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pubmed-article:9871458pubmed:abstractTextThe amino acid, 6-hydroxydopa (6-OHDOPA), found at the active site of amine oxidases, exists as a keto-enol. Exogenously administered 6-OHDOPA is an excitotoxin like beta-N-oxalylamino-L-alanine (BOAA) and beta-N-methylamino-L-alanine (BMAA), acting at the non-N-methyl-D-aspartate (non-NMDA) alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptor. BMAA and BOAA are causal factors of neurolathyrism in humans. Much exogenously administered 6-OHDOPA is biotransformed by aminoacid decarboxylase (AADC) to the highly potent and catecholamine-(CA) selective neurotoxin, 6-hydroxydopamine (6-OHDA). 6-OHDOPA destroys locus coeruleus noradrenergic perikarya and produces associated denervation of brain by norepinephrine-(NE) containing fibers. Opiopeptides and opioids enhance neurotoxic effects of 6-OHDOPA on noradrenergic nerves, by a naloxone-reversible process. An understanding of mechanisms underlying neurotoxic effects of 6-OHDOPA can be helpful in defining actions of known and newfound amino acids and for investigating their potential neurotoxic properties.lld:pubmed
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pubmed-article:9871458pubmed:dateRevised2005-11-17lld:pubmed
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pubmed-article:9871458pubmed:articleTitleDestruction of catecholamine-containing neurons by 6-hydroxydopa, an endogenous amine oxidase cofactor.lld:pubmed
pubmed-article:9871458pubmed:affiliationDepartment of Pharmacology, Quillen College of Medicine, East Tennessee State University, Johnson City, USA.lld:pubmed
pubmed-article:9871458pubmed:publicationTypeJournal Articlelld:pubmed
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