Changes in the Protein Profile of Cervical Cancer Mice Xenograft Model in Response to Streblus asper Treatment


  • Advanced Medical and Dental Institute, Universiti Sains Malaysia, 13200 Kepala Batas, Pulau Pinang
  • Advanced Medical and Dental Institute, Universiti Sains Malaysia, 13200 Kepala Batas, Pulau Pinang
  • Faculty of Health Science, Universiti Teknologi MARA, Cawangan Pulau Pinang, Kampus Bertam, 13200 Kepala Batas, Pulau Pinang
  • Malaysian Institute of Pharmaceuticals and Neutraceuticals, National Institute of Biotechnology
  • Faculty of Health Science, Universiti Teknologi MARA, Cawangan Pulau Pinang, Kampus Bertam, 13200, Kepala Batas, Pulau Pinang



Anticancer, Cervical Cancer, In vivo, Proteomics, Streblus asper, Xenograft


Cervical cancer is the third most prevalent cancer in females (2018) with an estimation of 569,847 incidences and 311,365 deaths worldwide despite the rapid advancement of current technology in treating cervical cancer. Radiotherapy and chemotherapy pose side effects and subsequently hinder treatment efficacy. Therefore, taken together with the previous reports of the plants' ability in treating cancers, Streblus asper is suggested to be a potential candidate for cervical cancer. This study was conducted to investigate the anti-cervical cancer potential of Streblus asper through the identification of key proteins and their expression that are regulated in the treatment using mice xenograft model. By employing the use of Liquid Chromatography Mass Spectrometry (LCMS), several proteins associated with cancer growth mechanisms were successfully identified. Four-hundred and fifty-two proteins common to both groups were identified, and 122 proteins were found able to be quantified. Among those proteins, 52 proteins were expressed more than 2-fold changes and 12 proteins were selected based on its established relationship with cancers, including annexin A2, 14-3-3 protein, transgelin-2, galectin-1, keratin, heat shock protein 10 and 70, glucose regulated protein (78kDa), gelsolin, alpha enolase, cofilin-1, vimentin, and calreticulin. All these proteins were downregulated upon treatment of cervical cancer tumour by Streblus asper. Pathway enrichment analysis revealed 40 related pathways which include among others, metabolism of protein, post-translational protein modification, cellular responses to external stimuli and stress, cell cycle, and apoptosis. These analyses may improve our molecular insight of the mechanisms involved in the treatment of cervical cancer tumour by Streblus asper extract.


Download data is not yet available.


Metrics Loading ...


Bruni L, Barrionuevo-Rosas L, Albero G, Aldea M, Serrano B, Valencia S, et al. Human papillomavirus and related diseases in Malaysia. ICO/IARC Inf Cent HPV Cancer (HPV Inf Centre); 2018 Dec.

Torre LA, Siegel RL, Ward EM, Jemal A. Global cancer incidence and mortality rates and trends--An update. Cancer Epidemiology, Biomarkers & Prevention. 2016 Jan; 25(1):16–27. PMid:26667886

Kleine W, Rau K, Schwoeorer D, Pfleiderer A. Prognosis of the adenocarcinoma of the cervix uteri: A comparative study. Gynecologic Oncology. 1989; 35(2):145–9.

Rizzo AE, Feldman S. Update on primary HPV screening for cervical cancer prevention. Current Problems in Cancer. 2018 ;0:1–14.

Ramakrishnan S, Partricia S, Mathan G. ScienceDirect overview of high-risk HPV ‘ s 16 and 18 infected cervical cancer: Pathogenesis to prevention. Biomedicine & Pharmacotherapy. 2015; 70:103–10. PMid:25776487

Sankaranarayanan R, Joshi S, Muwonge R, Esmy PO, Basu P, Prabhu P, et al. Can a single dose of human papillomavirus (HPV) vaccine prevent cervical cancer? Early findings from an Indian study. Vaccine. 2018 Aug; 36(32 Pt A):4783–91. https:// PMid:29551226

Bonanni P, Zanella B, Santomauro F, Lorini C, Bechini A, Boccalini S. Safety and perception: What are the greatest enemies of HPV vaccination programmes? Vaccine. 2018; 36(36):5424–9. PMid:28610824

