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 JBM  Vol.6 No.5 , May 2018
Description of Hemoproteins and Elemental Homeostasis in Brain Tumors
Abstract: The role of element homeostasis in neoplastic disease pathogenesis is be-yond question. The imbalance of trace elements precisely underlies the ini-tiation and promotion of tumor pathology. The aim of the study was to in-vestigate blood and tissue macroelements, microelements and hemoproteins level in brain tumors and their intermolecular interactions. Samples of blood and brain tumor tissues were investigated. Detection of myoglobin level was implemented by the reaction of passive hemagglutination and immunoturbidimetric test. Catalase activity was determined by the method of Beer and Sizer. Free radical activity was determined by the method of induced biochemiluminescence. Microelements level was investigated by usage of atomic emission spectrometry. To build the networks of studied hemoprotein interactions with signaling pathways of proteins, expressed in brain tumors, molecular interaction databases (STRING, BioGrid) were used. Modern databases of signaling pathways (KEGG) suggest that in normal cells hypoxia can lead to HIF-1A protein synthesis. ROS synthesis inhibits the PHD enzyme and triggers the release of calcium ions, and increases proliferation. Calcium ions are triggering factor of apoptosis and cell proliferation. Myoglobin can possibly be the cell adaptation factor towards hypoxia, oxidative stress and element homeostasis violation, and myoglobin level decreasing can additionally stimulate proliferation, by apoptosis inhibition.
Cite this paper: I. Erlykina, E. , M. Obukhova, L. , A. Medyanik, I. , S. Yashin, K. , G. Pimenov, V. , I. Evdokimov, I. , V. Barinova, O. and B. Yazykova, A. (2018) Description of Hemoproteins and Elemental Homeostasis in Brain Tumors. Journal of Biosciences and Medicines, 6, 89-96. doi: 10.4236/jbm.2018.65010.
References

[1]   Fazeny-Dorner, B., Wenzel, C., Veitl, M., Piribauer, M., Rossler, K. and Dieckmann, K. (2003) Survival and Prognostic Factors of Patients with Unresectable Glioblastoma Multiforme. Anti-Cancer Drug, 14, 305-312.
https://doi.org/10.1097/00001813-200304000-00008

[2]   Gresner, P., Gromadzinska, J., Jablonska, E., Kaczmarski, J. and Wasowicz, W. (2009) Expression of Selenoprotein-Coding Genes SEPP1, SEP15 and hGPX1 in Non-Small Cell Lung Cancer. Lung Cancer, 65, 34-40.
https://doi.org/10.1016/j.lungcan.2008.10.023

[3]   Valko, M., Rhodes, C.J., Moncol, J., Izakovic, M. and Mazur, M. (2006) Free Radicals, Metals and Antioxidants in Oxidative Stress-Induced Cancer. Chemico-Biological Interactions, 160, 1-40.
https://doi.org/10.1016/j.cbi.2005.12.009

[4]   Georg, B. (2015) Increasing the Endogenous NO Level Causes Catalase Inactivation and Reactivation of Intercellular Apoptosis Signaling Specifically in Tumor Cells. Redox Biology, 6, 353-371.
https://doi.org/10.1016/j.redox.2015.07.017

[5]   Kanatous, S.B. and Mammen, P.P.A. (2010) Regulation of Myoglobin Expression. Journal of Experimental Biology, 213, 2741-2747. https://doi.org/10.1242/jeb.041442

[6]   Flonta, S., Arena, S., Pisacane, A., Michieli, P. and Bardelli, A. (2009) Expression and Functional Regulation of Myoglobin in Epithelial Cancers. American Journal of Pathology, 175, 201.
https://doi.org/10.2353/ajpath.2009.081124

[7]   Kristiansen, G., Hu, J., Wichmann, D., Stiehl, D.P., Rose, M., Gerhardt, J., Bohnert, A., ten Haaf, A., Moch, H., Raleigh, J., Varia, M.A., Subarsky, P., Scandurra, F.M., Gnaiger, E., Gleixner, E., Bicker, A., Gassmann, M., Hankeln, T., Dahl, E. and Gorr, T.A. (2011) Endogenous Myoglobin in Breast Cancer Is Hypoxia-Inducible by Alternative Transcription and Functions to Impair Mitochondrial Activity: A Role in Tumor Suppression? The Journal of Biological Chemistry, 286, 43417-434128. https://doi.org/10.1074/jbc.M111.227553

