Table of Contents Author Guidelines Submit a Manuscript
Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 516469, 14 pages
http://dx.doi.org/10.1155/2010/516469
Research Article

The Differential Expression of Aqueous Soluble Proteins in Breast Normal and Cancerous Tissues in Relation to Stage and Grade of Patients

1School of Pharmaceutical Sciences, Science University of Malaysia, USM, 11800 Penang, Malaysia
2Department of Surgery, Penang General Hospital, Jalan Residensi, Georgetown, 10990 Penang, Malaysia

Received 3 June 2010; Revised 5 August 2010; Accepted 11 October 2010

Academic Editor: Anne Hamburger

Copyright © 2010 Seng Liang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. American Cancer Society, “How many women get breast cancer?” http://www.cancer.org/docroot/CRI/content/CRI_2_2_1X_How_many_people_get_breast_cancer_5.asp.
  2. World Health Organization, “Cancer: Fact Sheet,” http://www.who.int/entity/mediacentre/factsheets/fs297/en/index.html.
  3. G. C. C. Lim and Y. Halimah, Second Report of the National Cancer Registry 2003: Cancer Incidence in Malaysia 2003, National Cancer Registry, Kuala Lumpur, Malaysia, 2004.
  4. J. G. Molland, M. Donnellan, N. C. Janu, H. L. Carmalt, C. W. Kennedy, and D. J. Gillett, “Infiltrating lobular carcinoma—a comparison of diagnosis, management and outcome with infiltrating duct carcinoma,” The Breast, vol. 13, no. 5, pp. 389–396, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. Y. Peng, Y. Li, L. L. Gellert et al., “Androgen receptor coactivator p44/Mep50 in breast cancer growth and invasion,” Journal of Cellular and Molecular Medicine. In press.
  6. R. K. Rasmussen, H. Ji, J. S. Eddes et al., “Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2,” Electrophoresis, vol. 18, no. 3-4, pp. 588–598, 1997. View at Publisher · View at Google Scholar · View at Scopus
  7. M. R. Wilkins, C. Pasquali, R. D. Appel et al., “From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis,” Bio/Technology, vol. 14, no. 1, pp. 61–65, 1996. View at Google Scholar
  8. P. H. O'Farrell, “High resolution two dimensional electrophoresis of proteins,” The Journal of Biological Chemistry, vol. 250, no. 10, pp. 4007–4021, 1975. View at Google Scholar · View at Scopus
  9. C. S. Giometti, S. L. Tollaksen, C. Chubb, C. Williams, and E. Huberman, “Analysis of proteins from human breast epithelial cells using two-dimensional gel electrophoresis,” Electrophoresis, vol. 16, no. 7, pp. 1215–1224, 1995. View at Google Scholar · View at Scopus
  10. F. Le Naour, D. E. Misek, M. C. Krause et al., “Proteomics-based identification of RS/DJ-1 as a novel circulating tumour antigen in breast cancer,” Clinical Cancer Research, vol. 7, no. 11, pp. 3325–3327, 2001. View at Google Scholar
  11. D.-Q. Li, L. Wang, F. Fei et al., “Identification of breast cancer metastasis-associated proteins in an isogenic tumor metastasis model using two-dimensional gel electrophoresis and liquid chromatography-ion trap-mass spectrometry,” Proteomics, vol. 6, no. 11, pp. 3352–3368, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. M. J. Page, B. Amess, R. R. Townsend et al., “Proteomic definition of normal human luminal and myoepithelial breast cells purified from reduction mammoplasties,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 22, pp. 12589–12594, 1999. View at Publisher · View at Google Scholar · View at Scopus
