Reproductive and Developmental Biology

  • 제36권1호
  • /
  • Pages.39-47
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  • 2012
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  • 1738-2432(pISSN)
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  • 2288-0151(eISSN)
한국동물번식학회 (The Korean Society of Animal Reproduction)
권호 표지

The Oxidative Modification of COL6A1 in Membrane Proteins of Ovarian Cancer Patients

  • Yang, Hee-Young (Department of Oral Biochemistry, Dental Science Research Institute and the BK21 Project, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University) ;
  • Lee, Tae-Hoon (Department of Oral Biochemistry, Dental Science Research Institute and the BK21 Project, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University)
  • 투고 : 2012.03.14
  • 심사 : 2012.03.26
  • 발행 : 2012.03.31
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초록

Ovarian cancer is the most lethal gynecological malignancy, and specific biomarkers are important needed to improve diagnosis, prognosis, and to forecast and monitor treatment efficiency. There are a lot of pathological factors, including reactive oxygen species (ROS), involved in the process of cancer initiation and progression. The oxidative modification of proteins by ROS is implicated in the etiology or progression of disorders and diseases. In this study, a labeling experiment with the thiol-modifying reagent biotinylated iodoacetamide (BIAM) revealed that a variety of proteins were differentially oxidized between normal and tumor tissues of ovarian cancer patients. To identify cysteine oxidation-sensitive proteins in ovarian cancer patients, we performed comparative analysis by nano-UPLC-$MS^E$ shotgun proteomics. We found oxidation-sensitive 22 proteins from 41 peptides containing cysteine oxidation. Using Ingenuity program, these proteins identified were established with canonical network related to cytoskeletal network, cellular organization and maintenance, and metabolism. Among oxidation-sensitive proteins, the modification pattern of Collagen alpha-1(VI) chain (COL6A1) was firstly confirmed between normal and tumor tissues of patients by 2-DE western blotting. This result suggested that COL6A1 might have cysteine oxidative modification in tumor tissue of ovarian cancer patients.

