Abstract
In confirmation of the findings of Gaitonde et al. (1974), a decrease in the brain concentration of threonine and serine, and an increase in glycine, were observed in rats maintained on a thiamin-deficient diet. Similar changes were found in the blood, and the concentration of several other amino acids in the blood decreased significantly. There was a correlation between the concentrations of threonine, serine, aspartate and asparagine in the brain and blood. In experiments in which [U-14C]threonine was injected into rats most of the radioactivity in the brain and blood of control rats was, as expected, in threonine in the acid soluble metabolites. In contrast, a considerable proportion of radioactivity was also found in other amino acids, namely glutamate, glutamine, aspartate, gamma-aminobutyrate and alanine, in the brain of thiamin-deficient rats. [U-14C]Threonine was also converted into 14C-labelled lactate and glucose, but the extent of this conversion was severalfold higher in thiamin-deficient than in control rats. This finding gave evidence of the stimulation in thiamin-deficient rats of the catabolism of [U-14C]threonine to [14C]lactate by the aminoacetone pathway catalysed by threonine dehydrogenase, and into succinate via propionate by the alpha-oxobutyrate pathway catalysed by threonine dehydratase (deaminase). The measurement of specific radioactivities of glutamate, aspartate and glutamine after injection of [U-14C]threonine, indicated a stimulation of the activities of threonine dehydrogenase and threonine dehydratase (deaminase) in the brain of thiamin-deficient rats. The specific radioactivities of glutamate, asparatate and glutamine int he brain were consistent with an alteration in the metabolism of threonine, mainly in the 'large' compartment of the brain of thiamin-deficient rats. The measurement of relative specific radioactivity of proteins after injection of [U-14C]threonine indicated a marked decrease in the synthesis of proteins, mainly in the liver of thiamin-deficient rats.
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Selected References
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- BECK W. S., FLAVIN M., OCHOA S. Metabolism of propionic acid in animal tissues. III. Formation of succinate. J Biol Chem. 1957 Dec;229(2):997–1010. [PubMed] [Google Scholar]
- BUFFONI F., BLASCHKO H. ENZYMIC OXIDATION OF AMINOKETONES IN MAMMALIAN BLOOD PLASMA. Experientia. 1963 Aug 15;19:421–421. doi: 10.1007/BF02171524. [DOI] [PubMed] [Google Scholar]
- CREMER J. E. AMINO ACID METABOLISM IN RAT BRAIN STUDIED WITH 14C-LABELLED GLUCOSE. J Neurochem. 1964 Mar;11:165–185. doi: 10.1111/j.1471-4159.1964.tb06127.x. [DOI] [PubMed] [Google Scholar]
- Cremer J. E., Heath D. F. The estimation of rates of utilization of glucose and ketone bodies in the brain of the suckling rat using compartmental analysis of isotopic data. Biochem J. 1974 Sep;142(3):527–544. doi: 10.1042/bj1420527. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Doonan S., Koerner D. H., Schmutzler W., Vernon C. A. Inducibility and some properties of the threonine dehydratase of sheep liver. Biochem J. 1974 Dec;144(3):533–541. doi: 10.1042/bj1440533. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ELLIOTT W. H. Amino-acetone; its isolation and role in metabolism. Nature. 1959 Apr 11;183(4667):1051–1052. doi: 10.1038/1831051a0. [DOI] [PubMed] [Google Scholar]
