Glutamate dehydrogenase activity in lymphocytes of B-cell chronic lymphocytic leukaemia patients

Clinical Biochemistry

Volumn 42, Issue 16-17, 2009, Pages 1677-1684

  Pajič, Tadej ^a   Černelč, Peter ^a   Sešek Briški, Alenka ^a   Lejko Zupanc, Tatjana ^a   Malešič, Ivan ^b  

^a UNIVERSITY MEDICAL CENTRE LJUBLJANA   (Slovenia)

^b UNIVERSITY OF LJUBLJANA   (Slovenia)

Author keywords

Chronic lymphocytic leukaemia; GLUD1 and GLUD2 gene expressions; Glutamate dehydrogenase

Indexed keywords

CD19 ANTIGEN; GLUTAMATE DEHYDROGENASE; MESSENGER RNA; PROTEIN GLUD1; PROTEIN GLUD2; UNCLASSIFIED DRUG;

ADULT; AGED; ANTIGEN PURIFICATION; ARTICLE; B LYMPHOCYTE; CANCER PATIENT; CHRONIC LYMPHATIC LEUKEMIA; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; FOLLOW UP; GENE EXPRESSION; HUMAN; INFECTIOUS MONONUCLEOSIS; MAJOR CLINICAL STUDY; MALE; PERIPHERAL BLOOD MONONUCLEAR CELL; PRIORITY JOURNAL; REAL TIME POLYMERASE CHAIN REACTION; REFERENCE VALUE; SUPERNATANT;

ADULT; AGED; AGED, 80 AND OVER; CASE-CONTROL STUDIES; FEMALE; GLUTAMATE DEHYDROGENASE; HUMANS; LEUKEMIA, LYMPHOCYTIC, CHRONIC, B-CELL; LYMPHOCYTES; MALE; MIDDLE AGED; POLYMERASE CHAIN REACTION;

EID: 70349776031     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2009.08.003     Document Type: Article

References (52)

