Immunopharmacological Activity of Calcitriol Pre-Treated RAW264.7 Cell Line Stimulated by Phorbol 12-Myristate13-Acetate (PMA) and Formyl-Methionyl-Leucyl-Phenylalanine (FMLP) Agonist
American Journal of Bioscience and Bioengineering
Volume 2, Issue 4, August 2014, Pages: 55-59
Received: Sep. 7, 2014; Accepted: Sep. 15, 2014; Published: Sep. 30, 2014
Views 2591      Downloads 124
Authors
Samson Ayodeji Olofinsae, School of Health, Sport and Bioscience, University of East London, United Kingdom
Bartholomew Okechukwu Ibeh, Departments of Medical Biotechnology, National Biotechnology Development Agency, Abuja, Nigeria
Habu Josiah Bitrus, Bioresources Development Center, Odi, National Biotechnology Development Agency, Nigeria
Jatinder Ahluwalia, School of Health, Sport and Bioscience, University of East London, United Kingdom
Article Tools
Follow on us
Abstract
The study investigates the effect of calcitriol treatment on oxygen consumption rate as generated by agonist stimulation of RAW 264.7 cell lines and its usefulness in eliciting reduced oxygen consumption in high respiratory burst-dependent disease state. Phorbol 12-myristate 13-acetate (PMA) and Formyl-methionyl-leucyl-phenylalanine (FMLP) were used to artificially stimulate oxygen consumption in cultured pro-monocytic RAW264.7 cell line. Samples of the cultured cells were previously prepared with calcitriol (1, 25- Dihydroxyvitamin D3) followed by a 72-hour incubation period. The percentage oxygen consumption was measured using the Clark oxygen electrode. There was a significant increase in oxygen consumption in FMLP treated cells (P<0.05) when compared with the PMA and the control groups. The PMA calcitriol-treated cells showed 24% oxygen consumption rate more than the control while FMLP treated cells was 57% higher. The result demonstrated that calcitriol, a known stimulant used to prep most cells for agonists stimulation of oxygen consumption may serve as a physiological moderator of oxygen consumption in immune cells when co-administered with agonist (PMA and/or FMLP). This may result to increased pathogen attack in a diseased state.
Keywords
Respiratory Burst, Immunity, Oxidation, NADPH Oxidase, Promonocytes, RAW264.7, Calcitriol
To cite this article
Samson Ayodeji Olofinsae, Bartholomew Okechukwu Ibeh, Habu Josiah Bitrus, Jatinder Ahluwalia, Immunopharmacological Activity of Calcitriol Pre-Treated RAW264.7 Cell Line Stimulated by Phorbol 12-Myristate13-Acetate (PMA) and Formyl-Methionyl-Leucyl-Phenylalanine (FMLP) Agonist, American Journal of Bioscience and Bioengineering. Vol. 2, No. 4, 2014, pp. 55-59. doi: 10.11648/j.bio.20140204.11
References
[1]
Belikova I, Lukaszewicz AC, Faivre V, Damoisel C, Singer M, Payen D. “Oxygen consumption of human peripheral blood mononuclear cells in severe human sepsis”. Crit Care Med. 35(12). 2702-8.2007
[2]
Kvarstein B, Blichfeldt P. “Oxygen Consumption During Phagocytosis by Leukocytes in Patients with Rheumatic Diseases” Scand J Rheumatol.6 ( 3):148-150.1977.
[3]
Dawn Bowdish. Propagation & Culturing of Raw264.7 cells. 2013 http://www.bowdish.ca/lab/wp-content/uploads/2013/02/Culturing-RAW264.7-Cells.pdf
[4]
Dyer KD, Schellens IMM, Bonville CA, Martin BV, Domachowske JB, Rosenberg HF: “Efficient replication of pneumonia virus of mice (PVM) in a mouse macrophage cell line”. Virol Journal. 4:48-5.2007.
[5]
Rowley CA, Ikeda AK, Seidel M, Anaebere TC, Antalek MD, Seamon C, Conrey Ak, Mendelsohn L, Nichols J,Gorbach AM, Kato GJ, Ackerman H. “Microvascular oxygen consumption during sickle cell pain crisis”. Blood. 123 (20): 2014. DOI: http://dx.doi.org/10.1182/blood-2013-11-533406
[6]
Shin J-J, Wall EA, Zavzavadjian JR, Santat LA, Liu J, Hwang J-I, Rebres R, Roach T, Seaman W, Simon MI, Fraser IDC: “A single lentiviral vector platform for microRNA-based conditional RNA interference and coordinated gene expression”. Proc Natl Acad Sci USA. 103:13759-13764.2006.
[7]
Walloschke B, Fuhrmann H, Schumann J. “Macrophage cell line RAW264.7 but not P-388D1 is an appropriate in vitro-model for studying oxidative burst as well as cytokine production in context of fatty acid enrichment”. Cell Immunol. 262(1):58-61. 2010.
[8]
Xiaohui Wang, Yidong Li, Xiaoyan Zhu, Yan Wang, Fei Diao, Jian Lu. “Signal regulatory protein a1 is involved in the inhibitory effect of glucocorticoid receptor on the proliferation of murine macrophage RAW264.7 cell and mouse peritoneal macrophage”. Journal of Molecular Endocrinology. 41:393–403.2008.
[9]
Vittorina DB, Miroslawa G, Filoppo R. “Relationship between phosphorylation and translocation to the plasma membrane of p47 phox and p67 phox and activation of the NADPH oxidase in normal and Ca2+ depleted human neutrophils”. Biochem J 290:173-178.1993.
