Biotin requirements are lower in human Jurkat lymphoid cells but homeostatic mechanisms are similar to those of HepG2 liver cells

Journal of Nutrition

Volumn 140, Issue 6, 2010, Pages 1086-1092

  Mall, Gaganpreet Kaur ^a   Chew, Yap Ching ^a   Zempleni, Janos ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; CARBOXYLASE; MESSENGER RNA; METHYLCROTONOYL COENZYME A CARBOXYLASE;

ARTICLE; BIOTINYLATION; CELL STRAIN HEPG2; CELL TYPE; CONTROLLED STUDY; HOMEOSTASIS; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; LEUKEMIA CELL LINE; LYMPHOID CELL; LYMPHOID TISSUE; PROTEIN EXPRESSION; QUALITATIVE ANALYSIS; QUANTITATIVE ANALYSIS;

BIOTIN; BIOTINYLATION; CARBOXY-LYASES; CULTURE MEDIA; HEP G2 CELLS; HEPATOCYTES; HISTONES; HOMEOSTASIS; HUMANS; JURKAT CELLS; LYMPHOCYTES;

EID: 77952650770     PISSN: 00223166     EISSN: 15416100     Source Type: Journal    
DOI: 10.3945/jn.110.121475     Document Type: Article

References (52)

1. Mock DM, Lankford GL, Mock NI. Biotin accounts for only half of the total avidin-binding substances in human serum. J Nutr. 1995;125:941-946
2. Said HM. Recent advances in carrier-mediated intestinal absorption of water-soluble vitamins. Annu Rev Physiol. 2004;66:419-446
3. Prasad PD, Wang H, Kekuda R, Fujita T, Fei Y-J, Devoe LD, Leibach FH, Ganapathy V. Cloning and functional expression of a cDNA encoding a mammalian sodium-dependent vitamin transporter mediating the uptake of pantothenate, biotin, and lipoate. J Biol Chem. 1998;273:7501-7506
4. Daberkow RL, White BR, Cederberg RA, Griffin JB, Zempleni J. Monocarboxylate transporter 1 mediates biotin uptake in human peripheral blood mononuclear cells. J Nutr. 2003;133:2703-2706 (Pubitemid 37099748)
5. Gralla M, Camporeale G, Zempleni J. Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus. J Nutr Biochem. 2008;19:400-408 (Pubitemid 351685666)
6. Leon-Del-Rio A, Leclerc D, Akerman B, Wakamatsu N, Gravel RA. Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli. Proc Natl Acad Sci USA. 1995;92:4626-4630
7. Camporeale G, Zempleni J. Biotin. In: Bowman BA, Russell RM, editors. Present knowledge in nutrition. 9th ed. Washington, DC: International Life Sciences Institute; 2006. p. 314-326
8. Dakshinamurti K, Chauhan J. Biotin-binding proteins. In: Dakshinamurti K, editor. Vitamin receptors: vitamins as ligands in cell communication. Cambridge (UK): Cambridge University Press; 1994. p. 200-249
9. Mock DM, Henrich CL, Carnell N, Mock NI. Indicators of marginal biotin deficiency and repletion in humans: validation of 3-hydroxyisovaleric acid excretion and a leucine challenge. Am J Clin Nutr. 2002;76:1061-1068
10. Mock DM, Quirk JG, Mock NI. Marginal biotin deficiency during normal pregnancy. Am J Clin Nutr. 2002;75:295-299
11. Wolf B, Heard GS. Biotinidase deficiency. In: Barness L, Oski F, editors. Advances in pediatrics. Chicago: Medical Book Publishers; 1991. p. 1-21.
12. Suzuki Y, Yang X, Aoki Y, Kure S, Matsubara Y. Mutations in the holocarboxylase synthetase gene HLCS. Hum Mutat. 2005;26:285-290 (Pubitemid 41361794)
13. Roth KS, Yang W, Foreman JW, Rothman R, Segal S. Holocarboxylase synthetase deficiency: a biotin-responsive organic acidemia. J Pediatr. 1980;96:845-849 (Pubitemid 10068210)