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참고문헌

  1. Alexopoulos LG, Youn I, Bonaldo P, Guilak F (2009): Developmental and osteoarthritic changes in Col6a-1-knockout mice: biomechanics of type VI collagen in the cartilage pericellular matrix. Arthritis and Rheumatism 60:771-779. https://doi.org/10.1002/art.24293
  2. Bedard K, Krause KH (2007): The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiological Reviews 87:245-313. https://doi.org/10.1152/physrev.00044.2005
  3. Bhoola S, Hoskins, WJ (2006): Diagnosis and management of epithelial ovarian cancer. Obstetrics and Gynecology 107:1399-1410. https://doi.org/10.1097/01.AOG.0000220516.34053.48
  4. Bouayed J, Rammal H, Soulimani R (2009): Oxidative stress and anxiety: relationship and cellular pathways. Oxidative Medicine and Cellular Longevity 2:63-67. https://doi.org/10.4161/oxim.2.2.7944
  5. Braghetta P, Ferrari A, Fabbro C, Bizzotto D, Volpin D, Bonaldo P, Bressan GM (2008): An enhancer required for transcription of the Col6a1 gene in muscle connective tissue is induced by signals released from muscle cells. Experimental Cell Research 314:3508-3518. https://doi.org/10.1016/j.yexcr.2008.08.006
  6. Charles RL, Schroder E, May G, Free P, Gaffney PR, Wait R, Begum S, Heads RJ, Eaton P (2007): Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue. Molecular & Cellular Proteomics : MCP 6:1473-1484. https://doi.org/10.1074/mcp.M700065-MCP200
  7. Choi KS, Park SY, Baek SH, Dey-Rao R, Park YM, Zhang H, IP C, Park EM, Kim YH, Park JH (2006): Analysis of protein redox modification by hypoxia. Preparative Biochemistry & Biotechnology 36:65-79. https://doi.org/10.1080/10826060500388520
  8. D'alessandro A, Rinalducci S, Zolla L (2011): Redox proteomics and drug development. Journal of Proteomics, 74:2575-2595. https://doi.org/10.1016/j.jprot.2011.01.001
  9. Dai J, Wang J, Zhang Y, Lu Z, Yang B, Li X, Cai Y, Qian X (2005): Enrichment and identification of cysteine-containing peptides from tryptic digests of performic oxidized proteins by strong cation exchange LC and MALDI-TOF/TOF MS. Analytical Chemistry 77:7594-7604. https://doi.org/10.1021/ac0506276
  10. Dalle-Donne I, Scaloni A, Giustarini D, Cavarra E, Tell G, Lungarella G, Colombo R, Rossi R, Milzani A (2005): Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrometry Reviews 24:55-99. https://doi.org/10.1002/mas.20006
  11. Dansen TB, Smits LM, Van Triest MH, De Keizer P L, Van Leenen D, Koerkamp MG, Szypowska A, Meppelink A, Brenkman AB, Yodoi J, Holstege FC, Burgering BM (2009): Redox-sensitive cysteines bridge p300/CBP-mediated acetylation and FoxO4 activity. Nature Chemical Biology 5:664-72. https://doi.org/10.1038/nchembio.194
  12. Fu C, Wu C, Liu T, Ago T, Zhai P, Sadoshima J, Li H (2009): Elucidation of thioredoxin target protein networks in mouse. Molecular & Cellular Proteomics : MCP 8:1674-1687. https://doi.org/10.1074/mcp.M800580-MCP200
  13. Grune T, Reinheckel T, Davies KJ (1996): Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. The Journal of Biological Chemistry 271:15504-15509. https://doi.org/10.1074/jbc.271.26.15504
  14. Jemal A, Siegel R, Ward E, Murray T, Xu J, Smigal C, Thun MJ (2006): Cancer statistics, 2006. CA: A Cancer Journal for Clinicians 56:106-130. https://doi.org/10.3322/canjclin.56.2.106
  15. Jiang Z, Fletcher NM, Ali-Fehmi R, Diamond MP, Abu-Soud HM, Munkarah AR, Saed GM (2011): Modulation of redox signaling promotes apoptosis in epithelial ovarian cancer cells. Gynecologic Oncology 122:418-423. https://doi.org/10.1016/j.ygyno.2011.04.051
  16. Klaunig JE, Xu Y, Isenberg JS, Bachowski S, Kolaja KL, Jiang J, Stevenson DE, Walborg EF, JR (1998): The role of oxidative stress in chemical carcinogenesis. Environmental Health Perspectives 106 Suppl 1:289-295. https://doi.org/10.1289/ehp.98106s1289
  17. Kumar P, Devi U, Ali S, Upadhya R, Pillai S, Raja A, Rao S, Rao A (2009): Plasma protein oxidation in patients with brain tumors. Neurological Research, 31:270-273. https://doi.org/10.1179/174313209X382296
  18. Kuo HJ, Maslen CL, Keene DR, Glanville RW (1997): Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen. The Journal of Biological Chemistry 272:26522-26529. https://doi.org/10.1074/jbc.272.42.26522
  19. Kwon J, Lee SR, Yang KS, Ahn Y, Kim YJ, Stadtman ER, Rhee SG (2004): Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proceedings of the National Academy of Sciences of the United States of America 101:16419-16424. https://doi.org/10.1073/pnas.0407396101
