Generic placeholder image

Current Proteomics

Author(s): Asma Tariq*, Rana Muhammad Mateen, Iram Fatima and Muhammad Waheed Akhtar

DOI: 10.2174/1570164615666180907154459

DownloadDownload PDF Flyer Cite As
Calreticulin is Differentially Expressed in Invasive Ductal Carcinoma: A Comparative Study

Page: [148 - 155] Pages: 8

  • * (Excluding Mailing and Handling)

Abstract

Objective: The aim of the present study was to build protein profiles of untreated breast cancer patients of invasive ductal carcinoma grade II at tissue level in Pakistani population and to compare 2-D profiles of breast tumor tissues with matched normal tissues in order to evaluate for variations of proteins among them.

Materials & Methods: Breast tissue profiles were made after polytron tissue lysis and rehydrated proteins were further characterized by using two-dimensional gel electrophoresis. On the basis of isoelectric point (pI) and molecular weight, proteins were identified by online tool named Siena 2-D database and their identification was further confirmed by using MALDI-TOF.

Results: Among identified spots, 10 proteins were found to be differentially expressed i.e.; COX5A, THIO, TCTP, HPT, SODC, PPIA, calreticulin (CRT), HBB, albumin and serotransferrin. For further investigation, CRT was selected. The level of CRT in tumors was found to be significantly higher than in normal group (p < 0.05). The increased expression of CRT level in tumor was statistically significant (p = 0.010) at a 95% confidence level (p <0.05) as analyzed by Mann-Whitney. CRT was found distinctly expressed in high amount in tumor tissue as compared to their matched normal tissues.

Conclusion: It has been concluded that CRT expression could discriminate between normal tissue and tumor tissue so it might serve as a possible candidate for future studies in cancer diagnostic markers.

Keywords: Breast cancer, two-dimensional gel electrophoresis, MALDI, serum albumin, tumor, biomarkers.

