Colorectal cancer (CRC) is one of the most malignant tumors in both sexes among all types of tumors worldwide. Up to now, no precise biomarker has been capable of accurately predicting the prognosis for patients with CRC. Therefore, it is essential for us to find a new biomarker to predict the prognosis, overall survival, and disease-free survival of patients with CRC, especially for those patients who have a distant metastasis. There is a growing concern over the issues that osteopontin (OPN), a multifunction phosphorylated protein, has been identified in recent years among multiple tumors types, including CRC. There is increasing evidence showing that high expression of OPN is related to the proliferation, invasion and metastasis of CRC. OPN could support malignant formation by inducing tumor angiogenesis; aggravating the degradation of extracellular matrix; promoting chemo taxis, adhesion, and metastasis of tumors and affecting tumor immunity and apoptosis based on various complex mechanisms. More intensive studies are required in the future to clarify the roles of OPN and its related genes, relevant receptors, protein structure, biological features, and complex molecular mechanisms in colorectal carcinogenesis, as well as to develop beneficial agents for the clinical treatment of CRC to improve patient prognosis.
Ferlay, J., et al. (2015) Cancer Incidence and Mortality Worldwide: Sources, Methods and Major Patterns in GLOBOCAN 2012. International Journal of Cancer, 136, E359-86. http://dx.doi.org/10.1002/ijc.29210
Laubert, T., et al. (2015) Stage-Specific Frequency and Prognostic Significance of Aneuploidy in Patients with Sporadic Colorectal Cancer—A Meta-Analysis and Current Overview. International Journal of Colorectal Disease, 30, 1015-1028. http://dx.doi.org/10.1007/s00384-015-2259-x
King, L.E., et al. (2016) Differential RNA-Seq Analysis Comparing APC-Defective and APC-Restored SW480 Colorectal Cancer Cells. Genomics Data, 7, 293-296. http://dx.doi.org/10.1016/j.gdata.2016.02.001
Jiang, H.W., et al. (2015) Influence of the DCC Gene on Proliferation and Carcinoembryonic Antigen Expression in the Human Colorectal Cancer Cell Line SW1116. Genetics and Molecular Research, 14, 10273-10280. http://dx.doi.org/10.4238/2015.August.28.12
Al-Khayal, K., et al. (2016) Identification of the TP53-Induced Glycolysis and Apoptosis Regulator in Various Stages of Colorectal Cancer Patients. Oncology Reports, 35, 1281-1286.
Osumi, H., et al. (2016) RAS Mutation Is a Prognostic Biomarker in Colorectal Cancer Patients with Metastasectomy. International Journal of Cancer, 139, 803-811. http://dx.doi.org/10.1002/ijc.30106
Qu, L., et al. (2013) Inhibitory Effect of Upregulated DR-nm23 Expression on Invasion and Metastasis in Colorectal Cancer. European Journal of Cancer Prevention, 22, 512-522. http://dx.doi.org/10.1097/CEJ.0b013e328361625d
Friedman, K., et al. (2016) Medullary Carcinoma of the Colon: A Distinct Morphology Reveals a Distinctive Immunoregulatory Microenvironment. Modern Pathology, 29, 528-541. http://dx.doi.org/10.1038/modpathol.2016.54
Bolocan, A., et al. (2012) Prognostic and Predictive Factors in Colorectal Cancer. Chirurgia (Bucur), 107, 555-563.
