Share This Article:

Differential Measurements of Oxidatively Modified Proteins in Colorectal Adenopolyps

Abstract Full-Text HTML XML Download Download as PDF (Size:1294KB) PP. 289-299
DOI: 10.4236/ijcm.2015.64037    2,230 Downloads   2,651 Views   Citations

ABSTRACT

Introduction: Adenopolyps patients have a three-fold higher risk of colon cancer over the general population, which increases to six-fold if the polyps are multiple and with lower survival among African American population. Currently, 6% of CRC can be ascribed to mutations in particular genes. Moreover, the optimal management of patients with colorectal adenopolyps depends on the accuracy of appropriate staging strategies because patients with similar colorectal adenocarcinoma architecture display heterogeneity in the course and outcome of the disease. Oxidative stress, due to an imbalance between reactive oxygen species (ROS) and antioxidant capacities as well as a disruption of redox signaling, causes a wide range of damage to DNA, proteins, and lipids which promote tumor formation. Objective/Method: This study applied spectrophotometric, dinitrophenylhydrazone (DNPH) assay, two-dimensional gel electrophoresis, and western blot analyses to assess the levels of oxidatively modified proteins in 41 pairs of primary colorectal tissues including normal/surrounding, adenopolyps (tubular, tubulovillous, villous, polypvillous) and carcinoma. Analysis of variance (ANOVA) and Student’s t-tests were utilized for the resulting data set. Results: Our data showed that the levels of reactive protein carbonyl groups significantly increased as colorectal adenopolyps progresses to malignancy. No significant differences were found in the levels of carbonyl proteins between gender samples analyzed. For African American patients, there were, relative to Caucasians, 10% higher levels of reactive carbonyls in proteins of tubulovillous tissue samples (P < 0.05) and over 36% higher in levels in adenocarcinomas (P < 0.05). In normal tissues and tubular, there were no significant differences between the two groups in levels of protein carbonyls. Differences in the levels of protein carbonyl expression within individual patient samples with different number of tumor cells were notably evident. Conclusion: Results suggested that oxidative stress could be involved in the modification of oxidatively carbonyl proteins in the precancer stages, leading to increased aggressiveness of colorectal polyps.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Mehrabi, S. , Wallace, L. , Cohen, S. , Yao, X. and Aikhionbare, F. (2015) Differential Measurements of Oxidatively Modified Proteins in Colorectal Adenopolyps. International Journal of Clinical Medicine, 6, 289-299. doi: 10.4236/ijcm.2015.64037.