14. Dakshinamurti K, Cheah-Tan C. Liver glucokinase of the biotin deficient rat. Can J Biochem. 1968;46:75-80.
15. Solorzano-Vargas RS, Pacheco-Alvarez D, Leon-Del-Rio A. Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells. Proc Natl Acad Sci USA. 2002;99:5325-5330 (Pubitemid 34411547)
16. Rodriguez-Melendez R, Zempleni J. Nitric oxide signaling depends on biotin in Jurkat human lymphoma cells. J Nutr. 2009;139:429-433
17. Rodriguez-Melendez R, Griffin JB, Zempleni J. The expression of genes encoding ribosomal subunits and eukaryotic translation initiation factor 5A depends on biotin and bisnorbiotin in HepG2 cells. J Nutr Biochem. 2006;17:23-30. (Pubitemid 41774402)
18. Griffin JB, Rodriguez-Melendez R, Zempleni J. The nuclear abundance of transcription factors Sp1 and Sp3 depends on biotin in Jurkat cells. J Nutr. 2003;133:3409-3415 (Pubitemid 37409466)
19. Rodriguez-Melendez R, Griffin JB, Sarath G, Zempleni J. High-throughput immunoblotting identifies biotin-dependent signaling proteins in HepG2 hepatocarcinoma cells. J Nutr. 2005;135:1659-1666 (Pubitemid 40980715)
20. Camporeale G, Giordano E, Rendina R, Zempleni J, Eissenberg JC. Drosophila holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan and heat tolerance. J Nutr. 2006;136:2735-2742 (Pubitemid 44771766)
21. Kobza K, Sarath G, Zempleni J. Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3. BMB Rep. 2008;41:310-315
22. Hymes J, Fleischhauer K, Wolf B. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med. 1995;56:76-83.
23. Stanley JS, Griffin JB, Zempleni J. Biotinylation of histones in human cells: effects of cell proliferation. Eur J Biochem. 2001;268:5424-5429 (Pubitemid 32948369)
24. Chew YC, Camporeale G, Kothapalli N, Sarath G, Zempleni J. Lysine residues in N- and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. J Nutr Biochem. 2006;17:225-233
25. Kobza K, Camporeale G, Rueckert B, Kueh A, Griffin JB, Sarath G, Zempleni J. K4, K9, and K18 in human histone H3 are targets for biotinylation by biotinidase. FEBS J. 2005;272:4249-4259
26. Camporeale G, Shubert EE, Sarath G, Cerny R, Zempleni J. K8 and K12 are biotinylated in human histone H4. Eur J Biochem. 2004;271:2257-2263
27. Camporeale G, Oommen AM, Griffin JB, Sarath G, Zempleni J. K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells. J Nutr Biochem. 2007;18:760-768 (Pubitemid 47600652)
28. Wijeratne SS, Camporeale G, Zempleni J. K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts. J Nutr Biochem. Epub 2009 Apr 13.
29. Chew YC, West JT, Kratzer SJ, Ilvarsonn AM, Eissenberg JC, Dave BJ, Klinkebiel D, Christman JK, Zempleni J. Biotinylation of histones represses transposable elements in human and mouse cells and cell lines, and in Drosophila melanogaster. J Nutr. 2008;138:2316-2322
30. Berne RM, Levy MN. Special circulations. In: Berne RM, Levy MN, editors. Physiology. 4th ed. St. Louis: Mosby; 1998. p. 478-501.
31. Feder S, Daniel H, Rehner G. In vivo kinetics of intestinal absorption of riboflavin in rats. J Nutr. 1991;121:72-79
32. Manthey KC, Griffin JB, Zempleni J. Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells. J Nutr. 2002;132:887-892 (Pubitemid 34493547)
