PKC Is a Target to Modulate the Expression of Receptor Mediated Endocytosis (RME) Mice Macrophages BALB/c for Optimizing the Phagocytosis toward Candida albicans — Oak Academic Publishing
Research ArticleOpen AccessGoogle Scholar indexed
PKC Is a Target to Modulate the Expression of Receptor Mediated Endocytosis (RME) Mice Macrophages BALB/c for Optimizing the Phagocytosis toward Candida albicans
Department of Dental and Oral Disease, Faculty of Medicine, University of Sebelas Maret, Surakarta, Indonesia
,
Departement of Pathobiology, Faculty of Medicine, University of Airlangga, Surabaya, Indonesia
,
Department of Biology, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
,
Department of Pharmacy, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
,
Department of Biology, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
,
Department of Biology, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
,
Departement of Pathobiology, Faculty of Medicine, University of Airlangga, Surabaya, Indonesia
1 Department of Dental and Oral Disease, Faculty of Medicine, University of Sebelas Maret, Surakarta, Indonesia
2 Departement of Pathobiology, Faculty of Medicine, University of Airlangga, Surabaya, Indonesia
3 Department of Biology, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
4 Department of Pharmacy, Faculty of Mathematics and Natural Science, University of Sebelas Maret, Surakarta, Indonesia
Introduction: The existence of receptor-mediated endocytosis (RME) means that selectivity and selectivity occurs in capturing macromolecules. Protein kinase C (PKC) which can be expressed by almost all cells are proteins important in signal transduction groove that plays a role in a number of cell activity, e.g. phagocytosis. Aims: The purpose of this study is to determine the expression of RME after modulating the PKC which is characterized by the number of Candida albicans cells attached to the surface of macrophages. Methods: Peritoneal macrophages cultured BALB/c mice are treated with PMA and/or bisindolylmaleimides of providing levels of 5 ng/ml to 100 ng/ml for 10 minutes. Then immediately insert Candida albicans and observe every 30 minutes for 120 minutes. The research design used the same subject. Data collected in the form of number of Candida albicans cells attached to the surface of macrophages are analyzed with ANOVA statistical test (one way) to show the differences between treatments. Results: The test shows statistically significant difference in the number of Candida albicans cells attached to the surface of macrophages after administration of various levels of PMA (p < 0.001). The higher level of PMA is given, the more active the PKC is, the more RME are formed, the more Candida albicans cells attached to the surface of macrophages. Another result shows statistically significant difference in the number of Candida albicans cells attached to the surface of macrophages after administration of various levels of bisindolylmaleimides (p < 0.001). The higher level of bisindolylmaleimide is given, the less active PKC is, and the less RME are formed, the less Candida albicans cells attached to the surface of macrophages. Conclusion: Research shows that activator PKC (PMA) can increase the expression of RME on macrophages. Another research shows that inhibitor PKC (bisindolylmaleimides) can decrease the expression of RME on macrophages.
KeywordsPMABisindolylmaleimidesRMEPKCPhagocytosis
P. E. Driedger and P. M. Blumberg, “Specific Binding of Phorbol Ester Tumor Promoters,” Proceedings of the National Academy of Sciences of the United States of America, Vol. 77, No. 1, 1980, pp. 567-571. http://dx.doi.org/10.1073/pnas.77.1.567
J. A. Swanson, “Phorbol Ester Stimulate Macropinocytosis and Solute Flow through Macrophages,” Journal of Cell Science, Vol. 94, 1989, pp. 135-142.
G. Karp, “Cell and Molecular Biology: Concepts and Experiments,” John Wiley & Sons Inc., New York, 1996.
D. Toullec, P. Pianetti, H. Coste, P. Belleverque, T. Grand-Perret, M. Ajakene, V. Baudet, P. Boissin, E. Boursier, F. Lariolle, L. Duhamel, T. Charon and J. Kirilovski, “The Bisindolylmaleimide GF 109203X Is a Potent and Selective Inhibitor of Protein Kinase C,” The Journal of Biological Chemistry, Vol. 266, No. 24, 1991, pp. 15771-15781.