[8]   Mair, J., Artner-Dworzak, E., Lechleitner, P., Morass, B., Smidt, J., Wagner, I., et al. (1992) Early Diagnosis of Acute Myocardial Infarction by a Newly Developed Rapid Immunoturbidimetric Assay for Myoglobin. British Heart Journal, 68, 462-468.
https://doi.org/10.1136/hrt.68.11.462

[9]   Zaninotto, M., Altinier, S., Lachin, M., Celegon, L. and Plebani, M. (1999) Strategies for the Early Diagnosis of Acute Myocardial Infarction Using Biochemical Markers. American Journal of Pathology, 111, 399-405. https://doi.org/10.1093/ajcp/111.3.399

[10]   Erlykina, Е.I., Kopytova, Т.V., Alyasova, А.V., Gorshkova, T.N., Terentiev, I.G., Pimenov, V.G., Evdokimov, I.I. and Obukhova, L.M. (2013) Integral Analysis of Blood Plasma Biochemical Parameters as an Optimizing Diagnostic Technique of Epithelial Tissue Malignant Neoplasms. Modern Technologies in Medicine, 5, 51-55.

[11]   Meng, Q.H. and Wagar, E.A. (2014) Laboratory Approaches for the Diagnosis and Assessment of Hypercalcemia. Critical Reviews in Clinical Laboratory Sciences, 20, 1-13.

[12]   Vivanco, I. and Sawyers, C.L. (2002) The Phosphatidylinositol 3 Kinase AKT Pathway in Human Cancer. Nature Reviews. Cancer, 2, 489-501.
https://doi.org/10.1038/nrc839

[13]   Huang, C.Y., Hsieh, Y.L., Ju, D.T., Lin, C.C., Kuo, C.H., Liou, Y.F., Ho, T.J., Tsai, C.H., Tsai, F.J. and Lin, J.Y. (2015) Attenuation of Magnesium Sulfate on CoCl2-Induced Cell Death by Activating ERK1/2/MAPK and Inhibiting HIF-1α via Mitochondrial Apoptotic Signaling Suppression in a Neuronal Cell Line. The Chinese Journal of Physiology, 58, 244-253.
https://doi.org/10.4077/CJP.2015.BAD296

[14]   Lecuyer, M., Rubio, M., Chollat, C., Lecointre, M., Jégou, S., Leroux, P., Cleren, C., Leroux-Nicollet, I., Marpeau, L., Vivien, D., Marret, S. and Gonzalez, B.J. (2017) Experimental and Clinical Evidence of Differential Effects of Magnesium Sulfate on Neuroprotection and Angiogenesis in the Fetal Brain. Pharmacology Research & Perspectives, 5, No. 4.
https://doi.org/10.1002/prp2.315

[15]   Torii, S., Kobayashi, K., Takahashi, M., Katahira, K., Goryo, K., Matsushita, N., Yasumoto, K., Fujii-Kuriyama, Y. and Sogawa, K. (2009) Magnesium Deficiency Causes Loss of Response to Intermittent Hypoxia in Paraganglion Cells. The Journal of Biological Chemistry, 284, 19077-19089. https://doi.org/10.1074/jbc.M109.004424

[16]   Popov, B., Gadjeva, V., Valkanov, P. and Tolekova, A. (2000) Lipid Peroxidation, Superoxide Dismutase and Catalase Activities in Brain Tumor Tissues. Archives of Physiology and Biochemistry, 111, 455-459.
https://doi.org/10.3109/13813450312331342328

[17]   Liou, G.-Y. and Storz, P. (2010) Reactive Oxygen Species in Cancer. Free Radical Research, 44, 479-496. https://doi.org/10.3109/10715761003667554

[18]   Ke, Q.D. and Max, C. (2006) Hypoxia-Inducible Factor-1 (HIF-1). Molecular Pharmacology, 70, 1469-1480. https://doi.org/10.1124/mol.106.027029

[19]   Fraser, J., de Mello, L.V., Ward, D., Rees, H.H., Williams, D.R., Fang, Y., Brass, A., Gracey, A.Y. and Cossins, A.R. (2006) Hypoxia-Inducible Myoglobin Expression in Nonmuscle Tissues. Proceedings of the National Academy of Sciences of the United States of America, 103, 2977-2981. https://doi.org/10.1073/pnas.0508270103

[20]   Huang, L.E., Gu, J., Schau, M. and Bunn, H.F. (1998) Regulation of Hypoxia-Inducible Factor 1alpha Is Mediated by an O2-Dependent Degradation Domain via the Ubiquitin-Proteasome Pathway. Proceedings of the National Academy of Sciences of the United States of America, 95, 7987-7992.
https://doi.org/10.1073/pnas.95.14.7987

 
 
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