Publications

• Physiological functions and pharmacological and toxicological effects of p-octopamine.

  Stohs S.J.

  p-Octopamine occurs naturally in plants, invertebrates and animals with diverse functions and effects. This review summarizes the chemistry, metabolism, receptor binding characteristics, known physiological functions, and pharmacological and toxicological effects of p-octopamine. Databases used in ... >> More

  p-Octopamine occurs naturally in plants, invertebrates and animals with diverse functions and effects. This review summarizes the chemistry, metabolism, receptor binding characteristics, known physiological functions, and pharmacological and toxicological effects of p-octopamine. Databases used included PubMed and Google Scholar Advanced. p-Octopamine binds to neuroreceptors in insects that are not present in humans, while exhibiting poor binding to α-1, α-2, β-1, and β-2 adrenergic receptors in mammalian systems. p-Octopamine modestly binds to β-3 adrenergic receptors and may therefore promote lipolysis and weight loss. p-Octopamine is produced in brain and nerve tissues of mammals and is present and can be measured in the blood of normal human subjects. p-Octopamine is considered to be a CNS stimulant in spite of the fact that it binds poorly to adrenergic receptors. Variations occur in blood levels in association with neurological and hepatic diseases. Its precise role in normal neurophysiology is unclear. No human studies have been reported that demonstrate adverse cardiovascular effects following oral administration. No human studies have examined the effects of p-octopamine on athletic performance or weight loss and weight management. A need exists for both animal and human safety and efficacy studies involving oral administration of p-octopamine. << Less

  Drug Chem Toxicol 38:106-112(2015) [PubMed] [EuropePMC]

• Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes.

  Cuskey S.M., Peccoraro V., Olsen R.H.

  Pseudomonas aeruginosa PAO1 was able to utilize several aromatic biogenic amines as sole sources of carbon or nitrogen. These included the phenethylamines tyramine and dopamine and the phenethanolamines octopamine, synephrine, and norepinephrine. Initial catabolism of the phenethylamines was media ... >> More

  Pseudomonas aeruginosa PAO1 was able to utilize several aromatic biogenic amines as sole sources of carbon or nitrogen. These included the phenethylamines tyramine and dopamine and the phenethanolamines octopamine, synephrine, and norepinephrine. Initial catabolism of the phenethylamines was mediated by a membrane-bound tyramine dehydrogenase which produced 4-hydroxyphenylacetaldehyde (4HPAL) with tyramine as the substrate. The enzyme was induced by growth with both classes of amines. Initial catabolism of octopamine (except when present as the sole source of carbon and nitrogen) was mediated by a soluble enzyme with activity against the phenethanolamines but not against tyramine or dopamine. The product of the reaction with octopamine as substrate was also 4HPAL. Addition of NAD to reaction mixtures yielded 4-hydroxyphenylacetic acid and NADH. These activities, octopamine hydrolyase and 4-HPAL dehydrogenase (measured as a combined activity, OCAH-4HPALDH), were only induced by growth with phenethanolamines. However, the combined activities were not observed in extracts from cells grown with octopamine as the sole source of carbon and nitrogen, suggesting that an alternate pathway is used under this growth condition. Two independently isolated mutant strains were unable to utilize tyramine as a sole source of carbon or nitrogen. These mutants were also unable to utilize dopamine but grew at wild-type rates on the phenethanolamines. The mutations were mapped at about 70 min on the PAO1 chromosome with the chromosome-mobilizing plasmid R68.45, and both were linked to the catA1, mtu-9002, tyu-9009, and puuE mutations. DNA complementing both of the mutations was cloned on a single BamHI fragment approximately 13.8 kilobase pairs in length. Analysis of a subcloned fragment showed that the two mutations were in different genes. << Less

  J Bacteriol 169:2398-2404(1987) [PubMed] [EuropePMC]

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