- GAITONDE M. K., DAHL D. R., ELLIOTT K. A. ENTRY OF GLUCOSE CARBON INTO AMINO ACIDS OF RAT BRAIN AND LIVER IN VIVO AFTER INJECTION OF UNIFORMLY 14-C-LABELLED GLUCOSE. Biochem J. 1965 Feb;94:345–352. doi: 10.1042/bj0940345. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GIBSON K. D., LAVER W. G., NEUBERGER A. Initial stages in the biosynthesis of porphyrins. 2. The formation of delta-aminolaevulic acid from glycine and succinyl-coenzyme A by particles from chicken erythrocytes. Biochem J. 1958 Sep;70(1):71–81. doi: 10.1042/bj0700071. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GOLDSTEIN L., KNOX W. E., BEHRMAN E. J. Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver. J Biol Chem. 1962 Sep;237:2855–2860. [PubMed] [Google Scholar]
- Gaitonde M. K., Arnfred T. Metabolism of D-[U-14C]ribose in rat tissues. J Neurochem. 1971 Oct;18(10):1971–1987. doi: 10.1111/j.1471-4159.1971.tb09603.x. [DOI] [PubMed] [Google Scholar]
- Gaitonde M. K., Fayein N. A., Johnson A. L. Decreased metabolism in vivo of glucose into amino acids of the brain of thiamine-deficient rats after treatment with pyrithiamine. J Neurochem. 1975 Jun;24(6):1215–1223. doi: 10.1111/j.1471-4159.1975.tb03901.x. [DOI] [PubMed] [Google Scholar]
- Gaitonde M. K., Nixey R. W., Sharman I. M. The effect of deficiency of thiamine on the metabolism of (U-14C)glucose and (U-14C)ribose and the levels of amino acids in rat brain. J Neurochem. 1974 Jan;22(1):53–61. doi: 10.1111/j.1471-4159.1974.tb12178.x. [DOI] [PubMed] [Google Scholar]
- Gaitonde M. K., Nixey R. W. Sources of error in the determination of specific radioactivity of amino acids isolated by ion-exchange chromatography. Anal Biochem. 1972 Dec;50(2):416–429. doi: 10.1016/0003-2697(72)90050-4. [DOI] [PubMed] [Google Scholar]
- Green M. L., Elliott W. H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem J. 1964 Sep;92(3):537–549. doi: 10.1042/bj0920537. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holowach J., Kauffman F., Ikossi M. G., Thomas C., McDougal D. B., Jr The effects of a thiamine antagonist, pyrithiamine, on levels of selected metabolic intermediates and on activities of thiamine-dependent enzymes in brain and liver. J Neurochem. 1968 Jul;15(7):621–631. doi: 10.1111/j.1471-4159.1968.tb08961.x. [DOI] [PubMed] [Google Scholar]
- Hopkins F. G., Morgan E. J. Studies on glyoxalase: 1. A new factor. Biochem J. 1948;42(1):23–27. [PMC free article] [PubMed] [Google Scholar]
- ISHIKAWA E., NINAGAWA T., SUDA M. HORMONAL AND DIETARY CONTROL OF SERINE DEHYDRATASE IN RAT LIVER. J Biochem. 1965 Apr;57:506–513. doi: 10.1093/oxfordjournals.jbchem.a128109. [DOI] [PubMed] [Google Scholar]
- Jowett M., Quastel J. H. The glyoxalase activity of the red blood cell: The function of glutathione. Biochem J. 1933;27(2):486–498. [PMC free article] [PubMed] [Google Scholar]
- Jowett M., Quastel J. H. The glyoxalase activity of tissues. Biochem J. 1934;28(1):162–172. doi: 10.1042/bj0280162. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KARASEK M. A., GREENBERG D. M. Studies on the properties of threonine aldolases. J Biol Chem. 1957 Jul;227(1):191–205. [PubMed] [Google Scholar]
- Ku Y., Rogers Q. R., Harper A. E. Effects of thyroxine and cortisol on liver threonine dehydratase and tryptophan pyrrolase in rats fed a high protein diet. Proc Soc Exp Biol Med. 1969 Feb;130(2):556–563. doi: 10.3181/00379727-130-33605. [DOI] [PubMed] [Google Scholar]
