Skip to main content Accessibility help
×
Home

Riboflavin deprivation inhibits macrophage viability and activity – a study on the RAW 264.7 cell line

  • Agnieszka Irena Mazur-Bialy (a1), Beata Buchala (a2) and Barbara Plytycz (a2)

Abstract

Riboflavin, or vitamin B2, as a precursor of the coenzymes FAD and FMN, has an indirect influence on many metabolic processes and determines the proper functioning of several systems, including the immune system. In the human population, plasma riboflavin concentration varies from 3·1 nm (in a moderate deficiency, e.g. in pregnant women) to 10·4 nm (in healthy adults) and 300 nm (in cases of riboflavin supplementation). The purpose of the present study was to investigate the effects of riboflavin concentration on the activity and viability of macrophages, i.e. on one of the immunocompetent cell populations. The study was performed on the murine monocyte/macrophage RAW 264.7 cell line cultured in medium with various riboflavin concentrations (3·1, 10·4, 300 and 531 nm). The results show that riboflavin deprivation has negative effects on both the activity and viability of macrophages and reduces their ability to generate an immune response. Signs of riboflavin deficiency developed in RAW 264.7 cells within 4 d of culture in the medium with a low riboflavin concentration (3·1 nm). In particular, the low riboflavin content reduced the proliferation rate and enhanced apoptotic cell death connected with the release of lactate dehydrogenase. The riboflavin deprivation impaired cell adhesion, completely inhibited the respiratory burst and slightly impaired phagocytosis of the zymosan particles. In conclusion, macrophages are sensitive to riboflavin deficiency; thus, a low riboflavin intake in the diet may affect the immune system and may consequently decrease proper host immune defence.

  • View HTML
    • Send article to Kindle

      To send this article to your Kindle, first ensure no-reply@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about sending to your Kindle. Find out more about sending to your Kindle.

      Note you can select to send to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be sent to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

      Find out more about the Kindle Personal Document Service.

      Riboflavin deprivation inhibits macrophage viability and activity – a study on the RAW 264.7 cell line
      Available formats
      ×

      Send article to Dropbox

      To send this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Dropbox.

      Riboflavin deprivation inhibits macrophage viability and activity – a study on the RAW 264.7 cell line
      Available formats
      ×

      Send article to Google Drive

      To send this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Google Drive.

      Riboflavin deprivation inhibits macrophage viability and activity – a study on the RAW 264.7 cell line
      Available formats
      ×

Copyright

Corresponding author

*Corresponding author: A. I. Mazur-Bialy, fax +48 12 421 93 51, email agnieszka.mazur@uj.edu.pl

References

Hide All
1Powers, HJ (2003) Riboflavin (vitamin B-2) and health. Am J Clin Nutr 77, 13521360.
2McDowell, LR (2000) Vitamins in Animal and Human Nutrition, 2nd ed., pp. 311346. Ames: IA: Iowa State University Press.
3Hustad, S, McKinley, MC, McNutly, H, et al. (2002) Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after low-dose riboflavin supplementation. Clin Chem 48, 15711577.
4Zempleni, J, Galloway, JR & McCormick, DB (1996) Pharmacokinetics and utilization of orally and intravenously administered riboflavin in healthy humans. Am J Clin Nutr 63, 5466.
5Zempleni, J, Link, G & Bitsch, I (1995) Intrauterine vitamin B2 uptake of preterm and full-term infants. Pediatr Res 38, 585591.
6Depeint, F, Bruce, WR, Shangari, N, et al. (2006) Mitochondrial function and toxicity: role of the B vitamin family on mitochondrial energy metabolism. Chem Biol Interact 163, 94112.
7Camporeale, G & Zempleni, J (2003) 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 133, 668672.
8Manthey, KC, Chew, YC & Zempleni, J (2005) Riboflavin deficiency impairs oxidative folding and secretion of apolipoprotein B-100 in HepG2 cells, triggering stress response systems. J Nutr 135, 978982.
9Werner, R, Manthey, KC, Griffin, JB, et al. (2005) HepG2 cells develop signs of riboflavin deficiency within 4 days of culture in riboflavin-deficient medium. J Nutr Biochem 16, 617624.
10Bertollo, CM, Oliveira, ACP, Rocha, LTS, et al. (2006) Characterization of the antinociceptive and anti-inflammatory activities of riboflavin in different experimental models. Eur J Pharmacol 547, 184191.
11Mazur, AI, Kolaczkowska, E & Plytycz, B (2008) Anti-inflammatory effects of riboflavin and morphine on zymosan-induced peritonitis in Swiss mice. Cent Eur J Immunol 33, 98101.
12Mazur-Bialy, AI, Majka, A, Wojtas, L, et al. (2011) Strain-specific effects of riboflavin supplementation on zymosan-induced peritonitis in C57BL/6J, BALB/c and CBA mice. Life Sci 88, 265271.
13Toyosawa, T, Suzuki, M, Kodama, K, et al. (2004) Effects of intravenous infusion of highly purified vitamin B2 on lipopolysaccharide-induced shock and bacterial infection in mice. Eur J Pharmacol 492, 273280.
14Araki, S, Suzuki, M, Fujimoto, M, et al. (1995) Enhancement of resistance to bacterial infection in mice by vitamin B2. J Vet Med Sci 57, 599602.
15Wertman, KF & Sypherd, PS (1960) The effects of riboflavin deficiency on phagocytosis and susceptibility to infection. J Immunol 85, 511515.
16Pelliccione, NJ, Karmali, R, Rivlin, RS, et al. (1985) Effects of riboflavin deficiency upon prostaglandin biosynthesis in rat kidney. Prostag Leukotr Med 17, 349358.
17Graham, S & Secombes, CJ (1988) The production of macrophage-activating factor from rainbow trout Salomon gairdneri leukocytes. Immunology 65, 293297.
18Gordon, S (1999) Macrophages and the immune system. In Fundamental Immunology, pp. 533545 [William, PW, editor]. Philidelphia, PA: Lippincott-Raven Publishers.
19Manthey, KC, Rodriguez-Melendez, R, Tse Hoi, J, et al. (2006) Riboflavin deficiency causes protein and DNA damage in HepG2 cells, triggering arrest in G1 phase of the cell cycle. J Nutr Biochem 17, 250256.
20Brewer, JW & Diehl, JA (2000) PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc Natl Acad Sci U S A 97, 1262512630.
21Majno, G & Joris, I (1995) Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol 146, 315.
22Ishaque, A & Al-Rubeai, M (2002) Role of vitamins in determining apoptosis and extent of suppression by bcl-2 during hybridoma cell culture. Apoptosis 7, 231239.
23Zempleni, J & Mock, DM (2000) Proliferation of peripheral blood mononuclear cells increases riboflavin influx. Proc Soc Exp Biol Med 225, 7279.
24Hart, SP, Ross, JA, Ross, K, et al. (2000) Molecular characterization of the surface of apoptotic neutrophils: implications for functional downregulation and recognition by phagocytes. Cell Death Differ 7, 493503.
25Tummala, PE, Chen, XL & Medford, RM (2000) NF-kappa B independent suppression of endothelial vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 gene expression by inhibition of flavin binding proteins and superoxide production. J Mol Cell Cardiol 32, 14991508.
26Jessop, CE, Chakravarthi, S, Garbi, N, et al. (2007) ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J 26, 2840.
27Yazdanpanah, B, Wiegmann, KM, Tchikov, V, et al. (2010) Riboflavin kinase couples TNF receptor 1 to NADPH oxidase. Nature 460, 11591163.

Keywords

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed