Osteopontina, una proteína involucrada en la progresión tumoral, y su participación en el desarrollo del carcinoma colorrectal.

Osteopontin, a protein involved in tumor progression, and its participation in the development of colorectal carcinoma.

Contenido principal del artículo

Daniel Becerra
Ines Benedetti

Resumen

Introducción: La osteopontina es una proteína de la matriz extracelular que se ha encontrado sobre-expresada en varios tipos de tumores malignos, incluido el carcinoma colorrectal. Objetivo: Describir la evidencia científica disponible sobre la participación de osteopontina en la patogénesis del carcinoma colorrectal, y del posible uso de su expresión a nivel tisular, como biomarcador de esta neoplasia. Materiales y métodos: Se realizó una búsqueda bibliográfica de artículos en idioma inglés desde enero de 2012 hasta enero de 2018, en la base de datos Pubmed. Resultados: La revisión de la literatura permite decir que osteopontina está involucrada en casi todos los pasos de la progresión tumoral, y su sobre-expresión en el carcinoma colorrectal está asociada significativamente con altos grados tumorales, metástasis ganglionares y metástasis a distancia. Conclusión: Osteopontina podría servir como un biomarcador de pronóstico para el carcinoma colorrectal y tendría un papel importante en la predicción del resultado de la terapia clínica para esta neoplasia, se necesitan estudios más robustos que validen su uso en este sentido

Palabras clave:

Descargas

Los datos de descargas todavía no están disponibles.

Detalles del artículo

Biografía del autor/a (VER)

Daniel Becerra, Universidad de Cartagena

MD, Semillero de investigación NEO, Grupo Histopatología, Facultad de Medicina, Universidad de Cartagena, Colombia.

Ines Benedetti, Universidad de Cartagena

MD, Patóloga, PhD, Grupo Histopatología. Profesor titular, Facultad de Medicina, Universidad
de Cartagena, Colombia

Referencias (VER)

Ferlay J, Soerjomataram I, Dikshit R, Eser S, Mathers C, Rebelo M, et al. Cancer incidence and mortality worldwide: Sources, methods and major patterns in GLOBOCAN 2012. Int J Cancer. 2015; 136(5): E359-86. https://doi.org/10.1002/ijc.29210

WHO. Globocan 2012 - Home [Internet]. Globocan. 2012 [cited 2018 Jan 10]. Available from: http://globocan.iarc.fr/Default.aspx

McKee MD, Pedraza CE, Kaartinen MT. Osteopontin and wound healing in bone. In: Cells Tissues Organs. 2011. p. 313-9. https://doi.org/10.1159/000324244

Castello LM, Raineri D, Salmi L, Clemente N, Vaschetto R, Quaglia M, et al. Osteopontin at the Crossroads of Inflammation and Tumor Progression. Vol. 2017, Mediators of Inflammation. 2017. https://doi.org/10.1155/2017/4049098

Vaschetto R, Nicola S, Olivieri C, Boggio E, Piccolella F, Mesturini R, et al. Serum levels of osteopontin are increased in SIRS and sepsis. Intensive Care Med. 2008;34(12):2176-84. https://doi.org/10.1007/s00134-008-1268-4

Clemente N, Raineri D, Cappellano G, Boggio E, Favero F, Soluri MF, et al. Osteopontin Bridging Innate and Adaptive Immunity in Autoimmune Diseases. Vol. 2016, Journal of Immunology Research. 2016. https://doi.org/10.1155/2016/7675437

Anborgh PH, Mutrie JC, Tuck AB, Chambers AF. Role of the metastasis-promoting protein osteopontin in the tumour microenvironment. J Cell Mol Med. 2010;14(8):2037-44. https://doi.org/10.1111/j.1582-4934.2010.01115.x

Zhang J, Takahashi K, Takahashi F, Shimizu K, Ohshita F, Kameda Y, et al. Differential osteopontin expression in lung cancer. Cancer Lett. 2001; 171(2): 215-22. https://doi.org/10.1016/S0304-3835(01)00607-3

Bramwell VHC, Tuck AB, Chapman J-AW, Anborgh PH, Postenka CO, Al-Katib W, et al. Assessment of osteopontin in early breast cancer: correlative study in a randomised clinical trial. Breast Cancer Res. 2014;16(1):R8. https://doi.org/10.1186/bcr3600

