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D Liston

Publications and source records attributed to D Liston.

26 records · Page 2Linked to original sources
PubMed1984

Distribution and characterization of synenkephalin immunoreactivity in the bovine brain and pituitary.

The distribution of synenkephalin, the N-terminal fragment of proenkephalin, was studied in various parts of the bovine brain (globus pallidus, caudate nucleus, hypothalamus) and in the posterior pituitary by the use of a radioimmunoassay. The distribution of synenkephalin-immunoreactivity (IR) was compared to the distribution of Met-enkephalin-IR. Gel exclusion chromatography was used to examine the molecular forms of the immunoreactivities present in the tissues. The distribution of synenkephalin-IR was similar to the distribution of Met-enkephalin-IR, with a molar ratio of Met-enkephalin/synenkephalin ranging between 2.7 and 5.9. In all regions tested except the hypothalamus the synenkephalin-IR was present as a single species. However, in the hypothalamus a small amount of IR material (3% of the total synenkephalin-IR) was detected in fractions where larger Met-enkephalin-containing peptides eluted. Based on the concordance between the molar ratio of Met-enkephalin to synenkephalin found in the tissues and the molar ratio present in the sequence of adrenal proenkephalin, it is concluded that the brain and adrenal glands utilize a similar precursor for enkephalin biosynthesis.

Animals↗
PubMed1984

Purification from brain of synenkephalin, the N-terminal fragment of proenkephalin.

The primary sequence of adrenal proenkephalin was recently deduced from the structure of the cloned cDNA that codes for this protein. Several enkephalin-containing proteins with molecular weights between 8,000 and 20,000 daltons were purified from the bovine adrenal medulla. These proteins appear to represent intermediates in the processing of proenkephalin into physiologically active opioid peptides. While the concentrations of these large processing intermediates in the adrenal medulla are quite high, similar proteins have not yet been shown to be present in brain, and there is some question as to whether the brain synthesizes an enkephalin precursor similar to adrenal proenkephalin. We report here the purification from bovine caudate nucleus of synenkephalin, the N-terminal fragment of adrenal proenkephalin. The amino acid composition of synenkephalin indicates that the protein represents residues 1-70 of adrenal proenkephalin. Thus the brain and adrenal glands appear to utilize a similar precursor for enkephalin biosynthesis.

Amino Acids↗
PubMed1983

Purification of the N-terminal fragment of proenkephalin from bovine adrenal medulla.

Two forms of the N-terminal fragment of proenkephalin have been purified from the bovine adrenal medulla and characterized. One of these proteins contains the sequence of Met-enkephalin and is composed of residues 1-77 of proenkephalin. The other protein does not contain Met-enkephalin and is composed of residues 1-72 of proenkephalin.

Adrenal Medulla↗
PubMed1983

The enkephalinergic neuron: implications of a polyenkephalin precursor.

The study of the biochemical and physiological functions of the enkephalinergic cell has greatly extended our understanding of peptidergic cells in general. In the adrenal gland, the major part of the proenkephalin-derived peptides is present as intermediates in the processing of the precursor. These peptides are contained within the adrenergic chromaffin granules, from which they are released in response to stimulation of the cell. The nature of the products released depends on the nature of the stimulus, but it appears that mature granules containing completely processed peptides are preferentially released under physiological conditions. In the brain, the presence and release of the heptapeptide that comprises the carboxyl terminus of adrenal proenkephalin suggest that similar mechanisms are operating centrally. The identity of brain and adrenal proenkephalin is further supported by the purification from brain of a large fragment of the proenkephalin molecule, synenkephalin , and the occurrence in brain of this and the other proenkephalin-derived peptides in a molar ratio close to that found in the sequence of the adrenal precursor. The processing of proenkephalin in brain appears to follow the classical models first proposed for peptide hormones (Steiner et al. 1980), which may thus be generalized to include peptide neurotransmitters/neuroregulators. In addition, the results presented in this paper indicate that enkephalins may be cotransmitters in at least two diverse systems. Enkephalins and catecholamines are colocalized in the adrenergic granules of the adrenal gland. In the brain, enkephalins and oxytocin are colocalized in the magnocellular neurons of the hypothalamo-neurohypophyseal oxytocinergic pathway. In both of these systems, the enkephalins are present in a molar concentration that is less than 1% of the concentration of the principal messenger. Such colocalization , coupled with the numerous active peptides that may arise from proenkephalin, suggests many elegant but complex schemes of neurotransmitter interactions. For example, release of enkephalins in the neurohypophysis may regulate oxytocin release through an action on autoreceptors of the oxytocinergic terminal. In the adrenal the coreleased enkephalins may act by regulating presynaptically the cholinergic output of the splanchnic nerve. However, further studies are needed to define clearly the physiological roles of such cotransmission . From the abundance of proenkephalin-derived peptides in the basal ganglia, it appears that enkephalins may represent the principal transmitter in some central neurons.(ABSTRACT TRUNCATED AT 400 WORDS)

Adrenal Medulla↗
PubMedDate not supplied

Distribution of enkephalin-containing peptides within bovine chromaffin granules.

The distribution of large enkephalin-containing peptides (ECP's) between soluble and membrane components of bovine chromaffin granules was examined by immunoblotting with synenkephalin antiserum which recognizes the NH2-terminus of proenkephalin. Immunoblots showed that the 23.3 and 18.2 kilodalton ECP's were present in both soluble and membrane granule compartments but the 12.6 kilodalton ECP was present only in the soluble fraction. These results suggest that the larger ECP's may be preferentially associated with the granule membrane and may be redistributed to the soluble granule compartment upon proteolytic processing.

Animals↗