Laurent J, Luckett R, Feldman S. HPV vaccination and the effects on rates of HPV-related cancers. Current Problems in Cancer. 2018; 42(5):493–506. PMid:30041818

Levin A, Wang SA, Levin C, Tsu V, Hutubessy R. Costs of introducing and delivering HPV vaccines in low and lower middle income countries: Inputs for GAVI policy on introduction grant support to countries. PLoS One. 2014; 9(6). PMid:24968002. PMCid:PMC4072768

Nickel B, Dodd RH, Turner RM, Waller J, Marlow L, Zimet G, et al. Factors associated with the human papillomavirus (HPV) vaccination across three countries following vaccination introduction. 2017; 8(May):169–76. PMid:29062681. PMCid:PMC5645176

Priaulx J, de Koning HJ, de Kok IMCM, Széles G, McKee M. Identifying the barriers to effective breast, cervical and colorectal cancer screening in thirty one European countries using the Barriers to Effective Screening Tool (BEST). Health Policy (New York). 2018. PMid:30177278

Lobo N, Kulkarni M, Hughes S, Nair R, Khan MS, Thurairaja R. Urological complications following pelvic radiotherapy. Urology. 2018. PMid:30036617

Overbeek A, van den Berg MH, van Leeuwen FE, Kaspers GJL, Lambalk CB, van Dulmen-den Broeder E. Chemotherapyrelated late adverse effects on ovarian function in female survivors of childhood and young adult cancer: A systematic review. Cancer Treatment Reviews. 2017; 53:10–24. PMid:28056411

Gunderson CC, Matulonis U, Moore KN. Management of the toxicities of common targeted therapeutics for gynecologic cancers. Gynecologic Oncology. 2018; 148(3):591–600. https:// PMid:29395304

Rastogi S, Kulshreshtha DK, Rawat AKS. Streblus asper Lour. (Shakhotaka): A Review of its Chemical, Pharmacological and Ethnomedicinal Properties. Evidence-Based Complementary and Alternative Medicine. 2006 Jun; 3(2):217–22. PMid:16786051. PMCid:PMC1475940

Taweechaisupapong S, Choopan T, Singhara S, Chatrchaiwiwatana S, Wongkham S. In vitro inhibitory effect of Streblus asper leaf-extract on adhesion of Candida albicans to human buccal epithelial cells. Journal of Ethnopharmacology. 2005 Jan; 96(1–2):221–6. https:// PMid:15588674

Taweechaisupapong S, Klanrit P, Singhara S, Pitiphat W, Wongkham S. Inhibitory effect of Streblus asper leafextract on adhesion of Candida albicans to denture acrylic. Journal of Ethnopharmacology. 2006 Jul; 106(3):414–7. PMid:16529890

Chatterjee RK, Fatma N, Murthy PK, Sinha P, Kulshrestha DK, Dhawan BN. Macrofilaricidal activity of the stembark of Streblus asper and its major active constituents. Drug Development Research. 1992; 26(1):67–78.

Taweechaisupapong S, Wongkham S, Chareonsuk S, Suparee S, Srilalai P, Chaiyarak S. Selective activity of Streblus asper on Mutans streptococci. Journal of Ethnopharmacology. 2000 Apr; 70(1):73–9.

Chen H, Li J, Wu Q, Niu XT, Tang MT, Guan XL, et al. AntiHBV activities of Streblus asper and constituents of its roots. Fitoterapia. 2012; 83(4):643–9. PMid:22305944

Li J, Huang Y, Guan X-L, Li J, Deng S-P, Wu Q, et al. Anti-hepatitis B virus constituents from the stem bark of Streblus asper. Phytochemistry. 2012 Oct; 82:100–9. PMid:22818524

Li L-Q, Li J, Huang Y, Wu Q, Deng S-P, Su X-J, et al. Lignans from the heartwood of Streblus asper and their inhibiting activities to hepatitis B virus. Fitoterapia. 2012 Mar; 83(2):303–9. PMid:22119765

Sripanidkulchai B, Junlatat J, Wara-aswapati N, Hormdee D. Anti-inflammatory effect of Streblus asper leaf extract in rats and its modulation on inflammation-associated genes expression in RAW 264.7 macrophage cells. Journal of Ethnopharmacology. 2009 Jul; 124(3):566–70. PMid:19439173

Kumar RBS, Kar B, Dolai N, Bala A, Haldar PK. Evaluation of antihyperglycemic and antioxidant properties of Streblus asper Lour against streptozotocin-induced diabetes in rats. Asian Pacific Journal of Tropical Disease. 2012; 2(2):139–43.

