Metabolism of D- and L-[13C]alanine in rat liver detected by 1H and 13C NMR spectroscopy in vivo and in vitro

NMR in Biomedicine

Volumn 13, Issue 2, 2000, Pages 72-81

  Dölle, Andreas ^a,b  

^a UNIVERSITY OF BASEL   (Switzerland)

^b RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

1H and 13C NMR spectroscopy; Alanine metabolism; D amino acid oxidase; Gluconeogenesis; Rat liver

Indexed keywords

ALANINE; AMINO ACID OXIDASE; CARBON 13; PENTOSE PHOSPHATE; PERCHLORIC ACID; PROTON; PYRUVATE CARBOXYLASE; PYRUVATE DEHYDROGENASE; TRICARBOXYLIC ACID;

AMINO ACID METABOLISM; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONTROLLED STUDY; ENZYME ACTIVITY; GLUCONEOGENESIS; ISOTOPE LABELING; LIVER METABOLISM; MALE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; RAT;

ALANINE; AMINO ACIDS; ANIMALS; CARBON ISOTOPES; GLUCONEOGENESIS; GLUCOSE; HYDROGEN; LIVER; MAGNETIC RESONANCE SPECTROSCOPY; MALE; MODELS, BIOLOGICAL; RATS; RATS, SPRAGUE-DAWLEY; STEREOISOMERISM;

EID: 0342803849     PISSN: 09523480     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1492(200004)13:2<72::AID-NBM610>3.3.CO;2-Z     Document Type: Article

References (53)