References

[1] (2013) Cancer Facts & Figures 2013. American Cancer Society, Atlanta.
[2] Fearon, E.R. and Vogelstein, B. (1990) A Genetic Model for Colorectal Tumorigenesis. Cell, 61, 759-767.
http://dx.doi.org/10.1016/0092-8674(90)90186-I
[3] Yang, H.Y., Chay, K.O., Kwon, J., Kwon, S.O., Park, Y.K. and Lee, T.H. (2013) Comparative Proteomic Analysis of Cysteine Oxidation in Colorectal Cancer Patients. Molecules and Cells, 35, 533-542.
http://dx.doi.org/10.1007/s10059-013-0058-1
[4] Glei, M., Latunde-Dada, G.O., Klinder, A., Becker, T.W., Hermann, U., Voigt, K. and Pool-Zobel, B.L. (2002) Iron-Overload Induces Oxidative DNA Damage in the Human Colon Carcinoma Cell Line HT29 Clone 19A. Mutation Research, 519, 151-161.
http://dx.doi.org/10.1016/S1383-5718(02)00135-3
[5] Ribeiro, L.M., Priolli, D.G., Miranda, D.D.C., Arcari, D.P., Pedrazzoli Jr., J. and Martinez, C.A.R. (2008) Analysis of Oxidative DNA Damage in Patients with Colorectal Cancer. Clinical Colorectal Cancer, 7, 267-272.
http://dx.doi.org/10.3816/CCC.2008.n.034
[6] Parkin, D.M. (2006) The Global Health Burden of Infection-Associated Cancers in the Year 2002. International Journal of Cancer, 118, 3030-3044.
http://dx.doi.org/10.1002/ijc.21731
[7] Weitz, J., Koch, M., Debus, J., Hohler, T., Galle, P.R. and Buchler, M.W. (2005) Colorectal Cancer. Lancet, 365, 153-165.
http://dx.doi.org/10.1016/S0140-6736(05)17706-X
[8] Seril, D.N., Liao, J., Yang, G.Y. and Yang, C.S. (2003) Oxidative Stress and Ulcerative Colitis-Associated Carcinogenesis: Studies in Humans and Animals Models. Carcinogenesis, 24, 353-562.
http://dx.doi.org/10.1093/carcin/24.3.353
[9] Pelicano, H., Carney, D. and Huang, P. (2004) ROS Stress in Cancer Cells and Therapeutic Implications. Drug Resistance Updates, 7, 97-110.
http://dx.doi.org/10.1016/j.drup.2004.01.004
[10] Evans, P., Lyras, L. and Halliwell, B. (1999) Measurement of Protein Carbonyls in Human Brain Tissue. Methods in Enzymology, 300, 145-156.
http://dx.doi.org/10.1016/S0076-6879(99)00122-6
[11] Beal, M.F. (1990) Oxidatively Modified Proteins in Aging and Disease. Free Radical Biology and Medicine, 32, 797-803.
http://dx.doi.org/10.1016/S0891-5849(02)00780-3
[12] Levine, R.L., Garland, D., Oliver, C.N., Amici, A., Climent, I., Lenz, A.G., Ahn, B., Shaltiel, S. and Stadtman, E.R. (1990) Determination of Carbonyl Content in Oxidatively Modified Proteins. Methods in Enzymology, 186, 464-478.
http://dx.doi.org/10.1016/0076-6879(90)86141-H
[13] Mehrabi, S., Partridge, E.E., Seffens, W., Yao, X. and Aikhionbare, F.O. (2014) Oxidatively Modified Proteins in the Serous Subtype of Ovarian Carcinoma. BioMed Research International, 2014, 1-7.
http://dx.doi.org/10.1155/2014/585083
[14] Zipprich, J., Terry, M.B., Liao, Y., Agrawal, M., Gurvich, I., Senie, R. and Santella, R.M. (2009) Breast Cancer Family Registry Discordant for Breast Cancer from the New York Site of the Plasma Protein Carbonyls and Breast Cancer Risk in Sisters. Cancer Research, 69, 2966-2972.
http://dx.doi.org/10.1158/0008-5472.CAN-08-3418
[15] Smith, M.A., Perry, G., Richey, P.L., Sayre, L.M., Anderson, V.E., Beal, M.F. and Kowall, N. (1996) Oxidative Damage in Alzheimer’s. Nature, 382, 120-121.
http://dx.doi.org/10.1038/382120b0
[16] Murdoch, W.J. and Martinchick, J.F. (2004) Oxidative Damage to DNA of Ovarian Surface Epithelial Cells Affected by Ovulation: Carcinogenic Implication and Chemoprevention. Experimental Biology and Medicine, 229, 546-552.
[17] Marnett, L.J. (2008) Oxyradicals and DNA Damage. Carcinogenesis, 21, 361-370.
