Osteopontin is a multi-faceted pro-tumorigenic driver for central nervous system lymphoma

Oncotarget

Volumn 7, Issue 22, 2016, Pages 32156-32171

  Yushi, Qiu ^a   Li, Zhimin ^a   Von Roemeling, Christina A ^b   Doeppler, Heike ^a   Marlow, Laura A ^a   Kim, Betty Y S ^c   Radisky, Derek C ^a   Storz, Peter ^a   Copland, John A ^a   Tun, Han W ^a,c  

^a Department of Cancer Biology ^*  (United States)

^b MAYO CLINIC   (United States)

^c MAYO CLINIC   (United States)

Author keywords

CNS lymphoma; Invasion; NF B signaling; Osteopontin (OPN); Proliferation

Indexed keywords

CELL PROTEIN; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEUTROPHIL COLLAGENASE; OSTEOPONTIN; PROTEIN A20; PROTEIN ABIN1; PROTEIN TNFAIP3; PROTEIN TNIP1; REGULATOR PROTEIN; SECRETORY PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; MMP8 PROTEIN, HUMAN; SPP1 PROTEIN, HUMAN; TNFAIP3 PROTEIN, HUMAN; TNIP1 PROTEIN, HUMAN; TUMOR NECROSIS FACTOR ALPHA INDUCED PROTEIN 3;

ARTICLE; BRAIN TUMOR; CARCINOGENESIS; DOWN REGULATION; HUMAN; HUMAN CELL; HUMAN TISSUE; METASTASIS; MOLECULAR MECHANICS; PRIMARY CENTRAL NERVOUS SYSTEM LYMPHOMA; PROTEIN FUNCTION; PROTEIN INDUCTION; TRANSCRIPTION REGULATION; TUMOR INVASION; ANIMAL; AUTOCRINE EFFECT; B CELL LYMPHOMA; CELL MOTION; CELL PROLIFERATION; CENTRAL NERVOUS SYSTEM TUMOR; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETIC TRANSFECTION; GENETICS; METABOLISM; NUDE MOUSE; PATHOLOGY; RNA INTERFERENCE; SIGNAL TRANSDUCTION; TIME FACTOR; TUMOR CELL LINE; TUMOR VOLUME;

ANIMALS; AUTOCRINE COMMUNICATION; CELL LINE, TUMOR; CELL MOVEMENT; CELL PROLIFERATION; CENTRAL NERVOUS SYSTEM NEOPLASMS; DNA-BINDING PROTEINS; GENE EXPRESSION REGULATION, NEOPLASTIC; HUMANS; LYMPHOMA, B-CELL; MATRIX METALLOPROTEINASE 8; MICE, NUDE; NEOPLASM INVASIVENESS; NEOPLASM METASTASIS; NF-KAPPA B; OSTEOPONTIN; RNA INTERFERENCE; SIGNAL TRANSDUCTION; TIME FACTORS; TRANSCRIPTION, GENETIC; TRANSFECTION; TUMOR BURDEN; TUMOR NECROSIS FACTOR ALPHA-INDUCED PROTEIN 3;

EID: 84973524645     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.8537     Document Type: Article

References (49)

