Cytokine & Growth Factor Reviews
Volume 21, Issue 1 , Pages 67-76 , February 2010

Matricellular proteins and inflammatory cells: A task force to promote or defeat cancer?

References 

  1. Tlsty TD, Coussens LM. Tumor stroma and regulation of cancer development. Annu Rev Pathol. 2006;1:119–150
  2. Drake CG, Jaffee E, Pardoll DM. Mechanisms of immune evasion by tumors. Adv Immunol. 2006;90:51–81
  3. Rabinovich GA, Gabrilovich D, Sotomayor EM. Immunosuppressive strategies that are mediated by tumor cells. Annu Rev Immunol. 2007;25:267–296
  4. Dunn GP, Old LJ, Schreiber RD. The three Es of cancer immunoediting. Annu Rev Immunol. 2004;22:329–360
  5. Sakaguchi S. Naturally arising CD4+ regulatory t cells for immunologic self-tolerance and negative control of immune responses. Annu Rev Immunol. 2004;22:531–562
  6. Terabe M, Matsui S, Noben-Trauth N, et al. NKT cell-mediated repression of tumor immunosurveillance by IL-13 and the IL-4R-STAT6 pathway. Nat Immunol. 2000;1:515–520
  7. Colonna M, Trinchieri G, Liu YJ. Plasmacytoid dendritic cells in immunity. Nat Immunol. 2004;5:1219–1226
  8. Sotomayor EM, Borrello I, Rattis FM, et al. Cross-presentation of tumor antigens by bone marrow-derived antigen-presenting cells is the dominant mechanism in the induction of T-cell tolerance during B-cell lymphoma progression. Blood. 2001;98:1070–1077
  9. Morgan DJ, Kreuwel HT, Fleck S, Levitsky HI, Pardoll DM, Sherman LA. Activation of low avidity CTL specific for a self epitope results in tumor rejection but not autoimmunity. J Immunol. 1998;160:643–651
  10. Overwijk WW, Theoret MR, Finkelstein SE, et al. Tumor regression and autoimmunity after reversal of a functionally tolerant state of self-reactive CD8+ T cells. J Exp Med. 2003;198:569–580
  11. de Visser KE, Eichten A, Coussens LM. Paradoxical roles of the immune system during cancer development. Nat Rev Cancer. 2006;6:24–37
  12. Sotomayor EM, Borrello I, Tubb E, et al. Conversion of tumor-specific CD4+ T-cell tolerance to T-cell priming through in vivo ligation of CD40. Nat Med. 1999;5:780–787
  13. Luo JL, Maeda S, Hsu LC, Yagita H, Karin M. Inhibition of NF-kappaB in cancer cells converts inflammation- induced tumor growth mediated by TNFalpha to TRAIL-mediated tumor regression. Cancer Cell. 2004;6:297–305
  14. Swann JB, Vesely MD, Silva A, et al. Demonstration of inflammation-induced cancer and cancer immunoediting during primary tumorigenesis. Proc Natl Acad Sci USA. 2008;105:652–656
  15. Balkwill F, Charles KA, Mantovani A. Smoldering and polarized inflammation in the initiation and promotion of malignant disease. Cancer Cell. 2005;7:211–217
  16. Thun MJ, Henley SJ, Patrono C. Nonsteroidal anti-inflammatory drugs as anticancer agents: mechanistic, pharmacologic, and clinical issues. J Natl Cancer Inst. 2002;94:252–266
  17. Rahme E, Barkun AN, Toubouti Y, Bardou M. The cyclooxygenase-2-selective inhibitors rofecoxib and celecoxib prevent colorectal neoplasia occurrence and recurrence. Gastroenterology. 2003;125:404–412
  18. Cottone M, Scimeca D, Mocciaro F, Civitavecchia G, Perricone G, Orlando A. Clinical course of ulcerative colitis. Dig Liver Dis. 2008;40(Suppl. 2):S247–S252
  19. Houghton AM, Mouded M, Shapiro SD. Common origins of lung cancer and COPD. Nat Med. 2008;14:1023–1024
  20. Coley WB. The treatment of malignant tumors by repeated inoculations of erysipelas: with a report of ten original cases. Am J Med Sci. 1893;105:487–511