Senger, D.R., Wirth, D.F. and Hynes, R.O. (1979) Transformed Mammalian Cells Secrete Specific Proteins and Phosphoproteins. Cell, 16, 885-893. http://dx.doi.org/10.1016/0092-8674(79)90103-X
Zhang, H., et al. (2014) Osteopontin Knockdown Inhibits Alphav, Beta3 Integrin-Induced Cell Migration and Invasion and Promotes Apoptosis of Breast Cancer Cells by Inducing Autophagy and Inactivating the PI3K/Akt/mTOR Pathway. Cellular Physiology and Biochemistry, 33, 991-1002. http://dx.doi.org/10.1159/000358670
Li, Y.S., et al. (2015) Role of Osteopontin in Osteosarcoma. Medical Oncology, 32, 449. http://dx.doi.org/10.1007/s12032-014-0449-y
Sun, C.C., Qu, X.J. and Gao, Z.H. (2016) Arginine-Glycine-Aspartate-Binding Integrins as Therapeutic and Diagnostic Targets. American Journal of Therapeutics, 23, e198-207. http://dx.doi.org/10.1097/MJT.0000000000000053
Beausoleil, M.S., et al. (2011) Deletion of the Thrombin Cleavage Domain of Osteopontin Mediates Breast Cancer Cell Adhesion, Proteolytic Activity, Tumorgenicity, and Metastasis. BMC Cancer, 11, 25. http://dx.doi.org/10.1186/1471-2407-11-25
Stemberger, C., et al. (2014) Osteopontin Is Associated with Decreased Apoptosis and Alphav Integrin Expression in Lung Adenocarcinoma. Acta Histochemica, 116, 222-229. http://dx.doi.org/10.1016/j.acthis.2013.07.009
Chen, Q., et al. (2014) An Osteopontin-Integrin Interaction Plays a Critical Role in Directing Adipogenesis and Osteogenesis by Mesenchymal Stem Cells. Stem Cells, 32, 327-337. http://dx.doi.org/10.1002/stem.1567
Jin, Y., et al. (2014) OPN and αvβ3 Expression Are Predictors of Disease Severity and Worse Prognosis in Hepatocellular Carcinoma. PLoS ONE, 9, e87930. http://dx.doi.org/10.1371/journal.pone.0087930
Mittelbronn, M., et al. (2013) Expression of Integrins αvβ3 andαvβ5 and Their Ligands in Primary and Secondary Central Nervous System Neoplasms. Histology and Histopathology, 28, 749-758.
Mizuno, Y., et al. (2015) Improvement of Cardiac Function after Implanting the Osteopontin-Derived Peptide SVVYGLR in a Hamster Model of Dilated Cardiomyopathy. Interactive Cardiovascular and Thoracic Surgery, 21, 506-514. http://dx.doi.org/10.1093/icvts/ivv197
Sharon, Y., et al. (2015) Tumor-Derived Osteopontin Reprograms Normal Mammary Fibroblasts to Promote Inflammation and Tumor Growth in Breast Cancer. Cancer Research, 75, 963-973. http://dx.doi.org/10.1158/0008-5472.CAN-14-1990
Fok, T.C., et al. (2014) Expression and Localization of Osteopontin, Homing Cell Adhesion Molecule/CD44, and Integrin αvβ3 in Mucoepidermoid Carcinoma and Acinic Cell Adenocarcinoma of Salivary Gland Origin. Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology, 118, 320-329. http://dx.doi.org/10.1016/j.oooo.2014.05.004
Ng, L., et al. (2015) Osteopontin Overexpression Induced Tumor Progression and Chemoresistance to Oxaliplatin through Induction of Stem-Like Properties in Human Colorectal Cancer. Stem Cells International, 2015, Article ID: 247892. http://dx.doi.org/10.1155/2015/247892
Sun, J., et al. (2010) Involvement of Osteopontin Upregulation on Mesangial Cells Growth and Collagen Synthesis Induced by Intermittent High Glucose. Journal of Cellular Biochemistry, 109, 1210-1221. http://dx.doi.org/10.1002/jcb.22503
Oh, K., Seo, M.W., Kim, Y.W. and Lee, D.-S. (2015) Osteopontin Potentiates Pulmonary Inflammation and Fibrosis by Modulating IL-17/IFN-γ-Secreting T-Cell Ratios in Bleomycin-Treated Mice. Immune Network, 15, 142-149. http://dx.doi.org/10.4110/in.2015.15.3.142
Coppola, D., et al. (2004) Correlation of Osteopontin Protein Expression and Pathological Stage across a Wide Variety of Tumor Histologies. Clinical Cancer Research, 10, 184-190. http://dx.doi.org/10.1158/1078-0432.CCR-1405-2
Fisher, L.W., Jain, A., Tayback, M. and Fedarko, N.S. (2004) Small Integrin Binding Ligand N-Linked Glycoprotein Gene Family Expression in Different Cancers. Clinical Cancer Research, 10, 8501-8511. http://dx.doi.org/10.1158/1078-0432.CCR-04-1072
Han, J.C., et al. (2015) Serum Osteopontin Levels Correlate with Clinical and Pathological Features in Non-Small Cell Lung Cancer. Analytical and Quantitative Cytology and Histology, 37, 295-301.
