Literature DB >> 6870807

The contribution of phenylalanine to tyrosine metabolism in vivo. Studies in the post-absorptive and phenylalanine-loaded rat.

L L Moldawer, I Kawamura, B R Bistrian, G L Blackburn.   

Abstract

1. Rates of appearance and oxidation of plasma L-leucine, L-phenylalanine and L-tyrosine, as well as conversion of plasma phenylalanine into plasma tyrosine, were determined in 90-120 g rats after overnight starvation and while receiving 115-120 mumol of L-phenylalanine/h. 2. In the post-absorptive state, plasma tyrosine and phenylalanine appearances were similar, despite the fact that 22% of plasma tyrosine appearance could be attributed to the hydroxylation of phenylalanine. 3. A constant infusion of 115-120 mumol of L-phenylalanine/h did not significantly alter plasma leucine kinetics, but increased appearance of plasma phenylalanine and tyrosine. The percentage of phenylalanine and tyrosine appearance that was oxidized increased from 12.1% and 24.4% to 37.3% and 48.0% respectively. In phenylalanine-loaded rats, 72% of plasma tyrosine appearance could be attributed to the conversion of phenylalanine. 4. Whole-body tyrosine oxidation measured from a continuous infusion of either L-[14C]tyrosine or L-[14C]phenylalanine differed by 165%. 5. It can be concluded that, in the post-absorptive state, phenylalanine hydroxylation makes a substantial contribution to the plasma appearance of tyrosine and is significantly increased when phenylalanine is administered. The disposal of excess infused phenylalanine is a result of a greater percentage of plasma phenylalanine being converted into tyrosine and a greater proportion of tyrosine being further oxidized. However, apparent tyrosine oxidation rates estimated from plasma tyrosine specific radioactivities and appearance of expired 14CO2 during administration of [14C]tyrosine are underestimates of true rates, in part because tyrosine generated from phenylalanine hydroxylation is catabolized without freely equilibrating with the plasma compartment.

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Year:  1983        PMID: 6870807      PMCID: PMC1154294          DOI: 10.1042/bj2100811

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  20 in total

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3.  A technique for measuring brain protein synthesis.

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Journal:  J Neurochem       Date:  1972-03       Impact factor: 5.372

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Authors:  R J Neale; J C Waterlow
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5.  Determination of deuterium-labeled phenylalanine and tyrosine in human plasma with high pressure liquid chromatography and mass spectrometry.

Authors:  F K Trefz; D J Byrd; M E Blaskovics; W Kochen; P Lutz
Journal:  Clin Chim Acta       Date:  1976-12       Impact factor: 3.786

6.  Studies on the phenylalanine hydroxylase system in vivo. An in vivo assay based on the liberation of deuterium or tritium into the body water from ring-labeled L-phenylalanine.

Authors:  S Milstien; S Kaufman
Journal:  J Biol Chem       Date:  1975-06-25       Impact factor: 5.157

7.  The diurnal response of muscle and liver protein synthesis in vivo in meal-fed rats.

Authors:  P J Garlick; D J Millward; W P James
Journal:  Biochem J       Date:  1973-12       Impact factor: 3.857

8.  The effect of protein deprivation and starvation on the rate of protein synthesis in tissues of the rat.

Authors:  P J Garlick; D J Millward; W P James; J C Waterlow
Journal:  Biochim Biophys Acta       Date:  1975-11-18

9.  Effect of glucagon on phenylalanine metabolism and phenylalanine-degrading enzymes in the rat.

Authors:  L M Brand; A E Harper
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

10.  Studies of amino acid and protein metabolism in normal man with L-[U-14C]tyrosine.

Authors:  W P James; P J Garlick; P M Sender; J C Waterlow
Journal:  Clin Sci Mol Med       Date:  1976-06
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  7 in total

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Journal:  Am J Physiol Endocrinol Metab       Date:  2017-03-07       Impact factor: 4.310

2.  The Phenylalanine Requirement of Elderly Men and Women Measured by Direct 13C Carbon Oxidation Method Is Similar to That of Young Adults.

Authors:  Kimberly E Martin; Paul B Pencharz; Mahroukh Rafii; Ronald O Ball; Sylwia Szwiega; Rajavel Elango; Glenda Courtney-Martin
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3.  Comparison of different techniques for estimating rates of protein synthesis in vivo in healthy and bacteraemic rats.

Authors:  J J Pomposelli; J D Palombo; K J Hamawy; B R Bistrian; G L Blackburn; L L Moldawer
Journal:  Biochem J       Date:  1985-02-15       Impact factor: 3.857

4.  Monoacetoacetin and protein metabolism during parenteral nutrition in burned rats.

Authors:  A Maiz; L L Moldawer; B R Bistrian; R H Birkhahn; C L Long; G L Blackburn
Journal:  Biochem J       Date:  1985-02-15       Impact factor: 3.857

5.  The inefficiency of total parenteral nutrition to stimulate protein synthesis in moderately malnourished patients.

Authors:  I Warnold; E Edén; K Lundholm
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6.  Proteolysis and phenylalanine hydroxylation in response to parenteral nutrition in extremely premature and normal newborns.

Authors:  S C Denne; C A Karn; J A Ahlrichs; A R Dorotheo; J Wang; E A Liechty
Journal:  J Clin Invest       Date:  1996-02-01       Impact factor: 14.808

7.  Brain tyrosine depletion attenuates haloperidol-induced striatal dopamine release in vivo and augments haloperidol-induced catalepsy in the rat.

Authors:  George E Jaskiw; Rodolfo Bongiovanni
Journal:  Psychopharmacology (Berl)       Date:  2003-10-28       Impact factor: 4.530

  7 in total

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