Kim JY, Bae B-N, Kim KS, Shin E, Park K. Osteopontin, CD44, and NFkappaB expression in gastric adenocarcinoma. Cancer Res Treat. 2009;41(1):29-35. https://doi.org/10.4143/crt.2009.41.1.29

Shang S, Plymoth A, Ge S, Feng Z, Rosen HR, Sangrajrang S, et al. Identification of osteopontin as a novel marker for early hepatocellular carcinoma. Hepatology. 2012;55(2):483-90. https://doi.org/10.1002/hep.24703

Likui W, Hong W, Shuwen Z. Clinical Significance of the Upregulated Osteopontin mRNA Expression in Human Colorectal Cancer. J Gastrointest Surg. 2010; 14:74. https://doi.org/10.1007/s11605-009-1035-z

Brenner H, Kloor M, Pox CP. Colorectal cancer. In: The Lancet. 2014. p. 1490-502. https://doi.org/10.1016/S0140-6736(13)61649-9

Haggar FA, Boushey RP. Colorectal cancer epidemiology: incidence, mortality, survival, and risk factors. Clin Colon Rectal Surg. 2009; 22(4): 191-7. https://doi.org/10.1055/s-0029-1242458

Siegel R, Miller KD, Ahmedin J. Cáncer Statistics. Ca Cáncer J. 2017; 67(1): 7-30. https://doi.org/10.3322/caac.21387

Fondo Colombiano de Enfermedades de Alto Costo Cuenta de Alto Costo [CAC]. Situación del cáncer en la población adulta atendida en el sgsss de Colombia 2016. 2017.

J C-C, Ministerio de Salud y Protección Social, Sistema General de Seguridad Social en Salud - Colombia, Instituto Nacional de Cancerología, Ministerio de Salud y Protección Social. Guía de práctica clínica (GPC) para la detección temprana, diagnóstico, tratamiento, seguimiento y rehabilitación de pacientes con diagnóstico de cáncer de colon y recto. Instituto Nacional de Cancerología INC - ESE, COLCIENCIAS, Ministerio de Salud y Protección Social. 2013. 48 p.

Xue L, Williamson A, Gaines S, Andolfi C, Paul-Olson T, Neerukonda A, et al. An Update on Colorectal Cancer. Curr Probl Surg. 2018 Mar; 55(3): 76-116. https://doi.org/10.1067/j.cpsurg.2018.02.003

Bienz M, Clevers H. Linking Colorectal Cancer to Wnt Signaling. Cell. 2000 Oct; 103(2): 311-20. https://doi.org/10.1016/S0092-8674(00)00122-7

Kodach LL, Wiercinska E, de Miranda NFCC, Bleuming SA, Musler AR, Peppelenbosch MP, et al. The Bone Morphogenetic Protein Pathway Is Inactivated in the Majority of Sporadic Colorectal Cancers. Gastroenterology. 2008 May; 134(5): 1332-1341.e3. https://doi.org/10.1053/j.gastro.2008.02.059

Mi Z, Bhattacharya SD, Kim VM, Guo H, Talbotq LJ, Kuo PC. Osteopontin promotes CCL5-mesenchymal stromal cell-mediated breast cancer metastasis. Carcinogenesis. 2011; https://doi.org/10.1093/carcin/bgr009

Inés Benedetti, Niradiz Reyes. Transición epitelial-mesenquimal en la progresión del adenocarcinoma prostático. Iatreia. 2015; 28(4): 420-33. https://doi.org/10.17533/udea.iatreia.v28n4a07

Findlay VJ, Wang C, Watson DK, Camp ER. Epithelial-to mesenchymal transition and the cancer stem cell phenotype: insights from cancer biology with therapeutic implications for colorectal cancer. Cancer Gene Ther. 2014 May 2;21 (5): 181-7. https://doi.org/10.1038/cgt.2014.15

He X, Chen Z, Jia M, Zhao X. Downregulated E-Cadherin Expression Indicates Worse Prognosis in Asian Patients with Colorectal Cancer: Evidence from Meta-Analysis. Aziz SA, editor. PLoS One. 2013 Jul 29; 8(7): e70858. https://doi.org/10.1371/journal.pone.0070858