Cho, W.Y., et al. (2015) Suppression of Tumor Growth in lung Cancer Xenograft Model Mice by Poly(Sorbitol-co-PEI)-Mediated Delivery of Osteopontin siRNA. European Journal of Pharmaceutics and Biopharmaceutics, 94, 450-462. http://dx.doi.org/10.1016/j.ejpb.2015.06.017
Lee, S.H., et al. (2015) Ablation of Osteopontin Suppresses N-Methyl-N-Nitrosourea and Helicobacter Pylori-Induced Gastric Cancer Development in Mice. Carcinogenesis, 36, 1550-1560.
Anborgh, P.H., et al. (2015) Role of Plasma Osteopontin as a Biomarker in Locally Advanced Breast Cancer. American Journal of Translational Research, 7, 723-732.
You, Y., et al. (2015) Higher Matrix Stiffness Upregulates Osteopontin Expression in Hepatocellular Carcinoma Cells Mediated by Integrin Beta1/Gsk3Beta/Beta-Catenin Signaling Pathway. PLoS ONE, 10, e0134243. http://dx.doi.org/10.1371/journal.pone.0134243
Chakraborty, G., Jain, S., and Kundu, G.C. (2008) Osteopontin Promotes Vascular Endothelial Growth Factor-Dependent Breast Tumor Growth and Angiogenesis via Autocrine and Paracrine Mechanisms. Cancer Research, 68, 152-161. http://dx.doi.org/10.1158/0008-5472.CAN-07-2126
Xu, J., et al. (2015) Osteopontin Induces Vascular Endothelial Growth Factor Expression in Articular Cartilage through PI3K/AKT and ERK1/2 Signaling. Molecular Medicine Reports, 12, 4708-4712. http://dx.doi.org/10.3892/mmr.2015.3975
Bandopadhyay, M., et al. (2014) Osteopontin as a Therapeutic Target for Cancer. Expert Opinion on Therapeutic Targets, 18, 883-895. http://dx.doi.org/10.1517/14728222.2014.925447
Theocharis, A.D., Skandalis, S.S., Gialelia, C. and Karamanos, N.K. (2016) Extracellular Matrix Structure. Advanced Drug Delivery Reviews, 97, 4-27. http://dx.doi.org/10.1016/j.addr.2015.11.001
Tzedakis, G., et al. (2015) The Importance of Neighborhood Scheme Selection in Agent-Based Tumor Growth Modeling. Cancer Informatics, 14, 67-81.
Li, Y., et al. (2015) Osteopontin Promotes Invasion, Migration and Epithelial-Mesenchymal Transition of Human Endometrial Carcinoma Cell HEC-1A through AKT and ERK1/2 Signaling. Cellular Physiology and Biochemistry, 37, 1503-1512. http://dx.doi.org/10.1159/000438518
Cho, A., Howell, V.M., and Colvin, E.K. (2015) The Extracellular Matrix in Epithelial Ovarian Cancer—A Piece of a Puzzle. Frontiers in Oncology, 5, 245. http://dx.doi.org/10.3389/fonc.2015.00245
Zhang, Y.Y., Chen, B., and Ding, Y.Q. (2012) Metastasis-Associated Factors Facilitating the Progression of Colorectal Cancer. Asian Pacific Journal of Cancer Prevention, 13, 2437-2344. http://dx.doi.org/10.7314/APJCP.2012.13.6.2437
Guan, X. (2015) Cancer Metastases: Challenges and Opportunities. Acta Pharmaceutica Sinica B, 5, 402-418. http://dx.doi.org/10.1016/j.apsb.2015.07.005
Shevde, L.A. and Samant, R.S. (2014) Role of Osteopontin in the Pathophysiology of Cancer. Matrix Biology, 37, 131-141. http://dx.doi.org/10.1016/j.matbio.2014.03.001
Kaleagasioglu, F. and Berger, M.R. (2014) SIBLINGs and SPARC Families: Their Emerging Roles in Pancreatic Cancer. World Journal of Gastroenterology, 20, 14747-14759. http://dx.doi.org/10.3748/wjg.v20.i40.14747
Nagoshi, S. (2014) Osteopontin: Versatile Modulator of Liver Diseases. Hepatology Research, 44, 22-30. http://dx.doi.org/10.1111/hepr.12166