1. Felig P, Wahren J. Protein turnover and amino acid metabolism in the regulation of gluconeogenesis. Fed. Proc. 1974; 33: 1092-1097.
2. Petersen KF, Cline GW, Blair JB, Shulman GI. Substrate cycling between pyruvate and oxaloacetate in awake normal and 3,3′-5-triiodo-L-thyronine-treated rats. Am. J. Physiol. 1994; 267: E273-E277.
3. Petersen KF, Blair JB, Shulman GI. Triiodothyronine treatment increases substrate cycling between pyruvate carboxylase and malic enzyme in perfused rat liver. Metabolism 1995; 44: 1380-1383.
4. I3C NMR study of gluconeogenesis from labeled alanine in hepatocytes from euthyroid and hyperthyroid rats. Proc. Natl Acad. Sci. USA 1981; 78: 60-64.
5. Brainard JR, Hutson JY, London RE, Matwiyoff NA. Carbon-13-enriched substrates for in situ and in vivo metabolic profiling studies by carbon-13 NMR. ACS Symp. Ser. 1984; 258: 157-174.
6. I3C NMR. Proc. Natl Acad. Sci. USA 1979; 76: 4808-4812.
7. Moldes M, Cruz F, Chapa F, Cerdan S. The perfused mouse liver as a model system for the NMR study of intracellular pH homeostasis. Q. Magn. Reson. Biol. Med. 1995; 2: 5-17.
8. I3C-labeled substrates by perfused liver from streptozotocin-diabetic and untreated rats. Biochemistry 1987; 26: 563-572.
9. I3C NMR assay of pyruvate kinase flux. Biochemistry 1987; 26: 573-580.
10. I3C NMR study of effects of fasting and diabetes on the metabolism of pyruvate in the tricarboxylic acid cycle and of the utilization of pyruvate and ethanol in lipogenesis in perfused rat liver. Biochemistry 1987; 26: 581-589.
11. I3C NMR studies of glycogen turnover in the perfused rat liver. J. Biol. Chem. 1988; 263: 5027-5029.
12. 2O as detected by multinuclear NMR spectroscopy. NMR Biomed. 1994; 7: 249-262.
13. Liu KJM, Henderson TO, Kleps RA, Reyes MC, Nyhaus LM. Gluconeogenesis in the liver of tumor rats. J. Surg. Res. 1990; 49: 179-185.
14. I3C NMR study of hepatic pyruvate carboxylase activity in tumor rats. Biochem. Biophys. Res. Commun. 1991; 179: 366-371.
15. I3C NMR analysis of alanine metabolism by isolated perfused livers from C3HeB/FeJ mice infected with African trypanosomes. Comp. Biochem. Physiol. 1988; 89B: 679-685.
16. I3C NMR study. Comp. Biochem. Physiol. 1990; 95B: 505-514.
17. I3C nuclear magnetic resonance methodology for in vivo studies. Magn. Reson. Med. 1986; 3: 24-32.
18. I3C NMR study. J. Biol. Chem. 1989; 264: 3930-3934.
19. I3C NMR investigation. Chem. Res. Toxicol. 1994; 7: 15-22.
20. Ostwald R, Adams PT, Tolbert BM. Synthesis of several carbon-14 labeled DL-alanines. J. Am. Chem. Soc. 1952; 74: 2425-2427.
21. I3C. J. Lab. Comp. 1975; 11: 37-42.
22. Djuric S, Venit J, Magnus P. Silicon in synthesis: STABASE adducts - a new primary amine protesting group: alkylation of ethyl glycinate. Tetrahedron Lett. 1981; 22: 1787-1790.
23. Birnbaum SM, Levintow L, Kingsley RB, Greenstein JP. Specificity of amino acid acylases. J. Biol. Chem. 1952; 194: 455-470.
24. I3C NMR spectroscopy. Biochemistry 1984; 23: 6398-6402.
25. I3C-multilabeled fatty acids. Biochemistry 1986; 25: 6799-6807.
26. IH NMR. J. Biol. Chem. 1988; 263: 11664-11674.
27. Aue WP, Karhan J, Ernst RR. Homonuclear broadband decoupling and two-dimensional J-resolved NMR spectroscopy. J. Chem. Phys. 1976; 64: 4226-4227.
28. Nagayama K, Bachmann P, Wüthrich K, Ernst RR. The use of cross-sections and of projections in two-dimensional NMR spectroscopy. J. Magn. Reson. 1978; 31: 133-148.
29. Turner DL. Basic two-dimensional NMR. Prog. NMR Spectrosc. 1985; 17: 281-358.
30. Bax A, Freeman R. Investigation of complex networks of spin -spin coupling by two-dimensional NMR. J. Magn. Reson. 1981; 44: 542-561.
31. Shaka AJ, Keeler J, Freeman R. Evaluation of a new broadband decoupling sequence: WALTZ-16. J. Magn. Reson. 1983; 53: 313-340.
32. Cross TA, M̈ller S, Aue WP. Radiofrequency resonators for high-field imaging and double-resonance spectroscopy. J. Magn. Reson. 1985; 62: 87-98.
33. Aue WP. Localization methods for in vivo nuclear magnetic resonance spectroscopy. Rev. Magn. Reson. Med. 1986; 1: 21-72.
34. I3C nuclear magnetic resonance spectroscopy of liver and adipose tissue of the living rat. Biochemistry 1983; 22: 4974-4980.
35. I3C surface coil. J. Magn. Reson. 1991; 94: 596-599.
36. Axelrod B. Other pathways of carbohydrate metabolism. In Metabolic Pathways; Greenberg DM (ed.), Vol. 1, 3rd ed.; Academic: New York, 1967.
37. Hollmann S. Non-Glycolytic Pathways of Glucose. Academic: New York, 1964.
38. I4C]glucose for evaluating the mechanism and quantitative significance of the 'liver-cell' pentose cycle. Biochem. J. 1980; 188: 847-857.
39. I3C NMR studies of gluconeogenesis in rat liver cells: utilization of labeled glycerol by cells from euthyroid and hyperthyroid rats. Proc. Natl Acad. Sci. USA 1979; 76: 1603-1607.
40. Cohen SM. Application of nuclear magnetic resonance to the study of liver physiology and disease. Hepatology 1983; 3: 738-749.
41. Meister A. Biochemistry of the Amino Acids, 2nd ed.; Academic: New York, 1965.
42. Perotti ME, Gavazzi E, Trussardo L, Malgaretti N, Curd B. Immunoelectron microscopic localization of D-amino acid oxidase in rat kidney and liver. Histochem. J. 1987; 19: 157-169.
43. Yagi K. Reaction mechanism of D-amino acid oxidase. Adv. Enzymol. 1971; 34: 41-78.
44. Porter DJT, Voet JG, Bright HJ. Mechanistic features of the D-amino acid oxidase reaction studied by double stopped flow spectrophotometry. J. Biol. Chem. 1977; 252: 4464-4473.
45. Barker RF, Hopkinson DA. The genetic and biochemical properties of the D-amino acid oxidases in human tissues. Ann. Hum. Genet. 1977; 41: 27-42.
46. Konno R, Niwa A, Yasumura Y. Intestinal bacterial origin of D-alanine in urine of mutant mice lacking D-amino acid oxidase. Biochem. J. 1990; 268: 263-265.
47. Nagata Y, Akino T. D-Amino acids in mouse tissues are not of microbial origin. Experentia 1990; 46: 466-468.
48. Nagata Y, Akino T, Ohno K, Kataoka Y, Ueda T, Sakurai T, Shiroshita K-I, Yasuda T. Free D-amino acids in human plasma in relation to senescence and renal diseases. Clin. Sci. 1987; 73: 105-108.
49. Nagata Y, Akino T, Ohno K. The presence of free D-amino acids in mouse tissues. Experentia 1989; 45: 330-332.
50. Nagata Y, Yamamoto K, Shimojo T, Konno R, Yasumura Y, Akino T. The presence of free D-alanine, D-proline and D-serine in mice. Biochim. Biophys. Acta 1992; 1115: 208-211.
51. Nagata Y, Konno R, Yasumura Y, Akino T. Involvement of D-amino acid oxidase in elimination of free D-amino acids in mice. Biochem. J. 1989; 257: 291-292.
52. Konno R, Nagata Y, Niwa A, Yasumura Y. Spontaneous excretion of D-alanine in urine in mutant mice lacking D-amino acid oxidase. Biochem. J. 1989; 261: 285-287.
53. I3C NMR measurements of hepatocellular tricarboxylic acid cycle flux. J. Biol. Chem. 1998; 273: 12187-12194.