Sears CL, Garrett WS. Microbes, Microbiota, and Colon Cancer. Cell Host Microbe. 2014 Mar; 15(3): 317-28. https://doi.org/10.1016/j.chom.2014.02.007

Tjalsma H, Boleij A, Marchesi JR, Dutilh BE. A bacterial driver-passenger model for colorectal cancer: Beyond the usual suspects. Nat Rev Microbiol. 2012. https://doi.org/10.1038/nrmicro2819

Schwabe RF, Jobin C. The microbiome and cancer. Nat Rev Cancer. 2013 Nov 17; 13(11): 800-12. https://doi.org/10.1038/nrc3610

Rubinstein MR, Wang X, Liu W, Hao Y, Cai G, Han YW. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin. Cell Host Microbe. 2013; https://doi.org/10.1016/j.chom.2013.07.012

Kostic AD, Chun E, Robertson L, Glickman JN, Gallini CA, Michaud M, et al. Fusobacterium nucleatum Potentiates Intestinal Tumorigenesis and Modulates the Tumor-Immune Microenvironment. Cell Host Microbe. 2013 Aug; 14(2): 207-15. https://doi.org/10.1016/j.chom.2013.07.007

Boleij A, Van Gelder MMHJ, Swinkels DW, Tjalsma H. Clinical importance of streptococcus gallolyticus infection among colorectal cancer patients: Systematic review and meta-analysis. Clin Infect Dis. 2011. https://doi.org/10.1093/cid/cir609

Shiryaev SA, Remacle AG, Chernov A V., Golubkov VS, Motamedchaboki K, Muranaka N, et al. Substrate cleavage profiling suggests a distinct function of bacteroides fragilis metalloproteinases (fragilysin and metalloproteinase ii) at the microbiome-inflammation-cancer interface. J Biol Chem. 2013. https://doi.org/10.1074/jbc.M113.516153

Yang Y, Wang X, Huycke T, Moore DR, Lightfoot SA, Huycke MM. Colon Macrophages Polarized by Commensal Bacteria Cause Colitis and Cancer through the Bystander Effect. Transl Oncol. 2013 Oct; 6(5): 596-IN8. https://doi.org/10.1593/tlo.13412

Denhardt DT, Noda M. Osteopontin expression and function: role in bone remodeling. Vols. 30-31, Journal of cellular biochemistry. Supplement. 1998. p. 92-102. https://doi.org/10.1002/(SICI)1097-4644(1998)72:30/31+<92::AID-JCB13>3.0.CO;2-A

Denhardt DT, Guo X. Osteopontin: a protein with diverse functions. FASEB J. 1993; 7: 1475-82. https://doi.org/10.1096/fasebj.7.15.8262332

Huang R, Quan Y, Chen J, Wang T, Xu M, Ye M, et al. Osteopontin Promotes Cell Migration and Invasion, and Inhibits Apoptosis and Autophagy in Colorectal Cancer by activating the p38 MAPK Signaling Pathway. Cell Physiol Biochem. 2017; 200032:1851-64. https://doi.org/10.1159/000471933

Thorsen SB, Lundberg M, Villablanca A, Christensen SLT, Belling KC, Nielsen BS, et al. Detection of serological biomarkers by proximity extension assay for detection of colorectal neoplasias in symptomatic individuals. J Transl Med. 2013;11(1). https://doi.org/10.1186/1479-5876-11-253

Kahles F, Findeisen HM, Bruemmer D. Osteopontin: A novel regulator at the cross roads of inflammation, obesity and diabetes. Vol. 3, Molecular Metabolism. 2014. p. 384-93. https://doi.org/10.1016/j.molmet.2014.03.004

Lund SA, Wilson CL, Raines EW, Tang J, Giachelli CM, Scatena M. Osteopontin mediates macrophage chemotaxis via ??4 and ??9 integrins and survival via the ??4 integrin. J Cell Biochem. 2013; 114(5): 1194-202. https://doi.org/10.1002/jcb.24462

O'Regan AW, Hayden JM, Berman JS. Osteopontin augments CD3-mediated interferon-gamma and CD40 ligand expression by T cells, which results in IL-12 production from peripheral blood mononuclear cells. Vol. 68, J Leukoc Biol. 2000. p. 495-502.

