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Volume 2012 (2012), Article ID 768190, 10 pages
Carbonic Anhydrase I as a New Plasma Biomarker for Prostate Cancer
1Division of Chemotherapy and Clinical Research, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan
2Department of Urology, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
3New Frontiers Research Laboratories, Toray Industries, Inc., 10-1 Tebiro, Kanagawa, Kamakura 248-8555, Japan
4Bio Science Department, Research and Development Center, Mitsui Knowledge Industry Co., Ltd., 2-7-14 Higashinakano, Nakano-Ku, Tokyo 164-8555, Japan
5Department of Anatomic Pathology, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
Received 17 September 2012; Accepted 2 October 2012
Academic Editors: A. E. Bilsland, B. Comin-Anduix, G. Ferrandina, and S. Holdenrieder
Copyright © 2012 Michiko Takakura 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.
- A. Jemal, R. Siegel, E. Ward, Y. Hao, J. Xu, and M. J. Thun, “Cancer statistics, 2009,” CA—A Cancer Journal for Clinicians, vol. 59, no. 4, pp. 225–249, 2009.
- W. J. Catalona, D. S. Smith, T. L. Ratliff, and J. W. Basler, “Detection of organ-confined prostate cancer is increased through prostate- specific antigen-based screening,” JAMA, vol. 270, no. 8, pp. 948–954, 1993.
- J. Pannek and A. W. Partin, “Prostate-specific antigen: what's new in 1997,” Oncology, vol. 11, no. 9, pp. 1273–1278, 1997.
- S. Loeb, S. N. Gashti, and W. J. Catalona, “Exclusion of inflammation in the differential diagnosis of an elevated prostate-specific antigen (PSA),” Urologic Oncology, vol. 27, no. 1, pp. 64–66, 2009.
- W. J. Catalona, J. P. Richie, F. R. Ahmann et al., “Comparison of digital rectal examination and serum prostate specific antigen in the early detection of prostate cancer: Results of a multicenter clinical trial of 6,630 men,” Journal of Urology, vol. 151, no. 5, pp. 1283–1290, 1994.
- W. J. Catalona, D. S. Smith, and D. K. Ornstein, “Prostate cancer detection in men with serum PSA concentrations of 2.6 to 4.0 ng/mL and benign prostate examination: Enhancement of specificity with free PSA measurements,” JAMA, vol. 277, no. 18, pp. 1452–1455, 1997.
- A. Magklara, A. Scorilas, W. J. Catalona, and E. P. Diamandis, “The combination of human glandular Kallikrein and free prostrate- specific antigen (PSA) enhances discrimination between prostate cancer and benign prostatic hyperplasia in patients with moderately increased total PSA,” Clinical Chemistry, vol. 45, no. 11, pp. 1960–1966, 1999.
- J. Cervera Deval, F. J. Morales Olaya, J. Jornet Fayos, and M. González Añón, “Diagnostic value of the second prostate biopsies in males of risk. Study stratified by value of PSA,” Actas Urologicas Espanolas, vol. 28, no. 9, pp. 666–671, 2004.
- M. Raber, V. Scattoni, A. Salonia, P. Consonni, and P. Rigatti, “Repeated ultrasound-guided transrectal prostate biopsy in patients with negative histologic test,” Archivio Italiano di Urologia, Andrologia, vol. 72, no. 4, pp. 197–199, 2000.
- M. Ono, M. Shitashige, K. Honda et al., “Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectromery,” Molecular and Cellular Proteomics, vol. 5, no. 7, pp. 1338–1347, 2006.
- A. Negishi, M. Ono, Y. Handa et al., “Large-scale quantitative clinical proteomics by label-free liquid chromatography and mass spectrometry,” Cancer Science, vol. 100, no. 3, pp. 514–519, 2009.
- M. Ono, J. Matsubara, K. Honda et al., “Prolyl 4-hydroxylation of α-fibrinogen. A novel protein modification revealed by plasma proteomics,” The Journal of Biological Chemistry, vol. 284, no. 42, pp. 29041–29049, 2009.
- Y. Murakoshi, K. Honda, S. Sasazuki et al., “Plasma biomarker discovery and validation for colorectal cancer by quantitative shotgun mass spectrometry and protein microarray,” Cancer Science, vol. 102, no. 3, pp. 630–638, 2011.
- J. Matsubara, K. Honda, M. Ono et al., “Reduced plasma level of CXC chemokine ligand 7 in patients with pancreatic cancer,” Cancer Epidemiology Biomarkers and Prevention, vol. 20, no. 1, pp. 160–171, 2011.
- A. Yokomizo, M. Takakura, Y. Kanai et al., “Use of quantitative shotgun proteomics to identify fibronectin 1 as a potential plasma biomarker for clear cell carcinoma of the kidney,” Cancer Biomarkers, vol. 10, no. 3-4, pp. 175–183, 2011.
- M. Ono, M. Kamita, Y. Murakoshi, et al., “Biomarker discovery of pancreatic and gastrointestinal cancer by 2DICAL: 2-dimensional image-converted analysis of liquid chromatography and mass spectrometry,” International Journal of Proteomics, vol. 2012, Article ID 897412, 10 pages, 2012.
- Y. Tanaka, H. Akiyama, T. Kuroda et al., “A novel approach and protocol for discovering extremely low-abundance proteins in serum,” Proteomics, vol. 6, no. 17, pp. 4845–4855, 2006.
- M. Idogawa, T. Yamada, K. Honda, S. Sato, K. Imai, and S. Hirohashi, “Poly(ADP-ribose) polymerase-1 is a component of the oncogenic T-cell factor-4/beta;-catenin complex,” Gastroenterology, vol. 128, no. 7, pp. 1919–1936, 2005.
- H. Lilja, D. Ulmert, and A. J. Vickers, “Prostate-specific antigen and prostate cancer: Prediction, detection and monitoring,” Nature Reviews Cancer, vol. 8, no. 4, pp. 268–278, 2008.
- S. Loeb and W. J. Catalona, “What to do with an abnormal PSA test,” Oncologist, vol. 13, no. 3, pp. 299–305, 2008.
- C. T. Supuran and A. Scozzafava, “Carbonic anhydrases as targets for medicinal chemistry,” Bioorganic and Medicinal Chemistry, vol. 15, no. 13, pp. 4336–4350, 2007.
- E. R. Swenson, “Distribution and functions of carbonic anhydrase in the gastrointestinal tract,” in Carbonic Anhydrases: Cellular Physiology and Molecular Genetics, S. J. Dodgson, R. E. Tashian, G. Gros, and N. D. Carter, Eds., pp. 265–287, Plenum Press, New York, NY, USA, 1991.
- G. Lonnerholm and P. Wistrand, “Carbonic anhydrase in the human fetal gastrointestinal tract,” Biology of the Neonate, vol. 44, no. 3, pp. 166–176, 1983.
- I. B. Renes, M. Verburg, D. J. P. M. Van Nispen et al., “Epithelial proliferation, cell death, and gene expression in experimental colitis: Alterations in carbonic anhydrase I, mucin MUC2, and trefoil factor 3 expression,” International Journal of Colorectal Disease, vol. 17, no. 5, pp. 317–326, 2002.
- C. T. Supuran, “Carbonic anhydrase inhibition/activation: Trip of a scientist around the world in the search of novel chemotypes and drug targets,” Current Pharmaceutical Design, vol. 16, no. 29, pp. 3233–3245, 2010.