Summary
At neutral (7.0) and slightly basic (8.2) pH, L-3,4-dihydroxyphenylalanine (L-DOPA), 3,4,5-trihydroxyphenylalanine (5-OH-DOPA) and 3,4-dihydroxyphenylethylamine (dopamine) undergo autoxidation. The binding of radiolabeled oxidation products of L-DOPA, 5-OH-DOPA and dopamine to membrane proteins was compared by a filtration procedure.
Membranes from tentacles of the sea anemoneMetridium senile bind significantly more 5-OH-DOPA than L-DOPA and dopamine. Membranes from rat brain and brains from the three-spined sticklebackGasterosteus aculeatus, bind significantly more dopamine than L-DOPA and 5-OH-DOPA.
Membranes fromMetridium contain an o-diphenol O2: oxidoreductase (tyrosinase). In the absence of inhibitors, enzymatic oxidation causes a fiftyfold increase in binding of L-DOPA and a more than tenfold increase in binding of dopamine, whereas the binding of 5-OH-DOPA only is increased by 10%. It is concluded than 5-OH-DOPA more easily undergo autoxidation than L-DOPA and dopamine, but its quinone form is probably less reactive with membrane proteins. The suitability of tyrosinase-mediated biosynthesis of L-DOPA and 5-OH-DOPA versus tyrosine hydroxylase-mediated biosynthesis of L-DOPA and dopamin in primitive nervous systems and in the vertebrate CNS is discussed on the basis of the cytotoxic potential through irreversible binding to membrane proteins of oxidation products of the catechol compounds formed.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Agrup G, Rorsman H, Rosengren E (1982a) 5-OH-DOPA, product and substrate for tyrosinase. Acta Derm Venereol (Stockholm) 62: 371–3786
Agrup G, Hansson C, Rorsman H, Rosengren E (1982b) The effect of cysteine and oxidation of tyrosine, dopa and cysteinyldopas. Arch Dermatol Res 272: 103–115
Anctil M (1985) Cholinergic and monoaminergic mechanisms associated with control of bioluminescence in the ctenophoreMnemiopsis leidyi. J Exp Biol 119: 225–238
Anctil M, Boulay D, Lariviere L (1982) Monoaminergic mechanisms associated with control of luminescence and contractile activities in the coelenterateRenilla köllikeri. J Exp Zool 223: 11–24
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254
Carlberg M (1983) Evidence of dopa in the nerves of sea anemones. J Neural Transm 57: 75–84
Carlberg M, Laxmyr L, Rosengren E, Elofsson R (1982) 5-OH-DOPA and 5-S-cysteinylDOPA: new biogenic amino acids in invertebrates. Comp Biochem Physiol 73 C: 23–25
Carlberg M, Jergil B, Lindbladh C, Rosengren E (1984) Enzymatic 5-hydroxylation of L-DOPA by a tyrosinase isolated from the sea anemoneMetridium senile. Gen Pharmacol 15: 301–307
Carlberg M, Rosengren E (1985) Biochemical basis for adrenergic neurotransmission in coelenterates. J Comp Physiol B 155: 251–255
Carlberg M, Elofsson R (1987) Presence of 3,4-dihydroxyphenylalanine and 3,4,5-trihydroxyphenylalanine in a coelenterate nervous system: possible tyrosinase-mediated accumulation. Neurochem Int 11: 161–167
Chung JM, Spencer AN, Gahm KH (1989) Dopamine in tissues of the hydrozoan jellyfishPolyorchis penicillatus as revealed by HPLC and GC/MS. J Comp Physiol B 159: 173–181
Cohen G (1983) The pathobiology of Parkinson's disease: biochemical aspects of dopamine neuron senescence. J Neural Transm [Suppl 19]: 89–103
Dahl E, Falck B, von Mecklenburg C, Myhrberg H (1963) An adrenergic system in sea anemone. QJ Microsc Sci 104: 531–534
De Waele J-P, Anctil M, Carlberg M (1987) Biogenic catecholamines in the cnidarianRenilla köllikeri: radioenzymatic and chromatographic detection. Can J Zool 65: 2458–2465
Graham DG, Tifany SM, Vogel FS (1978) The toxicity of melanin precursors. J Invest Dermatol 70: 113–116
Hadjiconstantinou M, Neff NH (1983) Ascobic acid could be hazardous to your experiments: a commentary on dopamine receptor binding studies with speculation on a role for ascorbic acid in neuronal function. Neuropharmacology 22: 939–943
Hansson C, Rorsman H, Rosengren E (1980) 5-Hydroxydopa a new compound in the Raper-Mason scheme of melanogenesis. Acta Derm Venereol (Stockholm) 60: 281–286
Kuo C-H, Hata F, Yoshida H, Yamatodani A, Wada H (1979) Effect of ascorbic acid on release of acetylcholine from synaptic vesicles prepared from different species of animals and release of noradrenaline from synaptic vesicles of rat brain. Life Sci 24: 911–916
Laxmyr L (1985) Tyrosine hydroxylase activity in central nervous system of the crayfish,Pacifastacus leniusculus (Crustacea, Decapoda). J Comp Physiol B 155: 603–609
Marle J van (1977) Contribution to the knowledge of the nervous system in the tentacles of some coelenterates. Bijdr Dierkd 46: 219–260
Nagatsu T, Levitt M, Udenfriend S (1964) Tyrosine hydroxylase—the initial step in norepinephrine biosynthesis. J Biol Chem 239: 2910–2917
Nickoloff BJ, Grimes M, Wohlfeil E, Hudson RA (1985) Affinity-dependent cross-linking to neurotoxin sites of the acetylcholine receptor mediated by catechol oxidation. Biochemistry 24: 999–1007
Prota G (1980) Recent advances in the chemistry of melanogenesis in mammals. J Invest Dermatol 75: 122–127
Riley PA (1977) The mechanism of melanogenesis. Symp Zool Soc Lond 39: 77–95
Scheulen M, Wollenberg P, Bolt HM, Kappus H, Remmer H (1975) Irreversible binding of dopa and dopamine metabolites to protein by rat liver microsomes. Biochem Biophys Res Comm 66: 1396–1400
Seeman P (1980) Brain dopamine receptors. Pharmacol Rev 32: 229–313
Tse DCS, McCreery RL, Adams RN (1976) Potential oxidative pathways of brain catecholamines. J Med Chem 19: 37–40
Welsh JH, Williams LD (1970) Monoamine-containing neurones inPlanaria. J Comp Neurol 138: 103–116
Wolfe BB, Zirolli JA, Molinoff PB (1974) Binding of dl-[3H]epinephrine to proteins of rat ventricular muscle: nonidentity with beta adrenergic receptors. Mol Pharmacol 10: 582–596
Yamamura HI, Enna SJ, Kuhar MJ (1985) Neurotransmitter receptor binding, 2nd edn. Raven Press, New York, p 69
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Carlberg, M. 3,4-dihydroxyphenylethylamine, L-3,4-dihydroxyphenylalanine and 3,4,5-trihydroxyphenylalanine: Oxidation and binding to membranes. A comparative study of a neurotransmitter, a precursor and a neurotransmitter candidate in primitive nervous systems. J. Neural Transmission 81, 111–119 (1990). https://doi.org/10.1007/BF01245831
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01245831