http://dx.doi.org/10.1093/carcin/21.3.361
[18] Franco, R., Schoneveld, O., Georgakilas, A. and Panayiotidis, M. (2008) Oxidative Stress, DNA Methylation and Carcinogenesis. Cancer Letters, 266, 6-11.
http://dx.doi.org/10.1016/j.canlet.2008.02.026
[19] Berlett, B.S. and Stadtman, E.R. (1997) Protein Oxidation in Aging, Disease, and Oxidative Stress. Journal of Biological Chemistry, 272, 20313-20316.
http://dx.doi.org/10.1074/jbc.272.33.20313
[20] Dalle-Donnea, I., Rossib, R., Giustarinib, D., Milzania, A. and Colomboa, R. (2003) Protein Carbonyl Groups as Biomarkers of Oxidative Stress. Clinica Chimica Acta, 329, 23-38.
http://dx.doi.org/10.1016/S0009-8981(03)00003-2
[21] Murlikiewicz, L., Sygut, A., Trzciński, R., Grzegorczyk, K., Rutkowski, M. and Dziki, A. (2010) Oxidative Protein Damage in Patients with Colorectal Cancer. Polish Journal of Surgery, 82, 454-458.
http://dx.doi.org/10.2478/v10035-010-0065-2
[22] Paz-Elizur, T., Sevilya, Z., Leitner-Dagan, Y., Elinger, D., Roisman, L.C. and Livneh, Z. (2008) DNA Repair of Oxidative DNA Damage in Human Carcinogenesis: Potential Application for Cancer Risk Assessment and Prevention. Cancer Letters, 266, 60-72.
http://dx.doi.org/10.1016/j.canlet.2008.02.032
[23] Ponczek, M.B. and Wachowicz, B. (2005) Interaction of Reactive Oxygen and Nitrogen Species with Proteins. Postepy Biochemii, 51, 140-145.
[24] Aw, T.Y. (1999) Molecular and Cellular Responses to Oxidative Stress and Changes in Oxidation-Reduction Imbalance in the Intestine. The American Journal of Clinical Nutrition, 70, 557-565.
[25] Slaga, T.J., Lichti, U., Hennings, H., Elgjo, K. and Yuspa, S.H. (1978) Effects of Tumor Promoters and Steroidal Anti-Inflammatory Agents on Skin of Newborn Mice in Vivo and in Vitro. Journal of the National Cancer Institute, 60, 425-431.
[26] Akira, S. and Kishimoto, T. (1997) NF-IL6 and NF-κB in Cytokine Gene Regulation. Advances in Immunology, 65, 1-46.
http://dx.doi.org/10.1016/S0065-2776(08)60740-3
[27] Khansari, N., Shakiba, Y. and Mahmoudi, M. (2009) Chronic Inflammation and Oxidative Stress as a Major Cause of Age-Related Diseases and Cancer. Recent Patents on Inflammation & Allergy Drug Discovery, 3, 73-80.
http://dx.doi.org/10.2174/187221309787158371
[28] Federico, A., Morgillo, F., Tuccillo, C., Ciardiello, F. and Loguercio, C. (2007) Chronic Inflammation and Oxidative Stress in Human Carcinogenesis. International Journal of Cancer, 121, 2381-2386.
http://dx.doi.org/10.1002/ijc.23192
[29] Chevion, M., Berenshtein, E. and Stadtman, E.R. (2000) Human Studies Related to Protein Oxidation: Protein Carbonyl Content as a Marker of Damage. Free Radical Research, 33, S99-S108.
[30] Shacter, E. (2000) Quantification and Significance of Protein Oxidation in Biological Samples. Drug Metabolism Reviews, 32, 307-326.
http://dx.doi.org/10.1081/DMR-100102336
[31] Klaunig, J. and Kamendulis, L.M. (2004) The Role of Oxidative Stress in Carcinogenesis. Annual Review of Pharmacology and Toxicology, 44, 239-267.
http://dx.doi.org/10.1146/annurev.pharmtox.44.101802.121851
[32] Rainis, T., Maor, I., Lanir, A., Shnizer, S. and Lavy, A. (2007) Enhanced Oxidative Stress and Leucocyte Activation in Neoplastic Tissues of the Colon. Digestive Diseases and Sciences, 52, 526-530.
http://dx.doi.org/10.1007/s10620-006-9177-2
[33] Ames, B.N., Gold, L.S. and Willett, W.C. (1995) The Causes and Prevention of Cancer. Proceedings of the National Academy of Sciences of the United States of America, 92, 5258-5265.
http://dx.doi.org/10.1073/pnas.92.12.5258