  20. Lei K, Townsend DM, Tew KD (2008): Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response. Oncogene 27:4877-4887. https://doi.org/10.1038/onc.2008.132
  21. Leichert LI, Gehrke F, Gudiseva HV, Blackwell T, Ilbert M, Walker AK, Strahler JR, Andrews PC, Jakob U (2008): Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proceedings of the National Academy of Sciences of the United States of America 105:8197-8202. https://doi.org/10.1073/pnas.0707723105
  22. Leitner A, Lindner W (2006): Chemistry meets proteomics: the use of chemical tagging reactions for MS-based proteomics. Proteomics 6:5418-5434. https://doi.org/10.1002/pmic.200600255
  23. Levine RL, Williams JA, Stadtman ER, Shacter E (1994): Carbonyl assays for determination of oxidatively modified proteins. Methods in Enzymology 233:346-357.
  24. Parker LP, Taylor DD, Kesterson S, Gercel-Taylor C (2009): Gene expression profiling in response to estradiol and genistein in ovarian cancer cells. Cancer Genomics & Proteomics 6:189-194.
  25. Phalen TJ, Weirather K, Deming PB, Anathy V, Howe AK, Van Der Vliet A, Jonsson TJ, Poole LB, Heintz NH (2006): Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery. The Journal of Cell Biology 175:779-789. https://doi.org/10.1083/jcb.200606005
  26. Poole LB, Zeng BB, Knaggs SA, Yakubu M, King SB (2005): Synthesis of chemical probes to map sulfenic acid modifications on proteins. Bioconjugate Chemistry 16:1624-1628. https://doi.org/10.1021/bc050257s
  27. Sangeetha N, Aranganathan S, Nalini N (2010): Silibinin ameliorates oxidative stress induced aberrant crypt foci and lipid peroxidation in 1,2 dimethylhydrazine induced rat colon cancer. Investigational New Drugs 28:225-233. https://doi.org/10.1007/s10637-009-9237-5
  28. Seo JH, Lim JC, Lee DY, Kim KS, Piszczek G, Nam HW, Kim YS, Ahn T, Yun CH, Kim K, Chock PB, Chae HZ (2009): Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II. The Journal of Biological Chemistry 284:13455-13465. https://doi.org/10.1074/jbc.M900641200
  29. Stadtman ER, Levine RL (2000): Protein oxidation. Annals of the New York Academy of Sciences 899:191-208.
  30. Tillet E, Wiedemann H, Golbik R, Pan TC, Zhang RZ, Mann K, Chu ML, Timpl R (1994): Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI. European Journal of Biochemistry / FEBS 221:177-185. https://doi.org/10.1111/j.1432-1033.1994.tb18727.x
  31. Toda T, Nakamura M, Morisawa H, Hirota M, Nishigaki R, Yoshimi Y (2010): Proteomic approaches to oxidative protein modifications implicated in the mechanism of aging. Geriatrics & Gerontology International 10 Suppl 1:S25-S31. https://doi.org/10.1111/j.1447-0594.2010.00606.x
  32. Ushio-Fukai M, Alexander RW (2004): Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase. Molecular and Cellular Biochemistry 264:85-97. https://doi.org/10.1023/B:MCBI.0000044378.09409.b5
  33. Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J (2004): Large- scale cDNA transfection screening for genes related to cancer development and progression. Proceedings of the National Academy of Sciences of the United States of America 101:15724-15729. https://doi.org/10.1073/pnas.0404089101
  34. Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG (2010): Inactivation of peroxiredoxin I by phosphorylation allows localized $H_2O_2$ accumulation for cell signaling. Cell 140:517-528. https://doi.org/10.1016/j.cell.2010.01.009
  35. Xu D, Suenaga N, Edelmann MJ, Fridman R, Muschel RJ, Kessler BM (2008): Novel MMP-9 substrates in cancer cells revealed by a label-free quantitative proteomics approach. Molecular & Cellular Proteomics : MCP 7:2215-2228. https://doi.org/10.1074/mcp.M800095-MCP200
  36. Yang HY, Kwon J, Cho EJ, Choi HI, Park C, Park HR, Park SH, Chung KJ, Ryoo ZY, Cho KO, Lee TH (2010): Proteomic analysis of protein expression affected by peroxiredoxin V knock-down in hypoxic kidney. Journal of Proteome Research 9:4003-4015. https://doi.org/10.1021/pr100190b
  37. Yang HY, Kwon J, Choi HI, Park SH, Yang U, Park HR, Ren L, Chung KJ, Kim YU, Park BJ, Jeong SH, Lee TH (2012.): In-depth analysis of cysteine oxidation by the RBC proteome: advantage of peroxiredoxin II knockout mice. Proteomics 12:101-112. https://doi.org/10.1002/pmic.201100275
  38. Zhao G, Chen J, Deng Y, Gao F, Zhu J, Feng Z, Lv X, Zhao Z (2011): Identification of NDRG1-regulated genes associated with invasive potential in cervical and ovarian cancer cells. Biochemical and Biophysical Research Communications 408:154-159. https://doi.org/10.1016/j.bbrc.2011.03.140