Opiate Receptors and Opioid Peptides: Are They Involved in Drug Addiction?

Author(s):  
Eric J. Simon
Life Sciences ◽  
1982 ◽  
Vol 31 (12-13) ◽  
pp. 1347-1350 ◽  
Author(s):  
Michael E. Lewis ◽  
Henry Khachaturian ◽  
Stanley J. Watson

1980 ◽  
Vol 89 (1) ◽  
pp. 239-255
Author(s):  
J. HUGHES ◽  
A. BEAUMONT ◽  
J. A. FUENTES ◽  
B. MALFROY ◽  
C. UNSWORTH

At the present time there is evidence for two families of related peptides which act as ligands for opiate receptor sites. The endorphin group of peptides are derived from the ACTH/LPH precursor pro-opiocortin. The enkephalins appear to be formed from a separate precursor or precursors that have yet to be fully characterized. There appear to be a number of different types of opiate receptors and this may be related to the multiplicity of peptide ligands that have so far been identified. The enkephalins and related peptides appear to have a much wider distribution than the endorphins but the latter may act as circulating hormones unlike the enkephalins. It is likely that both endorphins and enkephalins are involved in sensory modulation processes and release of these peptides has been demonstrated during brain stimulation for pain relief. The enkephalins are very rapidly inactivated by tissue proteases, the aminopeptidases appear largely responsible for the inactivation of exogenously administered enkephalins but the dipeptidyl carboxypeptidase, termed enkephalinase, may have a special inactivating function at enkephalinergic synapses. Evidence will be presented for the biosynthesis, the release and inactivation of the enkephalins relating to the above points.


1985 ◽  
Vol 110 (1) ◽  
pp. 101-106 ◽  
Author(s):  
L. Cacicedo ◽  
F. Sánchez Franco

Abstract. This study was undertaken to determine the effect of opioid peptides and naloxone on the secretion of thyrotrophin (TSH), alpha subunit (α subunit) and beta thyrotrophin (TSH-β) from rat pituitary dispersed cells in primary culture. Naloxone (NAL) 10−5m was found to increase basal TSH, α subunit and TSH-β secretion. This effect of NAL was not blocked by human β-endorphin (βh-End) 10−7 m. Concurrent treatment with triiodothyronine (T3) 10−7 m significantly decreased NAL stimulated secretion of TSH and its subunits. Thyrotrophin releasing hormone (TRH) stimulation of secretion of TSH and its subunits was not further augmented by NAL. In contrast, 10−7 m of βh-End, methionine-enkephaline (Met-Enk) and D-ala2-met-enkephalinamide (DALA) had no effect on secretion of TSH and subunits. A time course study confirmed no change in TSH secretion following pre-treatment with βh-End at 4, 10, 24 and 48 h. These findings go against a direct action of βh-End, Met-Enk and DALA on TSH secretion. The response of TSH and its subunits to NAL and the lack of interaction with βh-End might be explained by the existence of different types of opiate receptors. Counteraction of this effect by T3 suggests other possible mechanisms.


1979 ◽  
Vol 2 (1) ◽  
pp. 35-64 ◽  
Author(s):  
S H Snyder ◽  
S R Childers

1982 ◽  
Vol 1 (4) ◽  
pp. 195-198
Author(s):  
B. J. Meyer

In 1964 β-lipotropin, a compound consisting of 91 amino acids, was isolated from the adenohypophysis. In 1973, opiate receptors were found to be present in different areas of the brain and it was postulated that the brain probably produces opiate-like substances which react with these receptors. This finding was followed with an intensive search for opiate-like substances, resulting in the isolation of two groups of substances which react with the opiate receptors. These were named the encephalins and the endorphins. All members of these two groups were either peptides or polypeptides and the amino-acid sequence of each corresponded to the amino-acid sequence of specific segments of β-lipotropin.


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