D. Male, “Immunology and Illustrated Outline,” 2nd Edition, Mosby, London, 1994.
R. A. Bit, P. D. Davis, L. H. Elliott, W. Harris, C. H. Hill, E. Keech, H. Kumar, G. Lawton, A. Maw and J. S. Nixon, “Inhibitors of Protein Kinase C. 3. Potent and Highly Selective Bisindolylmaleimides by Conformational Restriction,” Journal of Medicinal Chemistry, Vol. 36, No. 1, 1993, pp. 21-29. http://dx.doi.org/10.1021/jm00053a003
S. Jaken, “Protein Kinase C Isoenzymes and Substrates,” Current Opinion in Cell Biology, Vol. 8, No. 2, 1996, pp. 168-173. http://dx.doi.org/10.1016/S0955-0674(96)80062-7
H. Fukasawa, M. Yamaguchi, Y. Hashimoto, Y. Endo, K. Shudo, “Enhancing Effect of Tumor Promoters, Phorbol Esters and Teleocidins on Nuclear Receptor-Mediated Transcription,” Biological and Pharmatical Bulletin, Vol. 23, No. 12, 2000, pp. 1414-1417. http://dx.doi.org/10.1248/bpb.23.1414
D. Mochly-Rosen, K. Das and K. V. Grimes, “Protein Kinase C, an Elusive Therapeutic Target?” Nature Review Drug Discovery, Vol. 11, No. 12. 2012, pp. 937-957. http://dx.doi.org/10.1038/nrd3871
S. X. Atwood, M. Li, A. Lee, J. Y. Tang and A. E. Oro, “GLI Activation by Atypical Protein Kinase C ι/λ Regulates the Growth of Basal Cell Carcinomas,” Nature, Vol. 494, No. 7438, 2013, pp. 484-488. http://dx.doi.org/10.1038/nature11889
G. T. Strickland, “Hunter’s Tropical Medicine,” 7th Edition, W. B. Saunders Company, Philadelphia, 1991.
F. S. Rosen, L. A. Steiner and E. R. Unanue, “Macmillan Dictionary of Immunology,” Macmillan Reference Books, London and Basingstoke, 1989.
D. P. Stites and A. I. Terr, “Basic Human Immunology,” 1st Edition, Prentice-Hall International Inc., Upper Saddle River, 1991, pp. 34-44.
I. Roitts, J. Brostoff and D. Male, “Immunology,” 3rd Edition, Mosby, St. Louis, 1993, pp.1-22.
C. R. Young and C. J. Welsh, “Stress, Health, and Disease,” Cell Science, Vol. 2, No. 2, 2005, pp. 132-158.
E. H. Vogel, M. E. Castro, P. A. Solar and F. A. Soto, “Enhancement of Pavlovian Conditioned Immunosuppression in Rats,” Acta Neurobiologie Experimentalis, Vol. 67, No. 1, 2007, pp. 71-81.
W. A. Dunn and A. L. Hubbard, “Receptor-Mediated Endocytosis of Epidermal Growth Factor by Hepatocytes in the Perfused Rat Liver: Ligand and Receptor Dynamics,” The Journal of Cell Biology, Vol. 98, No. 6, 1984, pp. 2148-2159. http://dx.doi.org/10.1083/jcb.98.6.2148
J. Feger, S. Gil-Falgon and C. Lamaze, “Cell Receptors: Definition, Mechanisms and Regulation of Receptor-Mediated Endocytosis,” Celluler and Molecular Biology, Vol. 40, No. 8, 1994, pp. 1039-1061.
H. S. Thatte and S. L. Schrier, “Comparison of Transferrin Receptor-Mediated Endocytosis and Drug-Induced Endocytosis in Human Neonatal and Adult RBCs,” Blood, Vol. 72, No. 5, 1988, pp. 1693-1700.
A. Dautry-Varsat, “Receptor-Mediated Endocytosis: the Intracellular Journey of Transferrin and Its Receptor,” Biochimie, Vol. 68, No. 3, 1986, pp. 375-381. http://dx.doi.org/10.1016/S0300-9084(86)80004-9
A. A. Khine and C. A. Lingwood, “Capping and Receptor-Mediated Endocytosis of Cell-Bound Verotoxin (Shiga-Like Toxin). 1: Chemical Identification of an Amino Acid in the B Subunit Necessary for Efficient Receptor Glyco- lipid Binding and Cellular Internalization,” Journal of Cellular Biology, Vol. 161, No. 2, 1994, pp. 319-332.
J. Mulholland, J. Konopka, B. Singer-Kruger, M. Zerial and D. Botstein, “Visualization of Receptor-Mediated Endocytosis in Yeast,” Molecular Biology of the Cell, Vol. 10, No. 3, 1999, pp. 799-817. http://dx.doi.org/10.1091/mbc.10.3.799
J. E. Coligan, A. M. Kruisbeek, D. A. Marquilies, E. M. Shevach, W. Strober and R. Coico, “Current Protocols in Immunology,” John Wiley & Sons. Inc., New York, 1994.
A. A. F. Machmoud, “Mononuclear Phagosytes and Resistance,” In: S. Kenneth and M. D. Warren, Eds., Immunology and Molecular Biology of Parasitic Infection, Black Well Scientific Publication, Boston, 1993. pp. 23-24.
A. Prayitno and J. B. Suparyatmo, “Changes of BALB/c Mice Macrophages Mobility after Protein Kinase C Inhibitor Administration,” Indonesian Journal of Clinical Pathology, Vol. 8, No. 1, 2000, pp. 18-22.