Choudhury MK, Venkatraman S, Upadhyay L. Phytochemical analysis and peripheral glucose utilization activity determination of Steblus asper. Asian Pacific Journal of Tropical Disease. 2012; 2(2):s656–61.

Phutdhawong W, Donchai A, Korth J, Pyne SG, Picha P, Ngamkham J, et al. The components and anticancer activity of the volatile oil from Streblus asper. Flavour and Fragrance Journal. 2004; 19(5):445–7.

Seeni A, Ayunie N, Abdul Wahab R. Apoptosis Inducer from Streblus asper Extracts for Cancer Chemoprevention. In: Novel Apoptotic Regulators in Carcinogenesis; 2012. p. 1–25. https://

Nabil M, Seeni A, Ismail WI, Rahim NA. Proteomic analysis of anti-cancer effects of streblus asper root extract on HeLa Cancer Cells. 2019; 12(Sep):1263–77.

Nabil M, Seeni A, Ismail WI, Ab N. Induction of apoptotic mechanism by streblus asper root extract on cervical cancer using in vitro and in vivo models. 2019; 12(Dec):1661–73.

Oghenesuvwe EE, Nwoke E, Lotanna AD. Guidelines on dosage calculation and stock solution preparation in experimental animals' studies. 2014; 4(18):100–6.

Huebner K, Cannizzaro LA, Frey AZ, Hecht BK, Hecht F, Croce CM, et al. Chromosomal localization of the human genes for lipocortin I and lipocortin II. Oncogene Research. 1988; 2(4):299–310.

Inokuchi J, Narula N, Yee DS, Skarecky DW, Lau A, Ornstein DK, et al. Annexin A2 positively contributes to the malignant phenotype and secretion of IL"6 in DU145 prostate cancer cells. International Journal of Cancer. 2009; 124(1):68–74. PMid:18924133

Mohammad HS, Kurokohchi K, Yoneyama H, Tokuda M, Morishita A, Jian G, et al. Annexin A2 expression and phosphorylation are up-regulated in hepatocellular carcinoma. International Journal of Oncology. 2008; 33(6):1157–63.

Sharma MR, Koltowski L, Ownbey RT, Tuszynski GP, Sharma MC. Angiogenesis-associated protein annexin II in breast cancer: selective expression in invasive breast cancer and contribution to tumor invasion and progression. Experimental and Molecular Pathology. 2006; 81(2):146–56. PMid:16643892

Vishwanatha JK, Chiang Y, Kumble KD, Hollingsworth MA, Pour PM. Enhanced expression of annexin II in human pancreatic carcinoma cells and primary pancreatic cancers. Carcinogenesis. 1993; 14(12):2575–9. carcin/14.12.2575. PMid:8269629

Mussunoor S, Murray GI. The role of annexins in tumour development and progression. Pathological Society of Great Britain and Ireland. 2008; 216(2):131–40. PMid:18698663

Bae SM, Lee C-H, Cho YL, Nam KH, Kim YW, Kim CK, et al. Two-dimensional gel analysis of protein expression profile in squamous cervical cancer patients. Gynecologic Oncology. 2005 Oct; 99(1):26–35. PMid:16051329

Hellman K, Alaiya AA, Becker S, Lomnytska M, Schedvins K, Steinberg W, et al. Differential tissue-specific protein markers of vaginal carcinoma. British Journal of Cancer. 2009; 100(8):1303. PMid:19367286. PMCid:PMC2676541

Khorrami A, Sharif Bagheri M, Tavallaei M, Gharechahi J. The functional significance of 14-3-3 proteins in cancer: Focus on lung cancer. Hormone Molecular Biology and Clinical Investigation. 2017 Aug; 32(3). PMid:28779564

Wilker E, Yaffe MB. 14-3-3 Proteins--a focus on cancer and human disease. Journal of Molecular and Cellular Cardiology. 2004 Sep; 37(3):633–42. PMid:15350836

Liu T-A, Jan Y-J, Ko B-S, Liang S-M, Chen S-C, Wang J, et al. 14-3-3ε overexpression contributes to epithelial-mesenchymal transition of hepatocellular carcinoma. PLoS One. 2013 Mar 6; 8(3):e57968. PMid:23483955 PMCid:PMC3590290

Pulukuri SM, Estes N, Rao JS. 14-3-3 sigma promotes cell survival in human prostate cancer cells. Cancer Research. 2005; 65(9 Supplement):229.