  21. Mueller A, O’Rourke J, Chu P, et al. The role of antigenic drive and tumor-infiltrating accessory cells in the pathogenesis of helicobacter-induced mucosa-associated lymphoid tissue lymphoma. Am J Pathol. 2005;167:797–812
  22. Sutton P, O’Rourke J, Wilson J, Dixon MF, Lee A. Immunisation against Helicobacter felis infection protects against the development of gastric MALT Lymphoma. Vaccine. 2004;22:2541–2546
  23. Schaider H, Oka M, Bogenrieder T, et al. Differential response of primary and metastatic melanomas to neutrophils attracted by IL-8. Int J Cancer. 2003;103:335–343
  24. Apetoh L, Ghiringhelli F, Tesniere A, et al. Toll-like receptor 4-dependent contribution of the immune system to anticancer chemotherapy and radiotherapy. Nat Med. 2007;13:1050–1059
  25. Nozawa H, Chiu C, Hanahan D. Infiltrating neutrophils mediate the initial angiogenic switch in a mouse model of multistage carcinogenesis. Proc Natl Acad Sci USA. 2006;103:12493–12498
  26. Bornstein P, Sage EH. Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol. 2002;14:608–616
  27. Elola MT, Wolfenstein-Todel C, Troncoso MF, Vasta GR, Rabinovich GA. Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival. Cell Mol Life Sci. 2007;64:1679–1700
  28. Dvorak HF. Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl J Med. 1986;315:1650–1659
  29. Podhajcer OL, Benedetti LG, Girotti MR, Prada F, Salvatierra E, Llera AS. The role of the matricellular protein SPARC in the dynamic interaction between the tumor and the host. Cancer Metastasis Rev. 2008;27:691–705
  30. Kaufmann B, Muller S, Hanisch FG, et al. Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity. Glycobiology. 2004;14:609–619
  31. Ledda MF, Adris S, Bravo AI, et al. Suppression of SPARC expression by antisense RNA abrogates the tumorigenicity of human melanoma cells. Nat Med. 1997;3:171–175
  32. Alvarez MJ, Prada F, Salvatierra E, et al. Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity. Cancer Res. 2005;65:5123–5132
  33. Prada F, Benedetti LG, Bravo AI, Alvarez MJ, Carbone C, Podhajcer OL. SPARC endogenous level, rather than fibroblast-produced SPARC or stroma reorganization induced by SPARC, is responsible for melanoma cell growth. J Invest Dermatol. 2007;127:2618–2628
  34. Sosa MS, Girotti MR, Salvatierra E, et al. Proteomic analysis identified N-cadherin, clusterin, and HSP27 as mediators of SPARC (secreted protein, acidic and rich in cysteines) activity in melanoma cells. Proteomics. 2007;7:4123–4134
  35. Barker TH, Baneyx G, Cardo-Vila M, et al. SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity. J Biol Chem. 2005;280:36483–36493
  36. Shi Q, Bao S, Song L, et al. Targeting SPARC expression decreases glioma cellular survival and invasion associated with reduced activities of FAK and ILK kinases. Oncogene. 2007;26:4084–4094
  37. Weaver MS, Workman GA, Sage EH. The copper-binding domain of sparc mediates cell survival in vitro via interaction with integrin beta 1 and activation of integrin-linked kinase. J Biol Chem. 2008;23:23
  38. Lane TF, Iruela-Arispe ML, Sage EH. Regulation of gene expression by SPARC during angiogenesis in vitro, changes in fibronectin, thrombospondin-1 and plasminogen activator inhibitor-1. J Biol Chem. 1992;267:16736–16745
  39. Lupetti R, Mortarini R, Panceri P, Sensi M, Anichini A. Interaction with fibronectin regulates cytokine gene expression in human melanoma cells. Int J Cancer. 1996;66:110–116
  40. White ES, Livant DL, Markwart S, Arenberg DA. Monocyte-fibronectin interactions, via alpha(5)beta(1) integrin, induce expression of CXC chemokine-dependent angiogenic activity. J Immunol. 2001;167:5362–5366