Liaw L, Birk DE, Ballas CB, Whitsitt JS, Davidson JM, Hogan BL, et al. Altered wound healing in mice lacking a functional osteopontin gene (spp1). J Clin Invest. 2007; 101(7): 1468-78. https://doi.org/10.1172/JCI2131

Mori R, Shaw TJ, Martin P. Molecular mechanisms linking wound inflammation and fibrosis: knockdown of osteopontin leads to rapid repair and reduced scarring. J Exp Med. 2008 Jan 21; 205(1): 43-51. https://doi.org/10.1084/jem.20071412

Higashiyama M, Ito T, Tanaka E, Shimada Y. Prognostic significance of osteopontin expression in human gastric carcinoma. Ann Surg Oncol. 2007; 14(12): 3419-27. https://doi.org/10.1245/s10434-007-9564-8

Weber GF, Lett GS, Haubein NC. Osteopontin is a marker for cancer aggressiveness and patient survival. Br J Cancer. 2010; 103(6): 861-9. https://doi.org/10.1038/sj.bjc.6605834

Zhang H, Li L, Dong Q, Wang Y, Feng Q, Ou X, et al. Activation of PKA/ CREB Signaling is Involved in BMP9-Induced Osteogenic Differentiation of Mesenchymal Stem Cells. Cell Physiol Biochem. 2015; 37(2): 548-62. https://doi.org/10.1159/000430376

Rangaswami H, Bulbule A, Kundu GC. Osteopontin: Role in cell signaling and cancer progression. Vol. 16, Trends in Cell Biology. 2006. p. 79-87. https://doi.org/10.1016/j.tcb.2005.12.005

Hirama M, Takahashi F, Takahashi K, Akutagawa S, Shimizu K, Soma S, et al. Osteopontin overproduced by tumor cells acts as a potent angiogenic factor contributing to tumor growth. Cancer Lett. 2003; 198(1): 107-17. https://doi.org/10.1016/S0304-3835(03)00286-6

Weber GF. Molecular mechanisms of metastasis. Vol. 270, Cancer Letters. 2008. p. 181-90. https://doi.org/10.1016/j.canlet.2008.04.030

Atai NA, Bansal M, Lo C, Bosman J, Tigchelaar W, Bosch KS, et al. Osteopontin is up-regulated and associated with neutrophil and macrophage infiltration in glioblastoma. Immunology. 2011. https://doi.org/10.1111/j.1365-2567.2010.03335.x

Dai J, Li B, Shi J, Peng L, Zhang D, Qian W, et al. A humanized anti-osteopontin antibody inhibits breast cancer growth and metastasis in vivo. Cancer Immunol Immunother. 2010 Mar 19; 59(3): 355-66. https://doi.org/10.1007/s00262-009-0754-z

Weber GF, Lett GS, Haubein NC. Categorical meta-analysis of osteopontin as a clinical cancer marker. Oncol Rep. 2011. https://doi.org/10.3892/or.2010.1106

Castellano G, Malaponte G, Mazzarino MC, Figini M, Marchese F, Gangemi P, et al. Activation of the osteopontin/matrix metalloproteinase-9 pathway correlates with prostate cancer progression. Clin Cancer Res. 2008. https://doi.org/10.1158/1078-0432.CCR-08-0870

Thoms JW, Dal Pra A, Anborgh PH, Christensen E, Fleshner N, Menard C, et al. Plasma osteopontin as a biomarker of prostate cancer aggression: Relationship to risk category and treatment response. Br J Cancer. 2012; 107(5): 840-6. https://doi.org/10.1038/bjc.2012.345

Trotter TN, Yang Y. Matricellular proteins as regulators of cancer metastasis to bone. Matrix Biol. 2016 May; 52-54(2): 301-14. https://doi.org/10.1016/j.matbio.2016.01.006

Bramwell VHC, Doig GS, Tuck AB, Wilson SM, Tonkin KS, Tomiak A, et al. Serial plasma osteopontin levels have prognostic value in metastatic breast cancer. Clin Cancer Res. 2006. https://doi.org/10.1158/1078-0432.CCR-05-2354