Xiao Y, Lin VY, Ke S, Lin GE, Lin F-T, Lin W-C. 14-3-3Ï„ Promotes breast cancer invasion and metastasis by inhibiting RhoGDIα. Molecular and Cellular Biology. 2014; 34(14):2635– 49. PMid:24820414. PMCid:PMC4097670

Liu T, Jan Y, Ko B, Hung Y, Hsu C, Shen T, et al. Increased Expression of 14-3-3 β Promotes Tumor Progression and Predicts Extrahepatic Metastasis and Worse Survival in Hepatocellular Carcinoma. 2011; 179(6):2698–708. PMid:21967815. PMCid:PMC3260858

Li Z, Zhao J, Du Y, Park HR, Sun S-Y, Bernal-Mizrachi L, et al. Down-regulation of 14-3-3ζ suppresses anchorageindependent growth of lung cancer cells through anoikis activation. Proc Natl Acad Sci. 2008; 105(1):162–7. PMid:18162532. PMCid:PMC2224179

Zhang W, Shen Q, Chen M, Wang Y, Zhou Q, Tao X, et al. The role of 14-3-3 proteins in gynecological tumors CANCER 3. 1. Changes in 14-3-3 proteins in cervical carcinogenesis 3. 2. Roles of 14-3-3 proteins in the treatment of cervical cancer. Frontiers in Bioscience. 2015; 934–45. PMid:25961534

Dvorakova M, Nenutil R, Bouchal P. Transgelins, cytoskeletal proteins implicated in different aspects of cancer development. Expert Review of Proteomics. 2014 Apr; 11(2):149–65. PMid:24476357

Kristo I, Bajusz I, Bajusz C, Borkuti P, Vilmos P. Actin, actinbinding proteins, and actin-related proteins in the nucleus. Histochemistry and Cell Biology. 2016 Apr; 145(4):373–88. PMid:26847179

Meng T, Liu L, Hao R, Chen S, Dong Y. Transgelin-2: A potential oncogenic factor. Tumor Biolody. 2017; (277). PMid:28639888

Fukushima C, Murakami A, Yoshitomi K, Sueoka K, Nawata S, Nakamura K, et al. Comparative proteomic profiling in squamous cell carcinoma of the uterine cervix. Proteomics – Clinical Applications. 2011 Apr 1; 5(3–4):133–40. PMid:21365771

Yakabe K, Murakami A, Kajimura T, Nishimoto Y, Sueoka K, Sato S, et al. Functional significance of transgelin-2 in uterine cervical squamous cell carcinoma. Journal of Obstetrics and Gynaecology Research. 2016 May; 42(5):566–72. PMid:26891454

Ebrahim AH, Alalawi Z, Mirandola L, Rakhshanda R, Dahlbeck S, Nguyen D, et al. Galectins in cancer: Carcinogenesis, diagnosis and therapy. Annals of Translational Medicine. 2014 Sep; 2(9):88.

Dalotto-Moreno T, Croci DO, Cerliani JP, Martinez-Allo VC, Dergan-Dylon S, Mendez-Huergo SP, et al. Targeting galectin-1 overcomes breast cancer-associated immunosuppression and prevents metastatic disease. Cancer Research. 2013 Feb; 73(3):1107–17. PMid:23204230

Compagno D, Gentilini LD, Jaworski FM, Perez IG, Contrufo G, Laderach DJ. Glycans and galectins in prostate cancer biology, angiogenesis and metastasis. Glycobiology. 2014 Oct; 24(10):899–906. PMid:24939371

Carlini MJ, Roitman P, Nuñez M, Pallotta MG, Boggio G, Smith D, et al. Clinical relevance of galectin-1 expression in non-small cell lung cancer patients. Lung Cancer. 2014; 84(1):73–8. https:// PMid:24560493