[10]
Bruce A, Johnson A, Lewis J, Raff M, Roberts K, Walters P. “Molecular Biology of the Cell” Fourth Edition. New York and London: Garland Science.2002.
[11]
Finlay B, McFadden G. “Anti-immunology: evasion of the host immune system by bacterial and viral pathogens”. Cell 124 (4): 767–82.2006.
[12]
Clark RA. “Activation of the Neutrophil Respiratory Burst Oxidase”. J Infect Dis 179(S 2): S309-S317. 1999.
[13]
Simchowitz L, Atkinson JP, Spilberg I, Arthritis Rheum. “Stimulation of the respiratory burst in human neutrophils by crystal phagocytosis”. Arthritis Rheum. 2:181-8.1982.
[14]
DeLeo FR, Quinn MT. “Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins”. J Leukocyte Biol. 60:677-9.1996.
[15]
Narayanan PK, Carter WO, Ganey PE, Roth RA, Voytik-Harbin SL, Robinson JP. “Impairment of human neutrophil oxidative burst by polychlorinated biphenyls: inhibition of superoxide dismutase activity”. J Leukocyte Bio. 63: 216-224.1998.
[16]
Mates JM, Perez-Gomez C, Blanca M. “Chemical and biological activity of free radical scavengers’ in allergic diseases”. Clinica Chimica Acta. 296: 1–15.2000.
[17]
Jiang F, Zhang Y, Dusting GJ. “NADPH Oxidase-Mediated Redox Signaling: Roles in Cellular Stress Response, Stress Tolerance, and Tissue Repair”. Pharmacol Rev 63(1): 218-242.2011.
[18]
Griendling KK, Sorescu D, Ushio-Fukai M. “NAD(P)H oxidase: role in cardiovascular biology and disease”. Circ Res. 86: 494–501.2000.
[19]
Lambeth JD. “NOX enzymes and the biology of reactive oxygen”. Nat Rev Immunol. 4:181–189.2004
[20]
Diepart C, Verrax J, Calderonb JB, Feronc O, Jordana BF, Gallez B. “Comparison of methods for measuring oxygen consumption in tumor cells in vitro”. Anal Biochem. 396 : 250–256.2010.
[21]
Dragavon J, Molter T, Young C, Strovas T, McQuaide S, Holl M, Zhang M, Cookson B, Alex Jen A, Lidstrom M, Meldrum D,Burgess L. “A cellular isolation system for real-time single-cell oxygen consumption monitoring.” J. R. Soc. Interface 25 ( Suppl 2 ): S151-S159.2008.
[22]
White C, Kambe T, Fulcher YG, Sachdev SW,2 Bush AI, Fritsche K,4 Lee J, Quinn TP, Petris MJ. “Copper transport into the secretory pathway is regulated by oxygen in macrophages”. J Cell Sci. 122(9): 1315–1321.2009.
[23]
Suh C, Stull ND, Li XJ, Tian W, Price MO, Grinstein S, Yaffe MB, Atkinson S, Dinauer, MC. “The phosphoinositide-binding protein p40phox activates the NADPH oxidase during Fc gammer IIA receptor–induced phagocytosis”. JEM . 203(8): 1915-1925.2006.
[24]
Shiose A, Sumitomo H. Arachidonic acid and phosphorylation synergistically induce a conformational change of p47 phox to activate the phagocyte NADPH oxidase. J Biol Chem. 275: 13793–801.2000.
[25]
Heinloth, Heermeier K, Raff U, Wanner C, Galle J. Stimulation of NADPH oxidase by oxidized low-density lipoprotein induces proliferation of human vascular endothelial cells. J Am Soc Nephrol. 11:1819-1825.2001.
[26]
Schwende H, Fitzke E, Ambs P, Dieter P. “Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1, 25-dihydroxyvitamin D3”. J Leukocyte Biol. 59: 555-561.1996.
[27]
Mark C, Philip M, Thomas LL, Ji-Liang G. “The N-formylpeptide receptor (FPR) and a second Gi-coupled receptor mediate fMet–Leu–Phe-stimulated activation of NADPH oxidase in murine neutrophils”. Cellular immunology. 218(2): 7-12.2002.
[28]
Selvatici R, Falzarano S, Mollica A, Spisani S. “Signal transduction pathwas triggered by selective formylpeptide analogues in human neutrophils”. Eur. J. Pharmacol. 534:1-11.2006.
[29]
Mills JS., Miettinen HM, Jesaitis AJ. “The N-formyl peptide receptor: structure, signaling, and disease”. C. N. Serhan, and P. A. Ward, eds. Molecular and Cellular Basis of Inflammation 215-246. Humana Press, Totowa.1999.
[30]
Shiose A, Sumitomo H. “Arachidonic acid and phosphorylation synergistically induce a conformational change of p47 phox to activate the phagocyte NADPH oxidase”. J Biol Chem. 275: 13793–801.2000.
[31]
Tam TW, Akhtar H, Arnason1 JT, Cvijovic K, Boon H, Cameron DW, EDrouin C, Jaeger W, Tsuyuki RT, Vohra S, Foster BC. “Inhibition of Human Cytochrome P450 Metabolism by Blended Herbal Products and Vitamins”. J Pharm Pharmaceut Sci. 14(1): 1-16.2011.
[32]
Ellis JA, Mayer SJ, Jones OT. “The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbial activities of human neutrophils”. Biochem J. 251(3) 887-891.1988.
[33]
Valerie BO, David GT, Owen TG, Paul J. “Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase”. Biochem. J. 290(1):41-49.1993.
ADDRESS
Science Publishing Group
1 Rockefeller Plaza,
10th and 11th Floors,
New York, NY 10020
U.S.A.
Tel: (001)347-983-5186