Interleukin-2 receptor-γ-dependent endocytosis depends on biotin in jurkat cells

American Journal of Physiology - Cell Physiology

Volumn 284, Issue 2 53-2, 2003, Pages

  Rodriguez Melendez, Rocio ^a   Camporeale, Gabriela ^a   Griffin, Jacob B ^a   Zempleni, Janos ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Cytokines; Gene expression; Propionyl CoA carboxylase

Indexed keywords

BIOTIN; GENISTEIN; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR;

ARTICLE; CONTROLLED STUDY; CYTOKINE RELEASE; ENDOCYTOSIS; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; IMMUNOCOMPETENT CELL; INTERNALIZATION; LEUKEMIA CELL LINE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

EID: 0037302162     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00365.2002     Document Type: Article

References (46)

1. 3: direct inhibition of NFATp/AP-1 complex formation by a nuclear hormone receptor. Mol Cell Biol 15: 5789-5799, 1995.
2. Arcari P, Martinelli R, and Salvatore F. The complete sequence of a full length cDNA for liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species. Nucleic Acids Res 12: 9179-9189, 1984.
3. Báez-Saldaña A, Díaz G, Espinoza B, and Ortega E. Biotin deficiency induces changes in subpopulations of spleen lymphocytes in mice. Am J Clin Nutr 67: 431-437, 1998.
4. Borboni P, Magnaterra R, Rabini RA, Staffolani R, Porzio O, Sesti G, Fusco A, Mazzanti L, Lauro R, and Marlier LN. Effect of biotin on glucokinase activity, mRNA expression and insulin release in cultured beta-cells. Acta Diabetol 33: 154-158, 1996.
5. Butscher WG, Haggerty CM, Chaudhry S, and Gardner K. Targeting of p300 to the interleukin-2 promoter via CREB-Rel cross-talk during mitogen and oncogenic molecular signaling in activated T cells. J Biol Chem 276: 27647-27656, 2001.
6. Chauhan J and Dakshinamurti K. Transcriptional regulation of the glucokinase gene by biotin in starved rats. J Biol Chem 266: 10035-10038, 1991.
7. Cowan MJ, Wara DW, Packman S, Yoshino M, Sweetman L, and Nyhan W. Multiple biotin-dependent carboxylase deficiencies associated with defects in T-cell and B-cell immunity. Lancet 2: 115-118, 1979.
8. Dakshinamurti K and Chauhan J. Biotin-binding proteins. In: Vitamin Receptors: Vitamins as Ligands in Cell Communication, edited by Dakshinamurti K. Cambridge, UK: Cambridge Univ. Press, 1994.
9. Dakshinamurti K and Cheah-Tan C. Liver glucokinase of the biotin deficient rat. Can J Biochem 46: 75-80, 1968.
10. Dakshinamurti K and Litvak S. Biotin and protein synthesis in rat liver. J Biol Chem 245: 5600-5605, 1970.
11. Fujita T, Shibuya H, Ohashi T, Yamanishi K, and Taniguchi T. Regulation of human interleukin-2 gene: functional DNA sequences in the 5′-flanking region of the gene expression in activated T lymphocytes. Cell 46: 401-407, 1986.
12. Gnarra JR, Otani H, Wang MG, McBride OW, Sharon M, and Leonard WJ. Human interleukin 2 receptor β-chain gene: chromosomal localization and identification of 5′ regulatory sequences. Proc Natl Acad Sci USA 87: 3440-3444, 1990.
13. Griffin JB, Stanley JS, and Zempleni J. Synthesis of a rabbit polyclonal antibody to the human sodium-dependent multivitamin transporter. Int J Vitam Nutr Res 72: 195-198, 2002.
14. Hatakeyama M, Tsudo M, Minamoto S, Kono T, Doi T, Miyata T, Miyasaka M, and Taniguchi T. Interleukin-2 receptor β chain gene: generation of three receptor forms by cloned human α and β chain cDNAs. Science 244: 551-556, 1989.
15. Hemar A and Dautry-Varsat A. Cyclosporin A inhibits the interleukin 2 receptor α chain gene transcription but not its cell surface expression: the α chain stability can explain this discrepancy. Eur J Immunol 20: 2629-2635, 1990.
16. Hentsch B, Mouzaki A, Pfeuffer I, Rungger D, and Serfling E. The weak, fine-tuned binding of ubiquitous transcription factors to the IL-2 enhancer contributes to its T cell-restricted activity. Nucleic Acids Res 20: 2657-2665, 1992.
17. Klein J and Horejsi V. Immunology. Oxford, UK: Blackwell Science, 1997.
18. Kumar M and Axelrod AE. Cellular antibody synthesis in thiamin, riboflavin, biotin and folic acid-deficient rats. Proc Soc Exp Biol Med 157: 421-423, 1978.
19. Lewis B, Rathman S, and McMahon R. Dietary biotin intake modulates the pool of free and protein-bound biotin in rat liver. J Nutr 131: 2310-2315, 2001.