E. C. Larsen, T. Ueyama, P. M. Brannock, Y. Shirai, N. Saito, C. Larsson, D. Loegering, P. B. Weber and M. R. Lennattz, “A Role for PKC-ε in FcγR-Mediated Phagocytosis by RAW 264.7 Cells,” The Journal of Cell Biology, Vol. 159, No. 6, 2002, pp. 939-944. http://dx.doi.org/10.1083/jcb.200205140
S. J. Slater, M. B. Kelly, F. Taddeo, E. Rubin and C. D. Stubbs, “Evidence for Discrete Diacylglycerol and Phorbol Ester Activator Sites on Protein Kinase C. Differences in Effects of 1-Alkanol Inhibition, Activation by Phosphatidylethanolamine and Calcium Chelation,” The Journal of Biological Chemistry, Vol. 269, No. 25, 1994, pp. 17160-17165.
Y. P. Hwang, H. J. Yun, J. H. Choi, K. W. Kang and H. G. Jeong, “Suppression of Phorbol-12-myristate-13-acetate- induced Tumor Cell Invasion by Bergamottin via the Inhibition of Protein Kinase Cdelta/p38 Mitogen-Activated Protein Kinase and JNK/Nuclear Factor-KappaB-Dependent Matrix Metalloproteinase-9 Expression,” Molecular Nutrition and Food Research, Vol. 54, No. 7, 2010, pp. 977-990. http://dx.doi.org/10.1002/mnfr.200900283
G. Harmati, F. Papp, N. Szentandrassy, L. Barandi, F. Ruzsnavszky, B. Horvath, T. Banyasz, J. Magyar, G. Panyi, Z. Krasznai and P. P. Nanasi, “Effects of the PKC Inhibitors Chelerythrine and Bisindolylmaleimide I (GF 109203X) on Delayed Rectifier K+ Currents,” Maunyn- Schmiedebergs Archives of Pharmacology, Vol. 383, No. 2, 2011, pp. 141-148. http://dx.doi.org/10.1007/s00210-010-0584-8
C. Rosse, M. Linch, S. Kermorgant, A. J. Cameron, K. Boeckeler and P. J. Parker “PKC and the Control of Localized Signal Dynamics,” Nature Reviews Molecular Cell Biology, Vol. 11, No. 2, 2010, pp. 103-112. http://dx.doi.org/10.1038/nrm2847
J. W. William, B. Ernest, J. E. Allan and R. R. Wayne, “Hematology,” 2nd Edition, Mc Grow Hill Book Company, A Blakistone Publication, New York, 1977.
M. Thenawijaya, “Dasar-Dasar Biokimia,” Penerbit Erlangga, Jakarta, 1994.
A. C. Newton, “Regulation of Protein Kinase C,” Current Opinion in Cell Biology, Vol. 9, No. 2, 1997, pp. 161-167. http://dx.doi.org/10.1016/S0955-0674(97)80058-0
S. Kuchera, H. Barth, P. Jacobson, A. Metz, C. Schaechtele and D. Schrier, “Anti-Inflammatory Properties of the Protein Kinase C Inhibitor, 3-[1-[3-(Dimethylamino)- propyl]-1H-indol-3-yl]-4-(1H-indol-3-yl)-1H-pyrrole-2,5- dione Monohydrochloride (GF109203X) in the PMA- Mouse Ear Edema Model,” Agents Actions, Vol. 39, No. 1, 1993, pp. C169-C173. http://dx.doi.org/10.1007/BF01972756
T. Leppanen, “Protein Kinase C in the Regulation of Inflammatory Genes iNOS and TTP,” Academic Dissertation, Medical School of the University of Tampere, Medisiinarinkatu 3, Tampere, 2010.
S. Chand, N. Mehta, M. S. Bahia, A. Dixit and O. Silakari, “Protein Kinase C-Theta Inhibitors: A Novel Therapy for Inflammatory Disorders,” Current Pharmaceutical Design, Vol. 18, No. 30, 2012, pp. 4725-4746. http://dx.doi.org/10.2174/138161212802651625
P. Geraldes and G. L. King, “Activation of Protein Kinase C Isoforms and Its Impact on Diabetic Complications,” Circulation Research, Vol. 106, No. 8, 2010. pp. 1319- 1331. http://dx.doi.org/10.1161/CIRCRESAHA.110.217117
A. Gonelli, C. Mischiati, R. Guerrini, R. Voltan, S. Salvadori and G. Zauli, “Perspectives of Protein Kinase C (PKC) Inhibitors as Anti-Cancer Agents,” Mini Reviews in Medical Chemistry, Vol. 9, No .4, 2009, pp. 498-509. http://dx.doi.org/10.2174/138955709787847967
C. Larsson, “Protein Kinase C and the Regulation of the Actin Cytoskeleton,” Cellular Signalling, Vol. 18, No. 3, 2006, pp. 276-284. http://dx.doi.org/10.1016/j.cellsig.2005.07.010
A. M. Gonzales-Guerrico, J. Meshki, L. Xiao, F. Benavides, C. J. Conti and M. G. kazanietz, “Molecular Mechanisms of Protein Kinase C-Induced Apoptosis in Prostate Cancer Cells,” Journal of Biochemistry and Molecular Biology, Vol. 38, No. 6, 2005, pp. 639-645. http://dx.doi.org/10.5483/BMBRep.2005.38.6.639