1. Rozman C., and Montserrat E. Chronic lymphocytic leukaemia. N. Engl. J. Med. 333 (1995) 1052-1057
2. Chiorazzi N., Rai K.R., and Ferrarini M. Chronic lymphocytic leukemia. N. Engl. J. Med. 352 (2005) 804-815
3. Rai K.R., Sawitsky A., Cronkite E.P., et al. Clinical staging of chronic lymphocytic leukemia. Blood 46 (1975) 219-234
4. Binet J.L., Lepoprier M., Dighiero G., et al. A clinical staging system for chronic lymphocytic leukemia: prognostic significance. Cancer 40 (1977) 855-864
5. Hallek M., Cheson B.D., Catovsky D., et al. Guidelines for the diagnosis and treatment of chronic lymphocytic leukemia: a report from the International Workshop on Chronic Lymphocytic Leukemia updating the National Cancer Institute Working Group 1996 guidelines. Blood 111 (2008) 5446-5456
6. Hallek M., Langenmayer I., Nerl C., et al. Elevated serum thymidine kinase levels identify a subgroup at high risk of disease progression in early, nonsmoldering chronic lymphocytic leukemia. Blood 93 (1999) 1732-1737
7. Messmer B.T., Messmer D., Allen S.L., et al. In vivo measurements document the dynamic cellular kinetics of chronic lymphocytic leukemia B cells. J. Clin. Invest. 115 (2005) 755-764
8. Baggetto L.G. Deviant energetic metabolism of glycolytic cancer cells. Biochimie 74 (1992) 959-974
9. Matsuno T., and Goto I. Glutaminase and glutamine synthetase activities in human cirrhotic liver and hepatocellular carcinoma. Cancer Res. 52 (1992) 1192-1194
10. Newsholme P., Procopio J., Lima M.M., Pithon-Curi T.C., and Curi R. Glutamine and glutamate-their central role in cell metabolism and function. Cell Biochem. Funct. 21 (2003) 1-9
11. Viswanathan T.S., Johnson R.E., and Fisher H.F. Alpha-ketoglutaric acid: solution structure and the active form for reductive amination by bovine liver glutamate dehydrogenase. Biochemistry 21 (1982) 339-345
12. Smith E.L., Austin B.M., Blumenthal K.M., and Nyc J.F. Glutamate dehydrogenase. In: Boyer P.D. (Ed). The enzymes (1975), Academic Press, New York 293-367
13. Schmidt E.S., and Schmidt F.W. Glutamate dehydrogenase: biochemical and clinical aspects of an interesting enzyme. Clin. Chim. Acta 43 (1988) 43-56
14. Hogeboom G.H., and Schneider W.C. Intracellular distribution of enzymes. XI. Glutamate dehydrogenase. J. Biol. Chem. 204 (1953) 233-238
15. Aoki C., Milner T.A., Berger S.B., et al. Glial glutamate dehydrogenase: ultrastructural localization and regional distribution in relation to the mitochondrial enzyme, cytochrome oxidase. J. Neurosci. Res. 18 (1987) 305-318
16. Rothe F., Wolf G., and Schunzel G. Immunohistochemical demonstration of glutamate dehydrogenase in the rat cerebellar cortex. Neuroscience 39 (1990) 19-29
17. Mastorodemos V., Zaganas I., Spanaki C., et al. Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J. Neurosci. Res. 79 (2005) 65-73
18. Di Prisco G., and Casola L. Detection of structural differences between nuclear and mitochondrial glutamate dehydrogenases by the use of imunoadsorbents. Biochemistry 4 (1975) 4679-4683
19. Colon A.D., Plaitakis A., Perakis A., et al. Purification and characterization of a soluble and a particulate glutamate dehydrogenase from rat brain. J. Neurochem. 46 (1986) 1811-1819
20. Rajas F., and Rousset B. A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity. Biochem. J. 295 (1993) 447-455
21. Woo-Kyoung L., Seungjin S., Soo Seock C., and Jong-Sang P. Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum. J. Cell. Biochem. 76 (1999) 244-253
22. Kravos M., and Malešič I. Kinetics and isoforms of serum glutamate dehydrogenase in alcoholics. Alcohol Alcohol. (2008) 1-7
23. Moon K., and Smith E.L. Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by specific chemical cleavages; the complete sequence of the protein. J. Biol. Chem. 248 (1973) 3082-3088
24. Julliard J.H., and Smith E.L. Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J. Biol. Chem. 254 (1979) 3427-3438
25. Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., et al. Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 3494-3498
26. Nakatani Y., Schneider M., Banner C., and Freese E. Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 16 (1988) 6237
27. Bais R., and Panteghini M. Principles of clinical enzymology. In: Burtis C.A., Ashwood E.R., and Bruns D.E. (Eds). Tietz Textbook of Clinical Chemistry and Molecular Diagnostics. 4th (2006), Elsevier Saunders, St.Louis 191-218.
28. T.M. Devlin, 2001. Textbook of Biochemistry with Clinical Correlation. New York: Wiley, p.784-785,895-896.
29. Thomas L. Glutamat-dehydrogenase. In: Thomas L. (Ed). Labor und Diagnose. 6.Aufl. Frankfurt/Maine: TH-Books Verlagsgesellschaft Gmbh (2005) 103-106
30. Stanley C.A., Lieu Y.K., Hsu B.Y.L., et al. Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N. Engl. J. Med. 338 (1998) 1352-1357
31. Yang S.J., Huh J.W., Kim M.J., et al. Regulatory effects of 5′-deoxypyridoxal on glutamate dehydrogenase activity and insulin secretion in pancreatic islets. Biochimie 85 (2003) 581-586
32. Plaitakis A., and Zaganas I. Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain. J. Neurosci. Res. 66 (2001) 899-908
33. Yamaguchi T., Hayashi K., Murakami H., et al. Glutamate dehydrogenase deficiency in spinocerebellar degenerations. Neurochem. Res. 7 (1982) 627-636
34. Plaitakis A., Berl S., and Yahr M.D. Neurological disorders associated with deficiency of glutamate dehydrogenase. Ann. Neurol. 15 (1984) 144-153
35. Trbojević-Čepe A., Jušić A., Kranjčec B., and Vuletić D. Leukocyte glutamate dehydrogenase activity in patients with neurodegenerative and psychiatric diseases. Neurol. Croat. 44 (1995) 33-43
36. Shashidharan P., Michaelides T.M., Robakis N.K., et al. Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J. Biol. Chem. 69 (1994) 16971-16976
37. Deloukas P., Dauwerse J.G., Moschonas N.K., et al. Three human glutamate dehydrogenase genes (GLUD1, GLUDP2, and GLUDP3) are located on chromosome 10q, but are not closely physically linked. Genomics 17 (1993) 676-681
38. Shashidharan P., Clarke D.D., Ahmed N., et al. Nerve tissue-specific human glutamate dehydrogenase that is thermo-labile and highly regulated by ADP. J. Neurochem. 68 (1997) 1804-1811
39. Plaitakis A., Metaxari M., and Shashidharan P. Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function. J. Neurochem. 75 (2000) 1862-1869
40. Yang S.J., Huh J.W., Hong H.N., et al. Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes. FEBS. Lett. 562 (2004) 59-64
41. Beutler E. Composition and metabolism of neutrophils. In: Beutler R., Lichtman M.A., Coller B.S., Kipps T.J., and Seligsohn U. (Eds). Williams Hematology. 6th (2005), McGraw-Hill companies, New York 745-752
42. Belfiore F., and Calcara G. Isocitrate dehydrogenase and glutamate dehydrogenase activity of the granulocytes and lymphocytes. Boll. Soc. Ital. Biol. Sper. 39 (1963) 1571-1574
43. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
44. Orsonneau J.L., Douet P., Massoubre C., et al. An improved pyrogallol red-molybdate method for determining total urinary protein. Clin. Chem. 35 (1989) 2233-2236
45. Gabert J., Beillard E., van der Velden V.H., et al. Standardization and quality control studies of 'real-time' quantitative reverse transcriptase polymerase chain reaction of fusion gene transcripts for residual disease detection in leukemia-a Europe Against Cancer program. Leukemia 17 (2003) 2318-2357
46. Kravos M., and Malešič I. Glutamate dehydrogenase activity at neuroexcitotoxic glutamate development. Eur. Psychiatry 21 (2006) S69
47. Matés J.M., Péres-Gómez C., Núñez de Castro I., Asenjo M., and Márquez J. Glutamine and its relationship with intracellular redox status, oxidative stress and cell proliferation/death. IJBCB 34 (2002) 439-458
48. Curi R., Lagrangha C.J., Doi S.Q., et al. Molecular mechanisms of glutamine action. J. Cell. Physiol. 204 (2005) 392-401
49. Thompson C.B., Bauer D.E., Lum J.J., et al. How do cancer cells acquire the fuel needed to support cell growth. Cold Spring Harb. Symp. Quant. Biol. 70 (2005) 357-362
50. Kovacevic Z. Possibility for the transfer of reducing equivalents from the cytosol to the mitochondrial compartment in Erlich ascites tumor cells by the malate-aspartate shuttle. Eur. J. Biochem. 25 (1972) 372-378
51. DeBerardinis R.J., Mancuso A., Daikhin E., et al. Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. PNAS 104 (2007) 19345-19350
52. Yuneva M., Zamboni N., Oefner P., Sachidanandam R., and Lazebnik Y. Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells. JCB 178 (2007) 93-103