33. Camporeale G, Zempleni J. Oxidative folding of interleukin-2 is impaired in flavin-deficient Jurkat cells, causing intracellular accumulation of interleukin-2 and increased expression of stress response genes. J Nutr. 2003;133:668-672 (Pubitemid 36268337)
34. Manthey KC, Chew YC, Zempleni J. Riboflavin deficiency impairs oxidative folding and secretion of apolipoprotein B-100 in HepG2 cells, triggering stress-response systems. J Nutr. 2005;135:978-982 (Pubitemid 40638294)
35. Zempleni J, Helm RM, Mock DM. In vivo biotin supplementation at a pharmacologic dose decreases proliferation rates of human peripheral blood mononuclear cells and cytokine release. J Nutr. 2001;131:1479-1484
36. Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods. 2001;25:402-408 (Pubitemid 34164012)
37. Griffin JB, Stanley JS, Zempleni J. Synthesis of a rabbit polyclonal antibody to the human sodium-dependent multivitamin transporter. Int J Vitam Nutr Res. 2002;72:195-198
38. Dahl JA, Collas P. A rapid micro chromatin immunoprecipitation assay (microChIP). Nat Protoc. 2008;3:1032-1045 (Pubitemid 351818692)
39. Kouzarides T, Berger SL. Chromatin modifications and their mechanism of action. In: Allis CD, Jenuwein T, Reinberg D, editors. Epigenetics. Cold Spring Harbor (NY): Cold Spring Harbor Press; 2007. p. 191-209.
40. Blanchard R, Gu X, Burnette A, Huang J, Zeng X. Genome-wide, promoter-tilling, real-time PCR assays for analyzing chromatin immunoprecipitation samples. 2007 [cited 2009 Jun 15]. Available from: www.sabiosciences.com/support-posters.php.
41. Haring M, Offermann S, Danker T, Horst I, Peterhansel C, Stam M. Chromatin immunoprecipitation: optimization, quantitative analysis and data normalization. Plant Methods. 2007;3:11. (Pubitemid 350125929)
42. SAS Institute. StatViewreference. 3rd ed.Cary(NC):SAS Publishing; 1999.
43. Shriver BJ, Roman-Shriver C, Allred JB. Depletion and repletion of biotinyl enzymes in liver of biotin-deficient rats: evidence of a biotin storage system. J Nutr. 1993;123:1140-1149 (Pubitemid 23175952)
44. Mock DM. Marginal biotin deficiency is common in normal human pregnancy and is highly teratogenic in mice. J Nutr. 2009;139:154-157
45. Mardach R, Zempleni J, Wolf B, Cannon MJ, Jennings ML, Cress S, Boylan J, Roth S, Cederbaum S, et al. Biotin dependency due to a defect in biotin transport. J Clin Invest. 2002;109:1617-1623
46. NRC. Dietary reference intakes for thiamin, riboflavin, niacin, vitamin B6, folate, vitamin B12, pantothenic acid, biotin, and choline. Washington, DC: National Academy Press; 1998.
47. Said HM. Cell and molecular aspects of human intestinal biotin absorption. J Nutr. 2009;139:158-162
48. Petrelli F, Moretti P, Paparelli M. Intracellular distribution of biotin-14C COOH in rat liver. Mol Biol Rep. 1979;4:247-252
49. Halestrap AP, Price NT. The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Biochem J. 1999;343:281-299
50. Inoue T, Stuart J, Leno R, Maki CG. Nuclear import and export signals in control of the p53-related protein p73. J Biol Chem. 2002;277:15053-15060 (Pubitemid 34952582)
51. Chauhan J, Dakshinamurti K. Role of human serum biotinidase as biotin-binding protein. Biochem J. 1988;256:265-270
52. Mock DM, Malik MI. Distribution of biotin in human plasma: most of the biotin is not bound to protein. Am J Clin Nutr. 1992;56:427-432