  41. Prud’homme GJ. Pathobiology of transforming growth factor beta in cancer, fibrosis and immunologic disease, and therapeutic considerations. Lab Invest. 2007;87:1077–1091
  42. Bassuk JA, Pichler R, Rothmier JD, et al. Induction of TGF-beta1 by the matricellular protein SPARC in a rat model of glomerulonephritis. Kidney Int. 2000;57:117–128
  43. Francki A, Bradshaw AD, Bassuk JA, Howe CC, Couser WG, Sage EH. SPARC regulates the expression of collagen type I and transforming growth factor-beta1 in mesangial cells. J Biol Chem. 1999;274:32145–32152
  44. Francki A, McClure TD, Brekken RA, et al. SPARC regulates TGF-beta1-dependent signaling in primary glomerular mesangial cells. J Cell Biochem. 2004;91:915–925
  45. Schiemann BJ, Neil JR, Schiemann WP. SPARC inhibits epithelial cell proliferation in part through stimulation of the TGF-beta-signaling system. Mol Biol Cell. 2003;14:3977–3988
  46. Zhou X, Tan FK, Guo X, et al. Small interfering RNA inhibition of SPARC attenuates the profibrotic effect of transforming growth factor beta1 in cultured normal human fibroblasts. Arthritis Rheum. 2005;52:257–261
  47. Ford R, Wang G, Jannati P, et al. Modulation of SPARC expression during butyrate-induced terminal differentiation of cultured human keratinocytes: regulation via a TGF-beta-dependent pathway. Exp Cell Res. 1993;206:261–275
  48. Reed MJ, Vernon RB, Abrass IB, Sage EH. TGF-β 1 induces the expression of type I collagen and SPARC, and enhances contraction of collagen gels, by fibroblasts from young and aged donors. J Cell Physiol. 1994;158:169–179
  49. Shanker G, Olson D, Bone R, Sawhney R. Regulation of extracellular matrix proteins by transforming growth factor beta1 in cultured pulmonary endothelial cells. Cell Biol Int. 1999;23:61–72
  50. Shiba H, Uchida Y, Kamihagi K, et al. Transforming growth factor-beta1 and basic fibroblast growth factor modulate osteocalcin and osteonectin/SPARC syntheses in vitamin-D-activated pulp cells. J Dent Res. 2001;80:1653–1659
  51. Wrana JL, Overall CM, Sodek J. Regulation of the expression of a secreted acidic protein rich in cysteine (SPARC) in human fibroblasts by transforming growth factor beta. comparison of transcriptional and post-transcriptional control with fibronectin and type I collagen. Eur J Biochem. 1991;197:519–528
  52. Bierie B, Moses HL. Tumour microenvironment: TGFbeta: the molecular Jekyll and Hyde of cancer. Nat Rev Cancer. 2006;6:506–520
  53. Ahmadzadeh M, Rosenberg SA. TGF-beta 1 attenuates the acquisition and expression of effector function by tumor antigen-specific human memory CD8 T cells. J Immunol. 2005;174:5215–5223
  54. Kitamura M. Identification of an inhibitor targeting macrophage production of monocyte chemoattractant protein-1 as TGF-beta 1. J Immunol. 1997;159:1404–1411
  55. Chen JJ, Sun Y, Nabel GJ. Regulation of the proinflammatory effects of Fas ligand (CD95L). Science. 1998;282:1714–1717
  56. Miwa K, Asano M, Horai R, Iwakura Y, Nagata S, Suda T. Caspase 1-independent IL-1beta release and inflammation induced by the apoptosis inducer Fas ligand. Nat Med. 1998;4:1287–1292
  57. Fridlender ZG, Sun J, Kim S, et al. Polarization of tumor-associated neutrophil phenotype by TGF-beta: “N1” versus “N2” TAN. Cancer Cell. 2009;16:183–194
  58. Rodeck U, Bossler A, Graeven U, et al. Transforming growth factor beta production and responsiveness in normal human melanocytes and melanoma cells. Cancer Res. 1994;54:575–581