Kim H-J, Do I-G, Jeon H-K, Cho YJ, Park YA, Choi J-J, et al. Galectin 1 expression is associated with tumor invasion and metastasis in stage IB to IIA cervical cancer. Human Pathology. 2013; 44(1):62–8. PMid:22939954

Magin TM, Vijayaraj P, Leube RE. Structural and regulatory functions of keratins. Experimental Cell Research. 2007 Jun; 313(10):2021–32. PMid:17434482

Karantza V. Keratins in health and cancer: more than mere epithelial cell markers. Oncogene. 2011 Jan; 30(2):127–38. PMid:20890307. PMCid:PMC3155291

Alix-Panabières C, Vendrell J-P, Slijper M, Pellé O, Barbotte E, Mercier G, et al. Full-length cytokeratin-19 is released by human tumor cells: a potential role in metastatic progression of breast cancer. Breast Cancer Research. 2009 Jun; 11(3):R39. PMid:19549321. PMCid:PMC2716508

Ding S-J, Li Y, Tan Y-X, Jiang M-R, Tian B, Liu Y-K, et al. From Proteomic Analysis to Clinical Significance. Molecular & Cellular Proteomics. 2004; 3(1):73–81. mcp.M300094-MCP200. PMid:14593079

Somiari RI, Sullivan A, Russell S, Somiari S, Hu H, Jordan R, et al. High-throughput proteomic analysis of human infiltrating ductal carcinoma of the breast. Proteomics. 2003 Oct; 3(10):1863–73. PMid:14625848

Jia H, Halilou AI, Hu L, Cai W, Liu J, Huang B. Heat shock protein 10 (Hsp10) in immune-related diseases: One coin, two sides. International Journal of Biochemistry and Molecular Biology. 2011; 2(1):47–57.

Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones. 2005 Jun; 10(2):86–103. PMid:16038406. PMCid:PMC1176476

Wang J-T, Ding L, Jiang S-W, Hao J, Zhao W-M, Zhou Q, et al. Folate deficiency and aberrant expression of DNA methyltransferase 1 were associated with cervical cancerization. Current Pharmaceutical Design. 2014; 20(11):1639–46.

Wu J, Liu T, Rios Z, Mei Q, Lin X, Cao S. Heat Shock Proteins and Cancer. Trends in Pharmacological Sciences. 2017 Mar 1; 38(3):226–56. PMid:28012700

Cappello F, Bellafiore M, David S, Anzalone R, Zummo G. Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix. Cancer Letters. 2003 Jun; 196(1):35–41.

Cappello F. HSP60 and HSP10 as diagnostic and prognostic tools in the management of exocervical carcinoma. Vol. 91, Gynecologic Oncology. United States; 2003. p. 661. PMid:14675699

Tetu B, Popa I, Bairati I, L'Esperance S, Bachvarova M, Plante M, et al. Immunohistochemical analysis of possible chemoresistance markers identified by micro-arrays on serous ovarian carcinomas. Modern Pathology features diagnostic anatomic pathology Inc. 2008 Aug; 21(8):1002–10. PMid:18500265

Kumar S, Stokes J, Singh UP, Gunn KS, Acharya A, Manne U, et al. Targeting Hsp70: A possible therapy for cancer. Cancer Letters. 2017; 374:156–66. PMid:26898980. PMCid:PMC5553548

Lee AS. Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential. Nature Reviews Cancer. 2014 Apr; 14(4):263–76. PMid:24658275. PMCid:PMC4158750

Dong D, Stapleton C, Luo B, Xiong S, Ye W, Zhang Y, et al. A critical role for GRP78/BiP in the tumor microenvironment for neovascularization during tumor growth and metastasis. Cancer Research. 2011; 71(8):2848–57. PMid:21467168. PMCid:PMC3078191

Li Z, Zhang L, Zhao Y, Li H, Xiao H, Fu R, et al. Cell-surface GRP78 facilitates colorectal cancer cell migration and invasion. International Journal of Biochemistry & Cell Biology. 2013; 45(5):987–94. PMid:23485528

Winder SJ, Kathryn R, Winder SJ, Ayscough KR. Actin-binding proteins Actin-binding Proteins. 2005; 2005(L):651–4. https:// PMid:15701920

