scholarly journals The inhibitory action of l-dihydroxyphenylalanine (l-dopa) in the presence of a monoamine oxidase inhibitor on protein synthesis in vivo and the partial amelioration of this by methionine supplementation

1980 ◽  
Vol 192 (2) ◽  
pp. 703-707 ◽  
Author(s):  
A H Bone ◽  
H R Taufek

Male Wistar rats of various age groups were injected daily over a period of 3 weeks with iproniazid (10 micrograms/g body wt.) and L-dihydroxyphenylalanine (L-dopa; 0.1 mg/g body wt.). On the final day 1 h before the termination of the experiment the animals were injected with L-[14C]valine (0.1 microCi/g body wt.). The specific radioactivity of the valine in the proteins of the subcellular fractions of the tissues examined, relative to the time-integrated mean specific radioactivity of this amino acid in the acid-soluble pools of these tissues, was used to assess protein synthesis. The L-dopa/monoamine oxidase-inhibitor treatment was associated with 30–40% inhibition of protein synthesis. Supplementation of the dietary methionine intake by injection of this amino acid markedly diminished the inhibitory action of the L-dopa/monoamine oxidase-inhibitor treatment on protein synthesis in all fractions examined.

1972 ◽  
Vol 50 (3) ◽  
pp. 261-267 ◽  
Author(s):  
Alan A. Boulton ◽  
P. H. Wu

Following the intraventricular injection of 14C-labelled dopamine, p-tyrosine, and p-tyramine to rats pretreated with a monoamine oxidase inhibitor, the labelled phenolic amines p-tyramine, octopamine, and synephrine were isolated and identified as their DNS derivatives. Differences in the amounts of the phenolicamines formed suggest that mechanisms other than just decarboxylation are involved.


1979 ◽  
Vol 18 (10) ◽  
pp. 771-776 ◽  
Author(s):  
D.S. Robinson ◽  
I.C. Campbell ◽  
Margaret Walker ◽  
Nancy J. Statham ◽  
W. Lovenberg ◽  
...  

1981 ◽  
Vol 74 (1) ◽  
pp. 8-12 ◽  
Author(s):  
David Pickar ◽  
Robert M. Cohen ◽  
David C. Jimerson ◽  
C. Raymond Lake ◽  
Dennis L. Murphy

1975 ◽  
Vol 152 (2) ◽  
pp. 201-210 ◽  
Author(s):  
N. Seiler ◽  
B. Eichentopf

The effects of inhibitors of diamine oxidase (EC 1.4.3.6), monoamine oxidase (EC 1.4.3.4) and 4-aminobutyrate aminotransferase (EC 2.6.1.19) on the catabolism of putrescine in mice in vivo were studied. Diamine oxidase inhibitors and carboxymethoxylamine (amino-oxyacetate) markedly inhibit the metabolism of [14C]putrescine to 14CO2, but affect different enzymes. Aminoguanidine specifically inhibits the mitochondrial and non-mitochondrial diamine oxidases, whereas carboxymethoxylamine specifically inhibits 4-aminobutyrate transamination by the mitochondrial pathway. Hydrazine inhibits at both sites, and results in increased concentrations of 4-aminobutyrate in brain and liver. Pretreatment of mice with carboxymethoxylamine and [14C]putrescine leads to the urinary excretion of amino[14C]butyrate. Carboxymethoxylamine does not affect the non-mitochondrial pathway of putrescine catabolism, as the product of oxidative deamination of putrescine in the extramitochondrial compartment is not further oxidized but is excreted in the urine as derivatives of 4-aminobutyraldehyde. Another catabolic pathway of putrescine involves monoamine oxidase, and the monoamine oxidase inhibitor, pargyline, decreases the metabolism of [14C]putrescine to 14CO2in vivo. Catabolism of putrescine to CO2in vivo occurs along different pathways, both of which have 4-aminobutyrate as a common intermediate, in contrast with the non-mitochondrial catabolism of putrescine, which terminates in the excretion of 4-aminobutyraldehyde derivatives. The significance of the different pathways is discussed.


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