, and neural
Rat brain preproenkephalin mRNA. cDNA cloning, primary structure, and distribution in the central nervous system.
Cell-free translation of rat striatal mRNA selected by hybridization with pRPE2 DNA resulted in the synthesis of a 31,000-Da protein, consistent with a single preproenkephalin gene.
Isolation and structural organization of the human preproenkephalin gene
The general organization of the preproenkephalin gene is strikingly similar to that of the gene encoding the common precursor of corticotropin and β-lipotropin (β-LPH)7–9 (alternatively designated preproopiomelanocortin), another multi-hormone precursor.
Binding Characteristics of a Monoclonal β‐Endorphin Antibody Recognizing the N‐Terminus of Opioid Peptides
Data indicate that for the binding to this antibody a tyrosine residue in position 61 is essential, and it thus recognizes a site that is of functional significance for many naturally occurring opioid peptides.
Mechanism of C-terminal amide formation by pituitary enzymes
Porcine pituitary contains an enzyme with the ability to convert peptides that terminate in glycine to the corresponding des-glycine peptide amide, and its mechanism of action involves dehydrogenation and hydrolysis of the glycine-containing substrate.