  59. Mantovani A. The yin-yang of tumor-associated neutrophils. Cancer Cell. 2009;16:173–174
  60. Sangaletti S, Stoppacciaro A, Guiducci C, Torrisi MR, Colombo MP. Leukocyte, rather than tumor-produced SPARC, determines stroma and collagen type IV deposition in mammary carcinoma. J Exp Med. 2003;198:1475–1485
  61. Sangaletti S, Di Carlo E, Gariboldi S, et al. Macrophage-derived SPARC bridges tumor cell-extracellular matrix interactions toward metastasis. Cancer Res. 2008;68:9050–9059
  62. Yiu GK, Chan WY, Ng SW, et al. SPARC (secreted protein acidic and rich in cysteine) induces apoptosis in ovarian cancer cells. Am J Pathol. 2001;159:609–622
  63. Said N, Socha MJ, Olearczyk JJ, Elmarakby AA, Imig JD, Motamed K. Normalization of the ovarian cancer microenvironment by SPARC. Mol Cancer Res. 2007;5:1015–1030
  64. Said NA, Elmarakby AA, Imig JD, Fulton DJ, Motamed K. SPARC ameliorates ovarian cancer-associated inflammation. Neoplasia. 2008;10:1092–1104
  65. Rempel SA, Hawley RC, Gutierrez JA, et al. Splenic and immune alterations of the sparc-null mouse accompany a lack of immune response. Genes Immun. 2007;8:262–274
  66. Savani RC, Zhou Z, Arguiri E, et al. Bleomycin-induced pulmonary injury in mice deficient in SPARC. Am J Physiol Lung Cell Mol Physiol. 2000;279:L743–750
  67. Camino AM, Atorrasagasti C, Maccio D, et al. Adenovirus-mediated inhibition of SPARC attenuates liver fibrosis in rats. J Gene Med. 2008;10:993–1004
  68. Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN, Helene Sage E. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J Invest Dermatol. 2003;120:949–955
  69. Zhou X, Tan FK, Guo X, Arnett FC. Attenuation of collagen production with small interfering RNA of SPARC in cultured fibroblasts from the skin of patients with scleroderma. Arthritis Rheum. 2006;54:2626–2631
  70. Rentz TJ, Poobalarahi F, Bornstein P, Sage EH, Bradshaw AD. SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts. J Biol Chem. 2007;282:22062–22071
  71. Strandjord TP, Madtes DK, Weiss DJ, Sage EH. Collagen accumulation is decreased in SPARC-null mice with bleomycin-induced pulmonary fibrosis. Am J Physiol. 1999;277:L628–L635
  72. Rotta G, Matteoli G, Mazzini E, Nuciforo P, Colombo MP, Rescigno M. Contrasting roles of SPARC-related granuloma in bacterial containment and in the induction of anti-Salmonella typhimurium immunity. J Exp Med. 2008;205:657–667
  73. Sangaletti S, Gioiosa L, Guiducci C, et al. Accelerated dendritic-cell migration and T-cell priming in SPARC-deficient mice. J Cell Sci. 2005;118:3685–3694
  74. Socha MJ, Manhiani M, Said N, Imig JD, Motamed K. Secreted protein acidic and rich in cysteine deficiency ameliorates renal inflammation and fibrosis in angiotensin hypertension. Am J Pathol. 2007;171:1104–1112
  75. Kyriakides TR, Bornstein P. Matricellular proteins as modulators of wound healing and the foreign body response. Thromb Haemost. 2003;90:986–992
  76. Lawler J, Sunday M, Thibert V, et al. Thrombospondin-1 is required for normal murine pulmonary homeostasis and its absence causes pneumonia. J Clin Invest. 1998;101:982–992
  77. Liaw L, Birk DE, Ballas CB, Whitsitt JS, Davidson JM, Hogan BL. Altered wound healing in mice lacking a functional osteopontin gene (spp1). J Clin Invest. 1998;101:1468–1478
  78. Mansfield PJ, Boxer LA, Suchard SJ. Thrombospondin stimulates motility of human neutrophils. J Cell Biol. 1990;111:3077–3086