- LIN S. C., GREENBERG D. M. Enzymatic breakdown of threonine by threonine aldolase. J Gen Physiol. 1954 Nov 20;38(2):181–196. doi: 10.1085/jgp.38.2.181. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Long C. The in vitro oxidation of pyruvic and alpha-ketobutyric acids by ground preparations of pigeon brain. The effect of inorganic phosphate and adenine nucleotide. Biochem J. 1943 Jul;37(2):215–225. doi: 10.1042/bj0370215. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MALKIN L. I., GREENBERG D. M. PURIFICATION AND PROPERTIES OF THREONINE OR ALLOTHREONINE ALDOLASE FROM RAT LIVER. Biochim Biophys Acta. 1964 Apr 6;85:117–131. doi: 10.1016/0926-6569(64)90172-5. [DOI] [PubMed] [Google Scholar]
- MELTZER H. L., SPRINSON D. B. The synthesis of 4-C14, N15-L-threonine and a study of its metabolism. J Biol Chem. 1952 May;197(1):461–474. [PubMed] [Google Scholar]
- Möhler H., Patel A. J., Balázs R. Metabolic compartmentation in the brain: metabolism of a tricarboxylic acid cycle intermediate, (1,4-14C)succinate, after intracerebral administration. J Neurochem. 1974 Dec;23(6):1281–1289. doi: 10.1111/j.1471-4159.1974.tb12228.x. [DOI] [PubMed] [Google Scholar]
- NISHIMURA J. S., GREENBERG D. M. Purification and properties of L-threonine dehydrase of sheep liver. J Biol Chem. 1961 Oct;236:2684–2691. [PubMed] [Google Scholar]
- O'Neal R. M., Koeppe R. E. Precursors in vivo of glutamate, aspartate and their derivatives of rat brain. J Neurochem. 1966 Sep;13(9):835–847. doi: 10.1111/j.1471-4159.1966.tb05879.x. [DOI] [PubMed] [Google Scholar]
- O'neal R. M., Koeppe R. E., Williams E. I. Utilization in vivo of glucose and volatile fatty acids by sheep brain for the synthesis of acidic amino acids. Biochem J. 1966 Dec;101(3):591–597. doi: 10.1042/bj1010591. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PITOT H. C., PERAINO C. STUDIES ON THE INDUCTION AND REPRESSION OF ENZYMES IN RAT LIVER. I. INDUCTION OF THREONINE DEHYDRASE AND ORNITHINE-DELTA-TRANSAMINASE BY ORAL INTUBATION OF CASEIN HYDROLYSATE. J Biol Chem. 1964 Jun;239:1783–1788. [PubMed] [Google Scholar]
- Patel A. J., Balázs R. Manifestation of metabolic compartmentation during the maturation of the rat brain. J Neurochem. 1970 Jul;17(7):955–971. doi: 10.1111/j.1471-4159.1970.tb02249.x. [DOI] [PubMed] [Google Scholar]
- Peraino C. Interactions of diet and cortisone in the regulation of adaptive enzymes in rat liver. J Biol Chem. 1967 Sep 10;242(17):3860–3867. [PubMed] [Google Scholar]
- Peraino C., Lamar C., Jr, Pitot H. C. Studies on the induction and repression of enzymes in rat liver. IV. Effects of cortisone and phenobarbital. J Biol Chem. 1966 Jun 25;241(12):2944–2948. [PubMed] [Google Scholar]
- Riario-Sforza G., Pagani R., Marinello E. Threonine aldolase and allothreonine aldolase in rat liver. Eur J Biochem. 1969 Mar;8(1):88–92. doi: 10.1111/j.1432-1033.1969.tb00499.x. [DOI] [PubMed] [Google Scholar]
- SAYRE F. W., JENSEN D., GREENBERG D. M. Substrate induction of threonine dehydrase in vivo and in perfused rat livers. J Biol Chem. 1956 Mar;219(1):111–117. [PubMed] [Google Scholar]
- Salvatore F., Zappia V., Cortese R. Studies on the deamination of L-amino acids in mammalian tissues. Enzymologia. 1966 Aug 30;31(2):113–127. [PubMed] [Google Scholar]
- TUBBS P. K., GREVILLE G. D. The oxidation of D-alpha-hydroxy acids in animal tissues. Biochem J. 1961 Oct;81:104–114. doi: 10.1042/bj0810104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Turner J. M., Willetts A. J. Amino ketone formation and aminopropanol-dehydrogenase activity in rat-liver preparations. Biochem J. 1967 Feb;102(2):511–519. doi: 10.1042/bj1020511. [DOI] [PMC free article] [PubMed] [Google Scholar]
- URATA G., GRANICK S. Biosynthesis of alpha-aminoketones and the metabolism of aminoacetone. J Biol Chem. 1963 Feb;238:811–820. [PubMed] [Google Scholar]