1. Campo E, Swerdlow SH, Harris NL, Pileri S, Stein H, Jaffe ES. The 2008 WHO classification of lymphoid neoplasms and beyond: evolving concepts and practical applications. Blood. 2011; 117:5019-5032.
2. Ferreri AJ. How I treat primary CNS lymphoma. Blood. 2011; 118:510-522.
3. Rubenstein JL, Gupta NK, Mannis GN, Lamarre AK, Treseler P. How I treat CNS lymphomas. Blood. 2013; 122:2318-2330.
4. Villano JL, Koshy M, Shaikh H, Dolecek TA, McCarthy BJ. Age, gender, and racial differences in incidence and survival in primary CNS lymphoma. Br J Cancer. 2011; 105:1414-1418.
5. Anthony IC, Crawford DH, Bell JE. B lymphocytes in the normal brain: contrasts with HIV-associated lymphoid infiltrates and lymphomas. Brain. 2003; 126:1058-1067.
6. Lai R, Rosenblum MK, DeAngelis LM. Primary CNS lymphoma: a whole-brain disease? Neurology. 2002; 59:1557-1562.
7. Jiang L, Marlow LA, Cooper SJ, Roemeling CV, Menke DM, Copland JA, Tun HW. Selective central nervous system tropism of primary central nervous system lymphoma. Int J Clin Exp Pathol. 2010; 3:763-767.
8. Ponzoni M, Issa S, Batchelor TT, Rubenstein JL. Beyond high-dose methotrexate and brain radiotherapy: novel targets and agents for primary CNS lymphoma. Ann Oncol. 2014; 25:316-322.
9. Tun HW, Personett D, Baskerville KA, Menke DM, Jaeckle KA, Kreinest P, Edenfield B, Zubair AC, O'Neill BP, Lai WR, Park PJ, McKinney M. Pathway analysis of primary central nervous system lymphoma. Blood. 2008; 111:3200-3210.
10. Rubenstein JL, Shen A, Batchelor TT, Kadoch C, Treseler P, Shuman MA. Differential gene expression in central nervous system lymphoma. Blood. 2009; 113:266-267; author reply 267-268.
11. Nagel S, Hirschmann P, Dirnhofer S, Gunthert U, Tzankov A. Coexpression of CD44 variant isoforms and receptor for hyaluronic acid-mediated motility (RHAMM, CD168) is an International Prognostic Index and C-MYC gene status-independent predictor of poor outcome in diffuse large B-cell lymphomas. Exp Hematol. 2010; 38:38-45.
12. Anborgh PH, Mutrie JC, Tuck AB, Chambers AF. Role of the metastasis-promoting protein osteopontin in the tumour microenvironment. J Cell Mol Med. 2010; 14:2037-2044.
13. Shevde LA, Samant RS. Role of osteopontin in the pathophysiology of cancer. Matrix Biol. 2014; 37:131-141.
14. Wang KX, Denhardt DT. Osteopontin: role in immune regulation and stress responses. Cytokine Growth Factor Rev. 2008; 19:333-345.
15. Rangaswami H, Bulbule A, Kundu GC. Osteopontin: role in cell signaling and cancer progression. Trends Cell Biol. 2006; 16:79-87.
16. Guo B, Tumang JR, Rothstein TL. B cell receptor crosstalk: B cells express osteopontin through the combined action of the alternate and classical BCR signaling pathways. Mol Immunol. 2009; 46:587-591.
17. Kunii Y, Niwa S, Hagiwara Y, Maeda M, Seitoh T, Suzuki T. The immunohistochemical expression profile of osteopontin in normal human tissues using two site-specific antibodies reveals a wide distribution of positive cells and extensive expression in the central and peripheral nervous systems. Med Mol Morphol. 2009; 42:155-161.
18. Steinman L. A molecular trio in relapse and remission in multiple sclerosis. Nat Rev Immunol. 2009; 9:440-447.
19. Atai NA, Bansal M, Lo C, Bosman J, Tigchelaar W, Bosch KS, Jonker A, De Witt Hamer PC, Troost D, McCulloch CA, Everts V, Van Noorden CJ, Sodek J. Osteopontin is up-regulated and associated with neutrophil and macrophage infiltration in glioblastoma. Immunology. 2010.
20. Toy H, Yavas O, Eren O, Genc M, Yavas C. Correlation between osteopontin protein expression and histological grade of astrocytomas. Pathol Oncol Res. 2009; 15:203-207.
21. Inoue M, Shinohara ML. Intracellular osteopontin (iOPN) and immunity. Immunol Res. 2011; 49:160-172.
22. Lipinski CA, Tran NL, Menashi E, Rohl C, Kloss J, Bay RC, Berens ME, Loftus JC. The tyrosine kinase pyk2 promotes migration and invasion of glioma cells. Neoplasia. 2005; 7:435-445.
23. Das R, Mahabeleshwar GH, Kundu GC. Osteopontin stimulates cell motility and nuclear factor kappaB-mediated secretion of urokinase type plasminogen activator through phosphatidylinositol 3-kinase/Akt signaling pathways in breast cancer cells. J Biol Chem. 2003; 278:28593-28606.
24. Liu J, Xu K, Chase M, Ji Y, Logan JK, Buchsbaum RJ. Tiam1-regulated osteopontin in senescent fibroblasts contributes to the migration and invasion of associated epithelial cells. J Cell Sci. 2012; 125:376-386.
25. Scatena M, Almeida M, Chaisson ML, Fausto N, Nicosia RF, Giachelli CM. NF-kappaB mediates alphavbeta3 integrin-induced endothelial cell survival. J Cell Biol. 1998; 141:1083-1093.
26. Deckert M, Montesinos-Rongen M, Brunn A, Siebert R. Systems biology of primary CNS lymphoma: from genetic aberrations to modeling in mice. Acta Neuropathol. 2014; 127:175-188.