Li NY, Weber CE, Mi Z, Wai PY, Cuevas BD, Kuo PC. Osteopontin up-regulatescritical epithelial-mesenchymal transition transcription factors to induce an aggressive breast cancer phenotype. In: Journal of the American College of Surgeons. 2013. https://doi.org/10.1016/j.jamcollsurg.2013.02.025

Wang XM, Li J, Yan MX, Liu L, Jia DS, Geng Q, et al. Integrative Analyses Identify Osteopontin, LAMB3 and ITGB1 as Critical Pro-Metastatic Genes for Lung Cancer. PLoS One. 2013. https://doi.org/10.1371/journal.pone.0055714

Mole DJ, O'Neill C, Hamilton P, Olabi B, Robinson V, Williams L, et al. Expression of osteopontin coregulators in primary colorectal cancer and associated liver metastases. Br J Cancer. 2011. https://doi.org/10.1038/bjc.2011.33

Rud AK, Boye K, Oijordsbakken M, Lund-Iversen M, Halvorsen AR, Solberg SK, et al. Osteopontin is a prognostic biomarker in non-small cell lung cancer. BMC Cancer. 2013. https://doi.org/10.1186/1471-2407-13-540

Li Y, Li L, Wang JT, Kan X, Lu JG. Elevated content of osteopontin in plasma and tumor tissues of patients with laryngeal and hypopharyngeal carcinoma associated with metastasis and prognosis. Med Oncol. 2012. https://doi.org/10.1007/s12032-011-0012-z

Chang P-L, Harkins L, Hsieh Y-H, Hicks P, Sappayatosok K, Yodsanga S, et al. Osteopontin expression in normal skin and non-melanoma skin tumors. J Histochem Cytochem. 2008. https://doi.org/10.1369/jhc.7A7325.2007

Kale S, Raja R, Thorat D, Soundararajan G, Patil T V., Kundu GC. Osteopontin signaling upregulates cyclooxygenase-2 expression in tumor-associated macrophages leading to enhanced angiogenesis and melanoma growth via α9β1 integrin. Oncogene. 2014. https://doi.org/10.1038/onc.2013.184

Wei R, Pik J, Wong C, Kwok HF. Osteopontin -- a promising biomarker for cancer therapy. 2017;8. https://doi.org/10.7150/jca.20480

Subramani V, Thiyagarajan M, Malathi N, Rajan ST. OPN - Revisited. Journal of Clinical and Diagnostic Research. 2015. https://doi.org/10.7860/JCDR/2015/12872.6111

Ng L, Wan T, Chow A, Iyer D, Man J, Chen G, et al. Osteopontin Overexpression Induced Tumor Progression and Chemoresistance to Oxaliplatin through Induction of Stem-Like Properties in Human Colorectal Cancer. Stem Cells Int. 2015. https://doi.org/10.1155/2015/247892

Eschrich S, Yang I, Bloom G, Kwong KY, Boulware D, Cantor A, et al. Molecular staging for survival prediction of colorectal cancer patients. J Clin Oncol. 2005. https://doi.org/10.1200/JCO.2005.00.695

Leslie A, Carey FA, Pratt NR, Steele RJC. The colorectal adenoma-carcinoma sequence. Vol. 89, British Journal of Surgery. 2002. p. 845-60. https://doi.org/10.1046/j.1365-2168.2002.02120.x

Paoni NF, Feldman MW, Gutierrez LS, Ploplis V a, Castellino FJ. Transcriptional profiling of the transition from normal intestinal epithelia to adenomas and carcinomas in the APCMin/ + mouse. Physiol Genomics. 2003; 15(3): 228-35. https://doi.org/10.1152/physiolgenomics.00078.2003

Chambers AF, Behrend EI, Wilson SM, Denhardt DT. Induction of expression of osteopontin (OPN; secreted phosphoprotein) in metastatic, ras-transformed NIH 3T3 cells. Anticancer Res. 1992; 12(1): 43-7.

