Characterization of opiate receptor heterogeneity using affinity ligands and phospholipase A/sub 2/

Thesis/Dissertation · Mon Dec 31 23:00:00 EST 1984

OSTI ID:5006490

Reichman, M

The primary aim of the dissertation was to study the heterogeneity of opiate receptors by utilizing affinity ligands, and by modification of the receptor lipid-microenvironment with phospholipase A/sub 2/ (PLA/sub 2/). The affinity ligands, 14-bromacetamidomorphine (BAM) and 14-chloroacetylnaltrexone (CAN), selectively inactivated high affinity dihydromorphine binding sites in an apparently irreversible manner (the inhibition was resistant to extensive washes of treated neural membrane homogenates). The inhibitory effect of PLA/sub 2/ (10 ng/ml) on opiate receptor subtypes was determined using (/sup 3/H)-dihydromorphine (..mu..-type agonist), (/sup 3/H)-enkephalin (delta agonist) and (/sup 3/H)-naloxone (..mu.. antagonist). PLA/sub 2/ abolished the high affinity antagonist binding site, whereas it inhibited high and low affinity agonist binding sites similarly. The results suggest that high affinity antagonist binding sites are different from high affinity agonist binding sites. Indirect binding assays demonstrated that the selectivities of ..mu..- and delta receptors are not affected significantly by PLA/sub 2/ treatment.

• Research Organization: Rochester Univ., NY (USA)
• OSTI ID: 5006490
• Country of Publication: United States
• Language: English

Related Subjects

551001* -- Physiological Systems-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALKALOIDS
ANALGESICS
ANIMALS
BODY
BRAIN
CARBOXYLESTERASES
CENTRAL NERVOUS SYSTEM
CENTRAL NERVOUS SYSTEM DEPRESSANTS
CONFIGURATION INTERACTION
DRUGS
ENZYMES
ESTERASES
HYDROLASES
LABELLED COMPOUNDS
LIPASE
MAMMALS
MEMBRANE PROTEINS
MORPHINE
NARCOTICS
NERVOUS SYSTEM
OPIUM
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RATS
RECEPTORS
RODENTS
TRITIUM COMPOUNDS
VERTEBRATES