20. Maeda Y, Kawata S, Inui Y, Fukuda K, Igura T, and Matsuzawa Y. Biotin deficiency decreases ornithine transcarbamylase activity and mRNA in rat liver. J Nutr 126: 61-66, 1996.
21. Manthey KC, Griffin JB, and Zempleni J. Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells. J Nutr 132: 887-892, 2002.
22. Mock DM. Determinations of biotin in biological fluids. Methods Enzymol 279: 265-275, 1997.
23. Mock DM, Lankford GL, and Mock NI. Biotin accounts for only half of the total avidin-binding substances in human serum. J Nutr 125: 941-946, 1995.
24. Mock DM and Mock NI. Lymphocyte propionyl-CoA carboxylase is an early and sensitive indicator of biotin deficiency in rats, but urinary excretion of 3-hydroxypropionic acid is not. J Nutr 132: 1945-1950, 2002.
25. c chain. J Biol Chem 273: 22044-22051, 1998.
26. National Research Council. Dietary reference intakes for thiamin, riboflavin, niacin, vitamin B-6, folate, vitamin B-12, pantothenic acid, biotin, and choline. In: Recommended Dietary Allowances, edited by Food and Nutrition Board. Washington, DC: National Academy, 1998.
27. Ohbo K, Takasawa N, Ishii N, Tanaka N, Nakamura M, and Sugamura K. Functional analysis of the human interleukin-2 receptor γ chain promoter. J Biol Chem 270: 7479-7486, 1995.
28. Petrelli F, Moretti P, and Campanati G. Studies on the relationships between biotin and the behaviour of B and T lymphocytes in the guinea pig. Experientia 37: 1204-1206, 1981.
29. Pruzansky J and Axelrod AE. Antibody production to diphtheria toxoid in vitamin deficiency states. Proc Soc Exp Biol Med 89: 323-325, 1955.
30. Rabin BS. Inhibition of experimentally induced autoimmunity in rats by biotin deficiency. J Nutr 113: 2316-2322, 1983.
31. c chains with Jak1 and Jak3: implications for XSCID and XCID. Science 266: 1042-1045, 1994.
32. SAS Institute. StatView Reference. Cary, NC: SAS, 1999.
33. Solorzano-Vargas RS, Pacheco-Alvarez D, and 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 99: 5325-5330, 2002.
34. Spence JT and Koudelka AP. Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes. J Biol Chem 259: 6393-6396, 1984.
35. Stanley JS, Griffin JB, and Zempleni J. Biotinylation of histones in human cells: effects of cell proliferation. Eur J Biochem 268: 5424-5429, 2001.
36. Subtil A and Dautry-Varsat A. Several weak signals in the cytosolic and transmembrane domains of the interleukin-2-receptor β chain allow for its efficient endocytosis. Eur J Biochem 253: 525-530, 1998.
37. Sugamura K, Asao H, Kondo M, Tanaka N, Ishii N, Ohbo K, Nakamura M, and Takeshita T. The interleukin-2 receptor γ chain: its role in the multiple cytokine receptor complexes and T cell development in XSCID. Annu Rev Immunol 14: 179-205, 1996.
38. Takeshita T, Asao H, Ohtani K, Ishii N, Kumaki S, Tanaka N, Munakata H, Nakamura M, and Sugamura K. Cloning of the γ chain of the human IL-2 receptor. Science 257: 379-382, 1992.
39. Taniguchi T and Minami Y. The IL-2/IL-2 receptor system: a current overview. Cell 73: 5-8, 1993.
40. Wolffe A. Chromatin. San Diego: Academic, 1998.
41. Yu A and Malek TR. The proteasome regulates receptor-mediated endocytosis of interleukin-2. J Biol Chem 276: 381-385, 2001.
42. Yu A, Olosz F, Choi CY, and Malek TR. Efficient internalization of IL-2 depends on the distal portion of the cytoplasmic tail of the IL-2R common γ-chain and a lymphoid cell environment. J Immunol 165: 2556-2562, 2000.
43. Zempleni J, Helm RM, and Mock DM. In vivo biotin supplementation at a pharmacologic dose decreases proliferation rates of human peripheral blood mononuclear cells and cytokine release. J Nutr 131: 1479-1484, 2001.
44. Zempleni J and Mock DM. Uptake and metabolism of biotin by human peripheral blood mononuclear cells. Am J Physiol Cell Physiol 275: C382-C388, 1998.
45. Zempleni J, Stanley JS, and Mock DM. Proliferation of peripheral blood mononuclear cells causes increased expression of the sodium-dependent multivitamin transporter gene and increased uptake of pantothenic acid. J Nutr Biochem 12: 465-473, 2001.
46. Zempleni J, Trusty TA, and Mock DM. Lipoic acid reduces the activities of biotin-dependent carboxylases in rat liver. J Nutr 127: 1776-1781, 1997.