  79. Riser BL, Mitra R, Perry D, Dixit V, Varani J. Monocyte killing of human squamous epithelial cells: role for thrombospondin. Cancer Res. 1989;49:6123–6129
  80. Martin-Manso G, Galli S, Ridnour LA, Tsokos M, Wink DA, Roberts DD. Thrombospondin 1 promotes tumor macrophage recruitment and enhances tumor cell cytotoxicity of differentiated U937 cells. Cancer Res. 2008;68:7090–7099
  81. Agah A, Kyriakides TR, Lawler J, Bornstein P. The lack of thrombospondin-1 (TSP1) dictates the course of wound healing in double-TSP1/TSP2-null mice. Am J Pathol. 2002;161:831–839
  82. Murphy-Ullrich JE, Poczatek M. Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine Growth Factor Rev. 2000;11:59–69
  83. Patarca R, Freeman GJ, Singh RP, et al. Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene. Definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection. J Exp Med. 1989;170:145–161
  84. Rudland PS, Platt-Higgins A, El-Tanani M, et al. Prognostic significance of the metastasis-associated protein osteopontin in human breast cancer. Cancer Res. 2002;62:3417–3427
  85. Singhal H, Bautista DS, Tonkin KS, et al. Elevated plasma osteopontin in metastatic breast cancer associated with increased tumor burden and decreased survival. Clin Cancer Res. 1997;3:605–611
  86. Tuck AB, O’Malley FP, Singhal H, et al. Osteopontin expression in a group of lymph node negative breast cancer patients. Int J Cancer. 1998;79:502–508
  87. Rodrigues LR, Teixeira JA, Schmitt FL, Paulsson M, Lindmark-Mansson H. The role of osteopontin in tumor progression and metastasis in breast cancer. Cancer Epidemiol Biomarkers Prev. 2007;16:1087–1097
  88. Saeki Y, Mima T, Ishii T, et al. Enhanced production of osteopontin in multiple myeloma: clinical and pathogenic implications. Br J Haematol. 2003;123:263–270
  89. Hotte SJ, Winquist EW, Stitt L, Wilson SM, Chambers AF. Plasma osteopontin: associations with survival and metastasis to bone in men with hormone-refractory prostate carcinoma. Cancer. 2002;95:506–512
  90. Angelucci A, Festuccia C, Gravina GL, et al. Osteopontin enhances the cell proliferation induced by the epidermal growth factor in human prostate cancer cells. Prostate. 2004;59:157–166
  91. Bayless KJ, Meininger GA, Scholtz JM, Davis GE. Osteopontin is a ligand for the alpha4beta1 integrin. J Cell Sci. 1998;111(Pt 9):1165–1174
  92. Noti JD. Adherence to osteopontin via alphavbeta3 suppresses phorbol ester-mediated apoptosis in MCF-7 breast cancer cells that overexpress protein kinase C-alpha. Int J Oncol. 2000;17:1237–1243
  93. Feng B, Rollo EE, Denhardt DT. Osteopontin (OPN) may facilitate metastasis by protecting cells from macrophage NO-mediated cytotoxicity: evidence from cell lines down-regulated for OPN expression by a targeted ribozyme. Clin Exp Metastasis. 1995;13:453–462
  94. Rollo EE, Laskin DL, Denhardt DT. Osteopontin inhibits nitric oxide production and cytotoxicity by activated RAW264.7 macrophages. J Leukoc Biol. 1996;60:397–404
  95. Leali D, Dell’Era P, Stabile H, et al. Osteopontin (Eta-1) and fibroblast growth factor-2 cross-talk in angiogenesis. J Immunol. 2003;171:1085–1093
  96. Bourassa B, Monaghan S, Rittling SR. Impaired anti-tumor cytotoxicity of macrophages from osteopontin-deficient mice. Cell Immunol. 2004;227:1–11
  97. Takahashi K, Takahashi F, Hirama M, Tanabe KK, Fukuchi Y. Restoration of CD44S in non-small cell lung cancer cells enhanced their susceptibility to the macrophage cytotoxicity. Lung Cancer. 2003;41:145–153