Deng R, Hao J, Han W, Ni Y, Huang X, Hu Q. Gelsolin regulates proliferation, apoptosis, migration and invasion in human oral carcinoma cells. Oncology Letters. 2015 May; 9(5):2129– 34. PMid:26137026. PMCid:PMC4467278

An J-H, Kim J-W, Jang S-M, Kim C-H, Kang E-J, Choi K-H. Gelsolin negatively regulates the activity of tumor suppressor p53 through their physical interaction in hepatocarcinoma HepG2 cells. Biochemical and Biophysical Research Communications. 2011 Aug; 412(1):44–9. PMid:21801713

Liao C-J, Wu T-I, Huang Y-H, Chang T-C, Wang C-S, Tsai M-M, et al. Overexpression of gelsolin in human cervical carcinoma and its clinicopathological significance. Gynecologic Oncology. 2011 Jan; 120(1):135–44. PMid:21035170

Fu Q, Liu Y, Fan Y, Hua S, Qu H, Dong S, et al. Alpha-enolase promotes cell glycolysis, growth, migration, and invasion in non-small cell lung cancer through FAK-mediated PI3K / AKT pathway. 2015; 1–13. PMid:25887760. PMCid:PMC4359783

Song Y, Luo Q, Long H, Hu Z, Que T, Zhang X, et al. Alphaenolase as a potential cancer prognostic marker promotes cell growth, migration, and invasion in glioma. 2014; 1–12. PMid:25600072. PMCid:PMC4464720

Sun L, Lu T, Tian K, Zhou D, Yuan J, Wang X, et al. Alphaenolase promotes gastric cancer cell proliferation and metastasis via regulating AKT signaling pathway. European Journal of Pharmacology. 2019 Feb; 845:8215. PMid:30582908

Sun L, Guo C, Cao J, Burnett J, Yang Z, Ran Y, et al. Overexpression of alpha-enolase as a prognostic biomarker in patients with pancreatic cancer. International Journal of Medical Sciences. 2017; 14(7):655–61. ijms.18736. PMid:28824297. PMCid:PMC5562116

Bamburg JR, Mcgough A. Putting a new twist on actin: ADF / cofilins modulate actin dynamics. 1999; 9(Sep):364–70. https://

Ding S, Li Y, Shao X, Zhou H, Zeng R, Tang Z, et al. Proteome analysis of hepatocellular carcinoma cell strains, MHCC97"H and MHCC97"L, with different metastasis potentials. Proteomics. 2004; 4(4):982–94. pmic.200300653. PMid:15048980

Dowling P, Meleady P, Dowd A, Henry M, Glynn S, Clynes M. Proteomic analysis of isolated membrane fractions from superinvasive cancer cells. Biochim Biophys Acta (BBA)Proteins Proteomics. 2007; 1774(1):93–101. PMid:17085086

Keshamouni VG, Michailidis G, Grasso CS, Anthwal S, Strahler JR, Walker A, et al. Differential protein expression profiling by iTRAQ− 2DLC− MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype. Journal of Proteome Research. 2006; 5(5):1143–54. PMid:16674103

Martoglio A-M, Tom BDM, Starkey M, Corps AN, CharnockJones DS, Smith SK. Changes in tumorigenesis-and angiogenesis-related gene transcript abundance profiles in ovarian cancer detected by tailored high density cDNA arrays. Molecular Medicine. 2000; 6(9):750. BF03402191

Sinha P, Hütter G, Köttgen E, Dietel M, Schadendorf D, Lage H. Increased expression of epidermal fatty acid binding protein, cofilin, and 14"3"3"σ (stratifin) detected by twodimensional gel electrophoresis, mass spectrometry and microsequencing of drug"resistant human adenocarcinoma of the pancreas. Electrophoresis. 1999; 20(14):2952–60.<2952::AIDELPS2952>3.0.CO;2-H

Turhani D, Krapfenbauer K, Thurnher D, Langen H, Fountoulakis M. Identification of differentially expressed, tumor"associated proteins in oral squamous cell carcinoma by proteomic analysis. Electrophoresis. 2006; 27(7):1417–23. PMid:16568407

Unwin RD, Craven RA, Harnden P, Hanrahan S, Totty N, Knowles M, et al. Proteomic changes in renal cancer and coordinate demonstration of both the glycolytic and mitochondrial aspects of the Warburg effect. Proteomics. 2003; 3(8):1620–32. PMid:12923786

Mousavi S, Safaralizadeh R, Hosseinpour-Feizi M, AzimzadehIsfanjani A, Hashemzadeh S. Study of cofilin 1 gene expression in colorectal cancer. Journal of Gastrointestinal Oncology. 2018 Oct; 9(5):791–6.