Behera, R., et al. (2010) Activation of JAK2/STAT3 Signaling by Osteopontin Promotes Tumor Growth in Human Breast Cancer Cells. Carcinogenesis, 31, 192-200. http://dx.doi.org/10.1093/carcin/bgp289
Wang, L., Wang, H. and Zhang, S. (2010) Clinical Significance of the Upregulated Osteopontin mRNA Expression in Human Colorectal Cancer. Journal of Gastrointestinal Surgery, 14, 74-81. http://dx.doi.org/10.1007/s11605-009-1035-z
Martinez, C., Churchman, M., Freeman, T. and Ilyas, M. (2010) Osteopontin Provides Early Proliferative Drive and May Be Dependent upon Aberrant C-Myc Signalling in Murine Intestinal Tumours. Experimental and Molecular Pathology, 88, 272-277. http://dx.doi.org/10.1016/j.yexmp.2009.12.008
Imano, M., et al. (2010) Increased Osteopontin-Positive Macrophage Expression in Colorectal Cancer Stroma with Synchronous Liver Metastasis. World Journal of Surgery, 34, 1930-1936. http://dx.doi.org/10.1007/s00268-010-0582-5
Huang, J., Pan, C., Hu, H., Zheng, S. and Ding, L. (2012) Osteopontin-Enhanced Hepatic Metastasis of Colorectal Cancer Cells. PLoS ONE, 7, e47901. http://dx.doi.org/10.1371/journal.pone.0047901
Fan, Y., et al. (2013) The Polymorphisms of Osteopontin Gene and Plasma Osteopontin Protein Levels with Susceptibility to Colorectal Carcinoma. DNA and Cell Biology, 32, 594-600. http://dx.doi.org/10.1089/dna.2013.2090
Ng, L., et al. (2015) Post-Operative Plasma Osteopontin Predicts Distant Metastasis in Human Colorectal Cancer. PLoS ONE, 10, e0126219. http://dx.doi.org/10.1371/journal.pone.0126219
Kashihara, H., et al. (2014) CD133 Expression Is Correlated with Poor Prognosis in Colorectal Cancer. Hepato-Gastroenterology, 61, 1563-1567.
Todaro, M., et al. (2014) CD44v6 Is a Marker of Constitutive and Reprogrammed Cancer Stem Cells Driving Colon Cancer Metastasis. Cell Stem Cell, 14, 342-356. http://dx.doi.org/10.1016/j.stem.2014.01.009
Sung, J.J., et al. (2008) Asia Pacific Consensus Recommendations for Colorectal Cancer Screening. Gut, 57, 1166-1176. http://dx.doi.org/10.1136/gut.2007.146316
Zhao, M., Liang, F., Zhang, B., Yan, W. and Zhang, J. (2015) The Impact of Osteopontin on Prognosis and Clinicopathology of Colorectal Cancer Patients: A Systematic Meta-Analysis. Scientific Reports, 5, Article Number: 12713. http://dx.doi.org/10.1038/srep12713
Michl, M., et al. (2015) Expression of Cancer Stem Cell Markers in Metastatic Colorectal Cancer Correlates with Liver Metastasis, but Not with Metastasis to the Central Nervous System. Pathology Research and Practice, 211, 601-609. http://dx.doi.org/10.1016/j.prp.2015.05.006
Wu, X.L., et al. (2014) Osteopontin Knockdown Suppresses the Growth and Angiogenesis of Colon Cancer Cells. World Journal of Gastroenterology, 20, 10440-10448. http://dx.doi.org/10.3748/wjg.v20.i30.10440
Ding, L., Hu, H.G., and Zheng, S. (2011) Effects of Osteopontin on Gap Junctional Intercellular Communication in Colon Cancer Cell Lines. National Medical Journal of China, 91, 2578-2581.
Shao, J., Kay Washington, M., Saxena, R. and Sheng, H. (2007) Heterozygous Disruption of the PTEN Promotes Intestinal Neoplasia in APC min/+ Mouse: Roles of Osteopontin. Carcinogenesis, 28, 2476-2483. http://dx.doi.org/10.1093/carcin/bgm186