  98. Hur EM, Youssef S, Haws ME, Zhang SY, Sobel RA, Steinman L. Osteopontin-induced relapse and progression of autoimmune brain disease through enhanced survival of activated T cells. Nat Immunol. 2007;8:74–83
  99. Okada H, Moriwaki K, Konishi K, et al. Tubular osteopontin expression in human glomerulonephritis and renal vasculitis. Am J Kidney Dis. 2000;36:498–506
  100. Ramaiah SK, Rittling S. Role of osteopontin in regulating hepatic inflammatory responses and toxic liver injury. Expert Opin Drug Metab Toxicol. 2007;3:519–526
  101. 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;205:43–51
  102. Behrem S, Zarkovic K, Eskinja N, Jonjic N. Distribution pattern of tenascin-C in glioblastoma: correlation with angiogenesis and tumor cell proliferation. Pathol Oncol Res. 2005;11:229–235
  103. Ilmonen S, Jahkola T, Turunen JP, Muhonen T, Asko-Seljavaara S. Tenascin-C in primary malignant melanoma of the skin. Histopathology. 2004;45:405–411
  104. Kulla A, Liigant A, Piirsoo A, Rippin G, Asser T. Tenascin expression patterns and cells of monocyte lineage: relationship in human gliomas. Mod Pathol. 2000;13:56–67
  105. Parekh K, Ramachandran S, Cooper J, Bigner D, Patterson A, Mohanakumar T. Tenascin-C, over expressed in lung cancer down regulates effector functions of tumor infiltrating lymphocytes. Lung Cancer. 2005;47:17–29
  106. Talts JF, Wirl G, Dictor M, Muller WJ, Fassler R. Tenascin-C modulates tumor stroma and monocyte/macrophage recruitment but not tumor growth or metastasis in a mouse strain with spontaneous mammary cancer. J Cell Sci. 1999;112(Pt 12):1855–1864
  107. Lebensztejn DM, Sobaniec-Lotowska ME, Kaczmarski M, Voelker M, Schuppan D. Matrix-derived serum markers in monitoring liver fibrosis in children with chronic hepatitis B treated with interferon alpha. World J Gastroenterol. 2006;12:3338–3343
  108. Nakahara H, Gabazza EC, Fujimoto H, et al. Deficiency of tenascin C attenuates allergen-induced bronchial asthma in the mouse. Eur J Immunol. 2006;36:3334–3345
  109. Camby I, Le Mercier M, Lefranc F, Kiss R. Galectin-1: a small protein with major functions. Glycobiology. 2006;16:137R–157R
  110. Ilarregui JM, Bianco GA, Toscano MA, Rabinovich GA. The coming of age of galectins as immunomodulatory agents: impact of these carbohydrate binding proteins in T cell physiology and chronic inflammatory disorders. Ann Rheum Dis. 2005;64:iv96–iv103
  111. Danguy A, Camby I, Kiss R, Galectins cancer. Biochim Biophys Acta. 2002;1572:285–293
  112. Salatino M, Croci DO, Bianco GA, Ilarregui JM, Toscano MA, Rabinovich GA. Galectin-1 as a potential therapeutic target in autoimmune disorders and cancer. Expert Opin Biol Ther. 2008;8:45–57
  113. Rabinovich GA, Ariel A, Hershkoviz R, Hirabayashi J, Kasai KI, Lider O. Specific inhibition of T-cell adhesion to extracellular matrix and proinflammatory cytokine secretion by human recombinant galectin-1. Immunology. 1999;97:100–106
  114. Santucci L, Fiorucci S, Rubinstein N, et al. Galectin-1 suppresses experimental colitis in mice. Gastroenterology. 2003;124:1381–1394
  115. Rabinovich GA, Daly G, Dreja H, et al. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. J Exp Med. 1999;190:385–398
  116. Rubinstein N, Alvarez M, Zwirner NW, et al. Targeted inhibition of galectin-1 gene expression in tumor cells results in heightened T cell-mediated rejection; a potential mechanism of tumor-immune privilege. Cancer Cell. 2004;5:241–251
  117. Peng W, Wang HY, Miyahara Y, Peng G, Wang RF. Tumor-associated galectin-3 modulates the function of tumor-reactive T cells. Cancer Res. 2008;68:7228–7236