Pappa KI, Lygirou V, Kontostathi G, Zoidakis J, Makridakis M, Vougas K, et al. Proteomic analysis of normal and cancer cervical cell lines reveals deregulation of cytoskeleton-associated proteins. Cancer Genomics Proteomics. 2017; 14(4):253– 66. PMid:28647699. PMCid:PMC5572303

Polachini GM, Sobral LM, Mercante AMC, Paes-Leme AF, Xavier FCA, Henrique T, et al. Proteomic approaches identify members of cofilin pathway involved in oral tumorigenesis. PLoS One. 2012; 7(12):e50517. PMid:23227181. PMCid:PMC3515627

Wang F, Wu D, Fu H, He F, Xu C, Zhou J, et al. Cofilin 1 promotes bladder cancer and is regulated by TCF7L2. Oncotarget. 2017 Sep 6; 8(54):92043–54. oncotarget.20664. PMid:29190896. PMCid:PMC5696162

Wang Y, Kuramitsu Y, Ueno T, Suzuki N, Yoshino S, Iizuka N, et al. Differential expression of up-regulated cofilin-1 and downregulated cofilin-2 characteristic of pancreatic cancer tissues. Oncology Reports. 2011; 26(6):1595–9.

Yang Z-L, Miao X, Xiong L, Zou Q, Yuan Y, Li J, et al. CFL1 and Arp3 are biomarkers for metastasis and poor prognosis of squamous cell/adenosquamous carcinomas and adenocarcinomas of gallbladder. Cancer Investigation. 2013; 31(2):132–9. PMid:2332082

Satelli A, Li S. Vimentin in cancer and its potential as a molecular target for cancer therapy. Cellular and Molecular Life Sciences. 2011 Sep; 68(18):3033–46. PMid:21637948. PMCid:PMC3162105

Gilles C, Polette M, Piette J, Delvigne A, Thompson EW, Foidart J, et al. Vimentin expression in cervical carcinomas: association with invasive and migratory potential. Journal of Pathology. 1996; 180(2):175–80.<175::AID-PATH630>3.0.CO;2-G

Gilles C, Polette M, Mestdagt M, Nawrocki-Raby B, Ruggeri P, Birembaut P, et al. Transactivation of vimentin by β-catenin in human breast cancer cells. Cancer Research. 2003; 63(10):2658– 64. PMid:12750294

Hong S-H, Misek DE, Wang H, Puravs E, Hinderer R, Giordano TJ, et al. Identification of a specific vimentin isoform that induces an antibody response in pancreatic cancer. Biomark Insights. 2006; 1.

Jin H, Morohashi S, Sato F, Kudo Y, Akasaka H, Tsutsumi S, et al. Vimentin expression of esophageal squamous cell carcinoma and its aggressive potential for lymph node metastasis. Biomedical Research. 2010; 31(2):105–12. biomedres.31.105. PMid:20460738

Ngan CY, Yamamoto H, Seshimo I, Tsujino T, Man-i M, Ikeda JI, et al. Quantitative evaluation of vimentin expression in tumour stroma of colorectal cancer. British Journal of Cancer. 2007; 96(6):986. PMid:17325702. PMCid:PMC2360104

Takemura K, Hirayama R, Hirokawa K, Inagaki M, Tsujimura K, Esaki Y, et al. Expression of vimentin in gastric cancer: a possible indicator for prognosis. Pathobiology. 1994; 62(3):149–54. PMid:7945921

Wu M, Bai X, Xu G, Wei J, Zhu T, Zhang Y, et al. Proteome analysis of human androgen"independent prostate cancer cell lines: Variable metastatic potentials correlated with vimentin expression. Proteomics. 2007; 7(12):1973–83. PMid:17566973