  13. K. Williams, C. Chubb, E. Huberman, and C. S. Giometti, “Analysis of differential protein expression in normal and neoplastic human breast epithelial cell lines,” Electrophoresis, vol. 19, no. 2, pp. 333–343, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. P. Alfonso, A. Núñez, J. Madoz-Gurpide, L. Lombardia, L. Sánchez, and J. I. Casal, “Proteomic expression analysis of colorectal cancer by two-dimensional differential gel electrophoresis,” Proteomics, vol. 5, no. 10, pp. 2602–2611, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. R. Chen, S. Pan, T. A. Brentnall, and R. Aebersold, “Proteomic profiling of pancreatic cancer for biomarker discovery,” Molecular and Cellular Proteomics, vol. 4, no. 4, pp. 523–533, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. D. B. Friedman, S. Hill, J. W. Keller et al., “Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry,” Proteomics, vol. 4, no. 3, pp. 793–811, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. P. R. Jungblut, U. Zimny-Arndt, E. Zeindl-Eberhart et al., “Proteomics in human disease: cancer, heart and infectious diseases,” Electrophoresis, vol. 20, no. 10, pp. 2100–2110, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. M. R. Emmert-Buck, J. W. Gillespie, C. P. Paweletz et al., “An approach to proteomic analysis of human tumors,” Molecular Carcinogenesis, vol. 27, no. 3, pp. 158–165, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. F. J. Esteva and G. N. Hortobagyi, “Prognostic molecular markers in early breast cancer,” Breast Cancer Research, vol. 6, no. 3, pp. 109–118, 2004. View at Publisher · View at Google Scholar · View at Scopus
  20. National Cancer Institute, “Breast cancer staging,” http://www.cancer.gov/cancertopics/wyntk/breast/page9.
  21. National Cancer Institute, “Tumor grade: questions and answers,” http://www.cancer.gov/cancertopics/factsheet/Detection/tumor-grade.
  22. A. Tsugita and M. Kamo, “2-D electrophoresis of plant proteins,” in Methods in Molecular Biology, A. J. Link, Ed., vol. 112 of 2-D Proteome Analysis Protocols, pp. 95–98, Humana Press, Totowa, NJ, USA, 1999. View at Google Scholar
  23. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
  24. M. I. Othman, M. I. A. Majid, M. Singh, S. Subathra, L. Seng, and L.-H. Gam, “Proteomics of Grade 3 infiltrating ductal carcinoma in Malaysian Chinese breast cancer patients,” Biotechnology and Applied Biochemistry, vol. 52, no. 3, pp. 209–219, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Lauriere, “A semidry electroblotting system efficiently transfers both high- and low-molecular-weight proteins separated by SDS-PAGE,” Analytical Biochemistry, vol. 212, no. 1, pp. 206–211, 1993. View at Publisher · View at Google Scholar · View at Scopus
  26. S. Liang, M. Singh, and L.-H. Gam, “The differential expression of aqueous soluble proteins in breast normal and cancerous tissues in relation to ethnicity of the patients; Chinese, Malay and Indian,” Disease Markers, vol. 28, no. 3, pp. 149–165, 2010. View at Google Scholar
  27. P. D. Nash, M. Opas, and M. Michalak, “Calreticulin: not just another calcium-binding protein,” Molecular and Cellular Biochemistry, vol. 135, no. 1, pp. 71–78, 1994. View at Google Scholar · View at Scopus
  28. L. Bini, B. Magi, B. Marzocchi et al., “Protein expression profiles in human breast ductal carcinoma and histologically normal tissue,” Electrophoresis, vol. 18, no. 15, pp. 2832–2841, 1997. View at Publisher · View at Google Scholar · View at Scopus
  29. K. Chahed, M. Kabbage, B. Hamrita et al., “Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: the involvement of several pathways in tumorigenesis,” Clinica Chimica Acta, vol. 388, no. 1-2, pp. 106–114, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. B. Franzén, S. Linder, A. A. Alaiya et al., “Analysis of polypeptide expression in benign and malignant human breast lesions,” Electrophoresis, vol. 18, no. 3-4, pp. 582–587, 1997. View at Publisher · View at Google Scholar · View at Scopus