27. Compagno M, Lim WK, Grunn A, Nandula SV, Brahmachary M, Shen Q, Bertoni F, Ponzoni M, Scandurra M, Califano A, Bhagat G, Chadburn A, Dalla-Favera R, et al. Mutations of multiple genes cause deregulation of NF-κB in diffuse large B-cell lymphoma. Nature. 2009; 459:717-721.
28. Bond M, Chase AJ, Baker AH, Newby AC. Inhibition of transcription factor NF-kappaB reduces matrix metalloproteinase-1, -3 and -9 production by vascular smooth muscle cells. Cardiovasc Res. 2001; 50:556-565.
29. Tak PP, Firestein GS. NF-kappaB: a key role in inflammatory diseases. J Clin Invest. 2001; 107:7-11.
30. Wai PY, Kuo PC. Osteopontin: regulation in tumor metastasis. Cancer Metastasis Rev. 2008; 27:103-118.
31. Junaid A, Moon MC, Harding GE, Zahradka P. Osteopontin localizes to the nucleus of 293 cells and associates with polo-like kinase-1. Am J Physiol. 2007; 292:C919-926.
32. Philip S, Bulbule A, Kundu GC. Osteopontin stimulates tumor growth and activation of promatrix metalloproteinase-2 through nuclear factor-kappa B-mediated induction of membrane type 1 matrix metalloproteinase in murine melanoma cells. J Biol Chem. 2001; 276:44926-44935.
33. Wai PY, Kuo PC. The role of Osteopontin in tumor metastasis. J Surg Res. 2004; 121:228-241.
34. Chen YJ, Wei YY, Chen HT, Fong YC, Hsu CJ, Tsai CH, Hsu HC, Liu SH, Tang CH. Osteopontin increases migration and MMP-9 up-regulation via alphavbeta3 integrin, FAK, ERK, and NF-kappaB-dependent pathway in human chondrosarcoma cells. J Cell Physiol. 2009; 221:98-108.
35. Kumar V, Behera R, Lohite K, Karnik S, Kundu GC. p38 kinase is crucial for osteopontin-induced furin expression that supports cervical cancer progression. Cancer Res. 2010; 70:10381-10391.
36. Samant RS, Clark DW, Fillmore RA, Cicek M, Metge BJ, Chandramouli KH, Chambers AF, Casey G, Welch DR, Shevde LA. Breast cancer metastasis suppressor 1 (BRMS1) inhibits osteopontin transcription by abrogating NF-kappaB activation. Mol Cancer. 2007; 6:6.
37. Zhao W, Wang L, Zhang M, Wang P, Zhang L, Yuan C, Qi J, Qiao Y, Kuo PC, Gao C. NF-kappaB- and AP-1- mediated DNA looping regulates osteopontin transcription in endotoxin-stimulated murine macrophages. J Immunol. 2011; 186:3173-3179.
38. Heyninck K, De Valck D, Vanden Berghe W, Van Criekinge W, Contreras R, Fiers W, Haegeman G, Beyaert R. The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. J Cell Biol. 1999; 145:1471-1482.
39. Zhou J, Wu R, High AA, Slaughter CA, Finkelstein D, Rehg JE, Redecke V, Hacker H. A20-binding inhibitor of NF-kappaB (ABIN1) controls Toll-like receptor-mediated CCAAT/enhancer-binding protein beta activation and protects from inflammatory disease. Proc Natl Acad Sci U S A. 2011; 108:E998-1006.
40. Rangaswami H, Bulbule A, Kundu GC. Nuclear factorinducing kinase plays a crucial role in osteopontin-induced MAPK/IkappaBalpha kinase-dependent nuclear factor kappaB-mediated promatrix metalloproteinase-9 activation. J Biol Chem. 2004; 279:38921-38935.
41. Kim SW, Ramasamy K, Bouamar H, Lin AP, Jiang D, Aguiar RC. MicroRNAs miR-125a and miR-125b constitutively activate the NF-kappaB pathway by targeting the tumor necrosis factor alpha-induced protein (TNFAIP3, A20). Proc Natl Acad Sci U S A. 2012; 109:7865-7870.
42. Zhang R, Pan X, Huang Z, Weber GF, Zhang G. Osteopontin enhances the expression and activity of MMP- 2 via the SDF-1/CXCR4 axis in hepatocellular carcinoma cell lines. PLoS One. 2011; 6:e23831.
43. Dejonckheere E, Vandenbroucke RE, Libert C. Matrix metalloproteinase8 has a central role in inflammatory disorders and cancer progression. Cytokine Growth Factor Rev. 2011; 22:73-81.
44. Schubert-Unkmeir A, Konrad C, Slanina H, Czapek F, Hebling S, Frosch M. Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8. PLoS Pathog. 2010; 6:e1000874.
45. Zhou Y, Liu X, Xu L, Tseng H, Cao Y, Jiang J, Ciccarelli BT, Yang G, Patterson CJ, Hunter ZR, Treon SP. Matrix metalloproteinase-8 is overexpressed in Waldenstrom's macroglobulinemia cells, and specific inhibition of this metalloproteinase blocks release of soluble CD27. Clin Lymphoma Myeloma Leuk. 2011; 11:172-175.
46. Mato AR GJ, Putt ME, et al. Baseline serum cytokines profiles in mantle cell lymphoma correlates with outcome. 54th ASH Annual Meeting Abstract. 2012.
47. Iwanaga Y, Ueno M, Ueki M, Huang CL, Tomita S, Okamoto Y, Ogawa T, Ueda N, Maekawa N, Sakamoto H. The expression of osteopontin is increased in vessels with blood-brain barrier impairment. Neuropathol Appl Neurobiol. 2008; 34:145-154.
48. Bartsch JE, Staren ED, Appert HE. Matrix metalloproteinase expression in breast cancer. J Surg Res. 2003; 110:383-392.
49. Li Z, Qiu Y, Personett D, Huang P, Edenfield B, Katz J, Babusis D, Tang Y, Shirely MA, Moghaddam MF, Copland JA, Tun HW. Pomalidomide shows significant therapeutic activity against CNS lymphoma with a major impact on the tumor microenvironment in murine models. PLoS One. 2013; 8:e71754.