  118. Zubieta MR, Furman D, Barrio M, Bravo AI, Domenichini E, Mordoh J. Galectin-3 expression correlates with apoptosis of tumor-associated lymphocytes in human melanoma biopsies. Am J Pathol. 2006;168:1666–1675
  119. Dumont P, Berton A, Nagy N, et al. Expression of galectin-3 in the tumor immune response in colon cancer. Lab Invest. 2008;88:896–906
  120. Nagahara K, Arikawa T, Oomizu S, et al. Galectin-9 increases Tim-3+ dendritic cells and CD8+ T cells and enhances antitumor immunity via galectin-9-Tim-3 interactions. J Immunol. 2008;181:7660–7669
  121. Pirinen R, Leinonen T, Bohm J, et al. Versican in nonsmall cell lung cancer: relation to hyaluronan, clinicopathologic factors, and prognosis. Hum Pathol. 2005;36:44–50
  122. Kim S, Takahashi H, Lin WW, et al. Carcinoma-produced factors activate myeloid cells through TLR2 to stimulate metastasis. Nature. 2009;457:102–106
  123. Mantovani A. Cancer: inflaming metastasis. Nature. 2009;457:36–37
  124. Daniel C, Amann K, Hohenstein B, Bornstein P, Hugo C. Thrombospondin 2 functions as an endogenous regulator of angiogenesis and inflammation in experimental glomerulonephritis in mice. J Am Soc Nephrol. 2007;18:788–798
  125. Frey AB, Wali A, Pass H, Lonardo F. Osteopontin is linked to p65 and MMP-9 expression in pulmonary adenocarcinoma but not in malignant pleural mesothelioma. Histopathology. 2007;50:720–726
  126. Motamed K. SPARC (osteonectin/BM-40). Int J Biochem Cell Biol. 1999;31:1363–1366
  127. Funk SE, Sage EH. Differential effects of SPARC and cationic SPARC peptides on DNA synthesis by endothelial cells and fibroblasts. J Cell Physiol. 1993;154:53–63
  128. Lane TF, Iruela-Arispe ML, Johnson RS, Sage EH. SPARC is a source of copper-binding peptides that stimulate angiogenesis. J Cell Biol. 1994;125:929–943
  129. Chen Y, Wang X, Weng D, Tao S, Lv L, Chen J. A TSP-1 functional fragment inhibits activation of latent transforming growth factor-beta1 derived from rat alveolar macrophage after bleomycin treatment. Exp Toxicol Pathol. 2009;61:67–73
  130. Senger DR, Perruzzi CA, Papadopoulos-Sergiou A, Van de Water L. Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain. Mol Biol Cell. 1994;5:565–574
  131. Yasuda M, Nakano K, Yasumoto K, Tanaka Y. CD44: functional relevance to inflammation and malignancy. Histol Histopathol. 2002;17:945–950
  132. Schor SL, Schor AM. Phenotypic and genetic alterations in mammary stroma: implications for tumour progression. Breast Cancer Res. 2001;3:373–379
  133. Maquart FX, Pasco S, Ramont L, Hornebeck W, Monboisse JC. An introduction to matrikines: extracellular matrix-derived peptides which regulate cell activity. Implication in tumor invasion. Crit Rev Oncol Hematol. 2004;49:199–202
  134. Brekken RA, Sage EH. SPARC, a matricellular protein: at the crossroads of cell-matrix. Matrix Biol. 2000;19:569–580
  135. Sasaki T, Gohring W, Mann K, et al. Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J Biol Chem. 1997;272:9237–9243
  136. Adair-Kirk TL, Senior RM. Fragments of extracellular matrix as mediators of inflammation. Int J Biochem Cell Biol. 2008;40:1101–1110
  137. Lin WW, Karin M. A cytokine-mediated link between innate immunity, inflammation, and cancer. J Clin Invest. 2007;117:1175–1183

PII: S1359-6101(09)00117-8

doi: 10.1016/j.cytogfr.2009.11.010

Cytokine & Growth Factor Reviews
Volume 21, Issue 1 , Pages 67-76 , February 2010

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