Li J, Yang GZ, Zhu ZM, Zhou ZY, Li L. Osteopontin is overexpressed in colorectal carcinoma and is correlated with P53 by immunohistochemistry. Exp Ther Med. 2012;3(4):621-4. https://doi.org/10.3892/etm.2012.465

Valcz G, Sipos F, Krenács T, Molnár J, Patai Á V., Leiszter K, et al. Elevated osteopontin expression and proliferative/apoptotic ratio in the colorectal adenoma-dysplasia-carcinoma sequence. Pathol Oncol Res. 2010; 16(4): 541-5. https://doi.org/10.1007/s12253-010-9260-z

Takami Y, Russell MB, Gao C, Mi Z, Guo H, Mantyh CR, et al. Sp1 regulates osteopontin expression in SW480 human colon adenocarcinoma cells. Surgery. 2007; 142(2): 163-9. https://doi.org/10.1016/j.surg.2007.02.015

Martinez C, Churchman M, Freeman T, Ilyas M. Osteopontin provides early proliferative drive and may be dependent upon aberrant c-myc signalling in murine intestinal tumours. Exp Mol Pathol. 2010; 88(2): 272-7. https://doi.org/10.1016/j.yexmp.2009.12.008

Liu Y-N, Kang B-B, Chen JH. Transcriptional regulation of human osteopontin promoter by C/EBPalpha and AML-1 in metastatic cancer cells. Oncogene. 2004;23(1):278-88. https://doi.org/10.1038/sj.onc.1207022

Zagani R, Hamzaoui N, Cacheux W, de Reyniès A, Terris B, Chaussade S, et al. Cyclooxygenase-2 Inhibitors Down-regulate Osteopontin and Nr4a2-New Therapeutic Targets for Colorectal Cancers. Gastroenterology. 2009;137(4). https://doi.org/10.1053/j.gastro.2009.06.039

El-Tanani M, Platt-Higgins A, Rudland PS, Campbell FC. Ets gene PEA3 cooperates with ??-catenin-Lef-1 and c-Jun in regulation of osteopontin transcription. J Biol Chem. 2004; 279(20): 20794-806. https://doi.org/10.1074/jbc.M311131200

Rohde F, Rimkus C, Friederichs J, Rosenberg R, Marthen C, Doll D, et al. Expression of osteopontin, a target gene of de-regulated Wnt signaling, predicts survival in colon cancer. Int J Cancer. 2007; 121(8): 1717-23. https://doi.org/10.1002/ijc.22868

El-Tanani MK, Jin D, Campbell FC, Johnston PG. Interferon-induced transmembrane 3 binds osteopontin in vitro: Expressed in vivo IFITM3 reduced OPN expression. Oncogene. 2010. https://doi.org/10.1038/onc.2009.379

Wild N, Andres H, Rollinger W, Krause F, Dilba P, Tacke M, et al. A combination of serum markers for the early detection of colorectal cancer. Clin Cancer Res. 2010; 16(24): 6111-21. https://doi.org/10.1158/1078-0432.CCR-10-0119

Ng L, Wan TMH, Lam CSC, Chow AKM, Wong SKM, Man JHW, et al. Post-operative plasma osteopontin predicts distant metastasis in human colorectal cancer. PLoS One. 2015; 10(5). https://doi.org/10.1371/journal.pone.0126219

Zhao M, Liang F, Zhang B, Yan W, Zhang J. The impact of osteopontin on prognosis and clinicopathology of colorectal cancer patients: A systematic meta-analysis. Sci Rep. 2015; 5. https://doi.org/10.1038/srep12713

Likui W, Hong W, Shuwen Z, Yuangang Y, Yan W. The Potential of Osteopontin as a Therapeutic Target for Human Colorectal Cancer. J Gastrointest Surg. 2011 Apr 12;15(4):652-9. https://doi.org/10.1007/s11605-011-1445-6

Boudjadi S, Bernatchez G, Beaulieu JF, Carrier JC. Control of the human osteopontin promoter by ERRα in colorectal cancer. Am J Pathol. 2013; 183(1): 266-76. https://doi.org/10.1016/j.ajpath.2013.03.021

Youssef NS, Osman WM. Relationship between osteopontin and β-catenin immunohistochemical expression and prognostic parameters of colorectal carcinoma. Int J Clin Exp Pathol. 2015; 8(2): 1503-14.

Citado por