Vuoriluoto K, Haugen H, Kiviluoto S, Mpindi JP, Nevo J, Gjerdrum C, et al. Vimentin regulates EMT induction by Slug and oncogenic H-Ras and migration by governing Axl expression in breast cancer. Oncogene. 2011; 30(12):1436. PMid:21057535

Walsh N, O'Donovan N, Kennedy S, Henry M, Meleady P, Clynes M, et al. Identification of pancreatic cancer invasionrelated proteins by proteomic analysis. Proteome Science. 2009; 7(1):3. PMid:19216797. PMCid:PMC2646716

Chen C-N, Chang C-C, Su T-E, Hsu W-M, Jeng Y-M, Ho M-C, et al. Identification of calreticulin as a prognosis marker and angiogenic regulator in human gastric cancer. Annals of Surgical Oncology. 2009; 16(2):524–33. PMid:19050968

Sheng W, Chen C, Dong M, Zhou J, Liu Q, Dong Q, et al. Overexpression of calreticulin contributes to the development and progression of pancreatic cancer. Journal of Cellular Physiology. 2014; 229(7):887–97. jcp.24519. PMid:24264800

Vaksman O, Davidson B, Tropé C, Reich R. Calreticulin expression is reduced in high-grade ovarian serous carcinoma effusions compared with primary tumors and solid metastases. Human Pathology. 2013; 44(12):2677–83. PMid:24060004

Alfonso P, Núñez A, Madoz"Gurpide J, Lombardia L, Sánchez L, Casal JI. Proteomic expression analysis of colorectal cancer by two"dimensional differential gel electrophoresis. Proteomics. 2005; 5(10):2602–11. PMid:15924290

Du X-L, Hu H, Lin D-C, Xia S-H, Shen X-M, Zhang Y, et al. Proteomic profiling of proteins dysregulted in Chinese esophageal squamous cell carcinoma. Journal of Molecular Medicine. 2007; 85(8):863–75. PMid:17318615

Harada K, Takenawa T, Ferdous T, Kuramitsu Y, Ueyama Y. Calreticulin is a novel independent prognostic factor for oral squamous cell carcinoma. Oncology Letters. 2017 Jun; 13(6):4857– 62. PMid:28599487. PMCid:PMC5452987

Kageyama S, Isono T, Iwaki H, Wakabayashi Y, Okada Y, Kontani K, et al. Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine. Clinical Chemistry. 2004; 50(5):857–66. clinchem.2003.027425. PMid:14764641

Matsukuma S, Yoshimura K, Ueno T, Oga A, Inoue M, Watanabe Y, et al. Calreticulin is highly expressed in pancreatic cancer stem-like cells. Cancer Science. 2016 Nov 1; 107(11):1599–609. PMid:27561105. PMCid:PMC5132278

Zamanian M, Qader Hamadneh LA, Veerakumarasivam A, Abdul Rahman S, Shohaimi S, Rosli R. Calreticulin mediates an invasive breast cancer phenotype through the transcriptional dysregulation of p53 and MAPK pathways. Cancer Cell International. 2016; 16(1):56. PMid:27418879. PMCid:PMC4944499

Opas M, Szewczenko-Pawlikowski M, Jass GK, Mesaeli N, Michalak M. Calreticulin modulates cell adhesiveness via regulation of vinculin expression. Journal of Cell Biology. 1996; 135(6):1913–23. PMid:8991101. PMCid:PMC2133944

Lu Y-C, Chen C-N, Wang B, Hsu W-M, Chen S-T, Chang K-J, et al. Changes in tumor growth and metastatic capacities of J82 human bladder cancer cells suppressed by down-regulation of calreticulin expression. American Journal of Pathology. 2011; 179(3):1425–33. PMid:21723245. PMCid:PMC3157280

Lu Y-C, Weng W-C, Lee H. Functional roles of calreticulin in cancer biology. BioMed Research International. 2015.




How to Cite

Nabil, M., Seeni, A., Ismahanisa Ismail, W., Hafiz Mail, M., & Rahim, N. A. (2020). Changes in the Protein Profile of Cervical Cancer Mice Xenograft Model in Response to <i>Streblus asper</i> Treatment. Journal of Natural Remedies, 20(3), 149–165.



Research Articles