Graphical Abstract

[1]
World Health Organization fact sheet February 2018. Available at http://www.who.int/mediacentre/factsheets/fs297/en/ (Accessed on April 20, 2018)
[2]
National cancer institute surveillance, epidemiology, and end results. Cancer stat facts: female breast cancer. Available at: https://seer.cancer.gov/statfacts/html/breast.html (Accessed on April 20, 2018).
[3]
Banning, M.; Hafeez, H. A two-center study of muslim women’s views of breast cancer and breast health practices in Pakistan and the UK. J. Cancer Educ., 2010, 25, 349-353.
[4]
Bhurgri, Y.; Bhurgri, A.; Hassan, S.H.; Zaidi, S.; Rahim, A.; Sankaranarayanan, R.; Parkin, D.M. Cancer incidence in Karachi, Pakistan: First results from Karachi cancer registry. Int. J. Cancer, 2000, 85, 325-329.
[5]
Gilani, G.M.; Kamal, S.; Gilani, S.A.M. Risk factors for breast cancer for women in Punjab, Pakistan: Results from a case-control study. Pak. J. Stat. Oper. Res., 2006, 2(1), 17-26.
[6]
Mamoon, N.; Hassan, U.; Mushtaq, S. Breast carcinoma in young women aged 30 or less in Northern Pakistan-the armed forces institute of pathology experience. Asian Pac. J. Cancer Prev., 2009, 10, 1079-1082.
[7]
Turashvili, G.; Bouchal, J.; Burkadze, G.; Kolar, Z. Differentiation of tumours of ductal and lobular origin: I. Proteomics of invasive ductal and lobular breast carcinomas. Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech Repub., 2005, 149, 57-62.
[8]
Misek, D.E.; Kim, E.H. Protein biomarkers for the early detection of breast cancer. Int. J. Proteomics, 2011, 2011, 343582.
[9]
Lacroix, M. Significance, detection and markers of disseminated breast cancer cells. Endocr. Relat. Cancer, 2006, 13, 1033-1067.
[10]
Bertucci, F.; Birnbaum, D.; Goncalves, A. Proteomics of breast cancer principles and potential clinical applications. Mol. Cell. Proteomics, 2006, 5, 1772-1786.
[11]
Cao, H.; Yang, Z.; Jiang, G. Expression and clinical significance of activating transcription factor 3 in human breast cancer. Iran. J. Basic Med. Sci., 2013, 16, 1151-1154.
[12]
O’Farrell, P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem., 1975, 250, 4007-4021.
[13]
Bjellqvist, B.; Ek, K.; Righetti, P.G.; Gianazza, E.; Görg, A.; Westermeier, R.; Postel, W. Isoelectric focusing in immobilized pH gradients: Principle, methodology and some applications. J. Biochem. Biophys. Methods, 1982, 6, 317-339.
[14]
Gorg, A.; Obermaier, C.; Boguth, G.; Harder, A.; Scheibe, B.; Wildgruber, R.; Weiss, W. The current state of two‐dimensional electrophoresis with immobilized pH gradients. Electrophoresis, 2000, 21, 1037-1053.
[15]
Ostwald, T.J.; MacLennan, D.H. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J. Biol. Chem., 1974, 249, 974-979.
[16]
Krause, K.H.; Michalak, M. Calreticulin. Cell, 1997, 88, 439-443.
[17]
Gelebart, P.; Opas, M.; Michalak, M. Calreticulin, a Ca2+- binding chaperone of the endoplasmic reticulum. Int. J. Biochem. Cell Biol., 2005, 37, 260-266.
[18]
Zhu, N.; Wang, Z. Calreticulin expression is associated with androgen regulation of the sensitivity to calcium ionophore-induced apoptosis in LNCaP prostate cancer cells. Cancer Res., 1999, 59, 1896-1902.
[19]
Bergner, A.; Kellner, J.; Tufman, A.; Huber, R.M. Endoplasmic reticulum Ca2+- homeostasis is altered in small and non-small cell lung cancer cell lines. J. Exp. Clin. Cancer Res., 2009, 28, 25.
[20]
Toquet, C.; Jarry, A.; Bou-Hanna, C.; Bach, K.; Denis, M.; Mosnier, J.; Laboisse, C. Altered Calreticulin expression in human colon cancer: Maintenance of Calreticulin expression is associated with mucinous differentiation. Oncol. Rep., 2007, 17, 1101-1107.
[21]
Lyons, K. TCA/acetone precipitation (large scale), AfCS. Procedure protocol ID PP00000148, version 1. The signaling gateway website 2003. Available at: http://www.signaling-gateway.org/ data/ProtocolLinks.html (Accessed on February 2, 2016).
[22]
Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 1976, 72, 248-254.
[23]
Neuhoff, V.; Stamm, R.; Eibl, H. Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: A systematic analysis. Electrophoresis, 1985, 6, 427-448.
[24]
Etzrodt, A.; Jung, H.; Tolxdorff, T.; Bigalke, L. Significance of the albumin content for axillary metastasis in breast cancer. Geburtshilfe Frauenheilkd., 1983, 43, 670-673.
[25]
Deng, S.S.; Xing, T.Y.; Zhou, H.Y.; Xiong, R.H.; Lu, Y.G.; Wen, B.; Liu, S.Q.; Yang, H.J. Comparative proteome analysis of breast cancer and adjacent normal breast tissues in human. Genomics Proteomics Bioinformatics, 2006, 4, 165-172.
[26]
Arnaudeau, S.; Frieden, M.; Nakamura, K.; Castelbou, C.; Michalak, M.; Demaurex, N. Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J. Biol. Chem., 2002, 277, 46696-46705.
[27]
Chen, C.N.; Chang, C.C.; Su, T.E.; Hsu, W.M.; Jeng, Y.M.; Ho, M.C.; Hsieh, F.J.; Lee, P.H.; Kuo, M.L.; Lee, H. Identification of calreticulin as a prognosis marker and angiogenic regulator in human gastric cancer. Ann. Surg. Oncol., 2009, 16, 524-533.
[28]
Kageyama, S.; Isono, T.; Matsuda, S.; Ushio, Y.; Satomura, S.; Terai, A.; Arai, Y.; Kawakita, M.; Okada, Y.; Yoshiki, T. Urinary calreticulin in the diagnosis of bladder urothelial carcinoma. Int. J. Urol., 2009, 16, 481-486.
[29]
Du, X.L.; Yang, H.; Liu, S.; Luo, M.; Hao, J.; Zhang, Y.; Lin, D.; Xu, X.; Cai, Y.; Zhan, Q. Calreticulin promotes cell motility and enhances resistance to anoikis through STAT3-CTTN-Akt pathway in esophageal squamous cell carcinoma. Oncogene, 2009, 28, 3714.
[30]
Gomes, I.; Dale, C.S.; Casten, K.; Geigner, M.A.; Gozzo, F.C.; Ferro, E.S.; Heimann, A.S.; Devi, L.A. Hemoglobin-derived peptides as novel type of bioactive signaling molecules. AAPS J., 2010, 12, 658-669.
[31]
Onda, M.; Akaishi, J.; Asaka, S.; Okamoto, J.; Miyamoto, S.; Mizutani, K.; Yoshida, A.; Ito, K.; Emi, M. Decreased expression of haemoglobin beta (HBB) gene in anaplastic thyroid cancer and recovory of its expression inhibits cell growth. Br. J. Cancer, 2005, 92, 2216.
[32]
Gamez-Pozo, A.; Sánchez-Navarro, I.; Nistal, M.; Calvo, E.; Madero, R.; Díaz, E.; Camafeita, E.; de Castro, J.; López, J.A.; González-Barón, M. MALDI profiling of human lung cancer subtypes. PLoS One, 2009, 4, e7731.
[33]
Ni, I.B.P.; Zakaria, Z.; Muhammad, R.; Abdullah, N.; Ibrahim, N.; Emran, N.A.; Abdullah, N.H.; Hussain, S.N. Gene expression patterns distinguish breast carcinomas from normal breast tissues: The Malaysian context. Pathol. Res. Pract., 2010, 206, 223-228.
[34]
Bini, L.; Magi, B.; Marzocchi, B.; Arcuri, F.; Tripodi, S.; Cintorino, M.; Sanchez, J.C.; Frutiger, S.; Hughes, G.; Pallini, V. Protein expression profiles in human breast ductal carcinoma and histologically normal tissue. Electrophoresis, 1997, 18, 2832-2841.
[35]
Chen, Y.W.; Chou, H.C.; Lyu, P.C.; Yin, H.S.; Huang, F.L.; Chang, W.S.W.; Fan, C.Y.; Tu, I.F.; Lai, T.C.; Lin, S.T. Mitochondrial proteomics analysis of tumorigenic and metastatic breast cancer markers. Funct. Integr. Genomics, 2011, 11, 225-239.
[36]
Yusenko, M.V.; Ruppert, T.; Kovacs, G. Analysis of differentially expressed mitochondrial proteins in chromophobe renal cell carcinomas and renal oncocytomas by 2-D gel electrophoresis. Int. J. Biol. Sci., 2010, 6, 213.
[37]
Chen, Z.; Pervaiz, S. Involvement of cytochrome C oxidase subunits Va and Vb in the regulation of cancer cell metabolism by Bcl-2. Cell Death Differ., 2010, 17(3), 408.