  31. A. Aitken, “14-3-3 and its possible role in co-ordinating multiple signalling pathways,” Trends in Cell Biology, vol. 6, no. 9, pp. 341–347, 1996. View at Publisher · View at Google Scholar · View at Scopus
  32. H. Fu, R. R. Subramanian, and S. C. Masters, “14-3-3 Proteins: structure, function, and regulation,” Annual Review of Pharmacology and Toxicology, vol. 40, pp. 617–647, 2000. View at Publisher · View at Google Scholar · View at Scopus
  33. P. Russell, “Checkpoints on the road to mitosis,” Trends in Biochemical Sciences, vol. 23, no. 10, pp. 399–402, 1998. View at Publisher · View at Google Scholar · View at Scopus
  34. E. M. C. Skoulakis and R. L. Davis, “14-3-3 Proteins in neuronal development and function,” Molecular Neurobiology, vol. 16, no. 3, pp. 269–284, 1998. View at Google Scholar · View at Scopus
  35. M. B. Yaffe, “How do 14-3-3 proteins work?—gatekeeper phosphorylation and the molecular anvil hypothesis,” FEBS Letters, vol. 513, no. 1, pp. 53–57, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. H. Hermeking, “The 14-3-3 cancer connection,” Nature Reviews Cancer, vol. 3, no. 12, pp. 931–943, 2003. View at Google Scholar · View at Scopus
  37. G. Tzivion, Z. Luo, and J. Avruch, “A dimeric.14-3-3 protein is an essential cofactor for Raf kinase activity,” Nature, vol. 394, no. 6688, pp. 88–92, 1998. View at Publisher · View at Google Scholar · View at Scopus
  38. A.-S. Vercoutter-Edouart, J. Lemoine, X. Le Bourhis et al., “Proteomic analysis reveals that 14-3-3σ is down-regulated in human breast cancer cells,” Cancer Research, vol. 61, no. 1, pp. 76–80, 2001. View at Google Scholar · View at Scopus
  39. L. Zang, D. P. Toy, W. S. Hancock, D. C. Sgroi, and B. L. Karger, “Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 16O/18O isotopic labeling,” Journal of Proteome Research, vol. 3, no. 3, pp. 604–612, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. B. L. Tang, F. Peter, J. Krijnse-Locker, S. H. Low, G. Griffiths, and W. Hong, “The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus,” Molecular and Cellular Biology, vol. 17, no. 1, pp. 256–266, 1997. View at Google Scholar · View at Scopus
  41. M.-K. Cha and I.-H. Kim, “Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma,” Biochemical and Biophysical Research Communications, vol. 222, no. 2, pp. 619–625, 1996. View at Publisher · View at Google Scholar · View at Scopus
  42. A. Gurachevsky, E. Muravskaya, T. Gurachevskaya, L. Smirnova, and V. Muravsky, “Cancer-associated alteration in fatty acid binding to albumin studied by spin-label electron spin resonance,” Cancer Investigation, vol. 25, no. 6, pp. 378–383, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. I. Laursen, P. Briand, and A. E. Lykkesfeldt, “Serum albumin as a modulator on growth of the human breast cancer cell line, MCF-7,” Anticancer Research, vol. 10, no. 2 A, pp. 343–351, 1990. View at Google Scholar · View at Scopus
  44. A. Purohit, D. Y. Wang, M. W. Ghilchik, and M. J. Reed, “Regulation of aromatase and sulphatase in breast tumour cells,” Journal of Endocrinology, vol. 150, pp. S65–S71, 1996. View at Google Scholar · View at Scopus
  45. E. F. Petricoin III, A. M. Ardekani, B. A. Hitt et al., “Use of proteomic patterns in serum to identify ovarian cancer,” The Lancet, vol. 359, no. 9306, pp. 572–577, 2002. View at Publisher · View at Google Scholar · View at Scopus