[34] Espey, L.L. (1994) Current Status of the Hypothesis That Mammalian Ovulation Is Comparable to an Inflammatory Reaction. Biology of Reproduction, 50, 233-238.
http://dx.doi.org/10.1095/biolreprod50.2.233
[35] Jung, T., Engels, M., Kaiser, B., Poppek, D. and Grune, T. (2006) Intracellular Distribution of Oxidized Proteins and Proteasome in HT22 Cells during Oxidative Stress. Free Radical Biology and Medicine, 40, 1303-1312.
http://dx.doi.org/10.1016/j.freeradbiomed.2005.11.023
[36] Schuessler, H. and Schilling, K. (1984) Oxygen Effect in the Radiolysis of Proteins. Part 2. Bovine Serum Albumin. International Journal of Radiation Biology, 45, 267-281.
http://dx.doi.org/10.1080/09553008414550381
[37] Friguet, B., Szweda, L. and Stadtman, E.R. (1994) Susceptibility of Glucose-6-Phosphate Dehydrogenase Modified 4-Hydroxynonenal and Metal-Catalyzed Oxidation to Proteolysis by Multicatalytic Protease. Archives of Biochemistry and Biophysics, 311, 168-173.
http://dx.doi.org/10.1006/abbi.1994.1222
[38] Grune, T., Reinheckel, T., Joshi, M. and Davies, K.J. (1995) Proteolysis in Cultured Liver Epithelial Cells during Oxidative Stress. Journal of Biological Chemistry, 270, 2344-2351.
http://dx.doi.org/10.1074/jbc.270.5.2344
[39] Grant, A.J., Jessup, W. and Dean, R.J. (1993) Inefficient Degradation of Oxidized Region of Protein Molecules. Free Radical Research, 18, 259-267.
http://dx.doi.org/10.3109/10715769309147493
[40] Suarez, G., Etlinger, J.D., Maturana, J. and Weitman, D. (1995) Fructated Protein Is More Resistant to ATP-Dependent Proteolysis than Glucated Protein Possibly as a Result of Higher Content of Maillard Fluorophores. Archives of Biochemistry and Biophysics, 321, 209-213.
http://dx.doi.org/10.1006/abbi.1995.1387
[41] Rivett, A.J. (1991) Regulation of Intracellular Protein Turnover: Covalent Modification as Marking Proteins for Degradation. Current Topics in Cellular Regulation, 28, 291-337.
http://dx.doi.org/10.1016/B978-0-12-152828-7.50010-X
[42] Szatrowski, T.P. and Nathan, C.F. (1991) Production of Large Amounts of Hydrogen Peroxide by Human Tumor Cells. Cancer Research, 51, 794-798.
[43] Fisher, G., Alvarez, J.A., Ellis, A.C., Granger, W.M., Ovalle, F., Dalla Man, C., Cobelli, C. and Gower, B.A. (2012) Race Differences in the Association of Oxidative Stress with Insulin Sensitivity in African- and European-American Women. Obesity, 20, 972-977.
http://dx.doi.org/10.1038/oby.2011.355
[44] Borrás, C., Sastre, J., García-Sala, D., Lloret A., Pallardó, F.V. and Vina, J. (2003) Mitochondria from Females Exhibit Higher Antioxidant Gene Expression and Lower Oxidative Damage than Males. Free Radical Biology & Medicine, 34, 546-552.
http://dx.doi.org/10.1016/S0891-5849(02)01356-4
[45] Wu, J. (2011) Regulating Cell Differentiation at Different Layers. Journal of Molecular Cell Biology, 3, 319.
http://dx.doi.org/10.1093/jmcb/mjr036
[46] Biggar, K.K. and Storey, K.B. (2011) The Emerging Roles of microRNAs in the Molecular Responses of Metabolic Rate Depression. Journal of Molecular Cell Biology, 3, 167-175.
http://dx.doi.org/10.1093/jmcb/mjq045
[47] Shah, K.M., Webber, J., Carzanig, R., Taylor, D.M., Fusi, L., Clayton, A., Brosens, J.J., Hartshorne, G. and Christian, M. (2013) Induction of microRNA Resistance and Secretion in Differentiating Human Endometrial Stromal Cells. Journal of Molecular Cell Biology, 5, 67-70.
http://dx.doi.org/10.1093/jmcb/mjs058

  
comments powered by Disqus

Copyright © 2018 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.