Matrix Metalloproteinases and Their Tissue Inhibitors - Expression, Role and Regulation in Human Malignant Non-Hodgkin's Lymphomas

References

• Writing Committee, Rosenberg S. A., chairman. National Cancer Institute sponsored study of classifications of non-Hodgkin's lymphomas. Summary and description of a Working Formulation for clinical usage. Cancer 1982; 49: 2112–2135
   PubMed Web of Science ®Google Scholar
• Harris N. L., Jaffe E. S., Stein H., Banks P. M., Chan J. K. C., Cleary M. L., Delsol G., De Wolf-Peeters C., Falini B., Gatter K. C., Grogan T. M., Isaacson P. G., Knowles D. M., Mason D. Y., Muller-Hermelink H-K., Pileri S. A., Ralfkiaer M. A., Piris E., Warnke R. A. A revised European-American Classification of Lymphoid Neoplasms: B proposal from the international lymphoma study group. Blood 1994; 5: 1361–1392
   Google Scholar
• Stauder R., Hamader S., Fashing B., Kemmler G., Thaler J., Huber H. Adhesion to high endothelial venules: a model for dissemination mechanisms in non-Hodgkin's lymphoma. Blood 1993; 82: 262–267
   PubMed Web of Science ®Google Scholar
• Müller-Hermelink H. K., Lennert K. Malignant lymphomas other than Hodgkin's disease, K Lennert, N Mohri, H. Stein, E Kaiserling, H K Müller-Hermelink. Springer-Verlag Berlin Heidelberg, New York 1978
   Google Scholar
• Cotran R. S., Kumar V., Robbins S. L. Malignant lymphomas. In Robbins Pathologic Basis of Disease, R. S. Cotran, V. Kumar, S. L. Robbins. W. B. Saunders Company, Toronto 1994; 634–648
   Google Scholar
• McCurley T. L., Gay R. E., Gay S., Click A. D., Haralson M. A., Collins R. D. The extracellular matrix in “sclerosing” follicular center cell lymphomas: an immuno-histochemical and ultrastructural study. Human Pathology 1986; 17: 930–938
   PubMed Web of Science ®Google Scholar
• McCurley T. L., Gay R. E., Gay S., Click A. D., Jones M. R., Haralson M. A., Collins R. D. The extracellular matrix in large cell lymphomas: a histopathologic, immunohistochemical, and ultrastructural study. Human Pathology 1989; 20: 164–173
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Urbanski S. J., Watson A., Hayden L. J., Edwards D. R. Patterns of expression of metalloproteinases and their inhibitors in human malignant lymphomas. Oncology Research 1993; 5: 19–28
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Urbanski S. J., Huchcroft S. A., Edwards D. R. Relationship between the clinical aggressiveness of large cell immunoblastic lymphomas and expression of 92 kDa gelatinase (Type IV Collagenase) and tissue inhibitor of metalloproteinase -1 (TIMP-I) RNAs. Oncology Research 1992; 4: 233–240
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Hinek A., Edwards D. R., Lim M. S., Zhang Ch-L., Breitman D. R., Prusinkiewiez C., Stabbler A. L., Urbanski L. S., Urbanski S. J. Proteolytic activity of human non-Hodgkin's lymphomas. American Journal of Pathology 1998; 152: 565–576
   PubMed Web of Science ®Google Scholar
• Goetzl E. J., Banda M. J., Leppert D. Matrix metalloproteinases in immunity. [Review]. Journal of Immunology 1996; 156: 1–4
   PubMed Web of Science ®Google Scholar
• Mainardi C. L., Pourmotabbed T. F., Haty K. A. Inflammatory phagocytes and connective tissue degrading metalloproteinases. American Journal of Medical Science 1991; 302: 171–175
   PubMed Web of Science ®Google Scholar
• Koop S., Schmidt E. E., MacDonald I. C., Morris V. L., Khokha R., Grattan M., Leone J., Chambers A. F., Groom A. C. Independence of metastatic ability and extravasation: metastatic ras-transformed and control fibroblasts extravasate equally well. Proceeding of the National Academy of Sciences of the United States of America 1996; 93: 11080–11084
   PubMed Web of Science ®Google Scholar
• Chambers A. F., MacDonald I. C., Schmidt E. E., Koop S., Morris V. L., Khokha R., Groom A. C. Steps in tumor metastasis: new concepts from intravital videomicroscopy. Cancer A Metastasis Reviews 1995; 14: 279–301
   PubMed Web of Science ®Google Scholar
• Murphy G. Matrix metalloproteinases and their inhibitors. Acta Orthopaedica Scandinavica 1995; 266: 55–60
   Google Scholar
• Matrisian L. M. The matrix-degrading metalloproteinases. BioEssays 1992; 14: 455–463
   PubMed Web of Science ®Google Scholar
• d'Ortho M. P., Will H., Atkinson S., Butler G., Messent A., Gavrilovic J., Smith B., Timpl R., Zardi L., Murphy G. Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. European Journal of Biochemistry 1997; 250: 751–757
   PubMedGoogle Scholar
• Murphy G., Cockett M. I., Ward R. V., Docherty J. P. Matrix metalloproteinase degradation of elastin. Type IV collagen and proteoglycan. Biochemistry Journal 1991; 277: 277–279
   PubMed Web of Science ®Google Scholar
• Birkedal-Hansen H., Moore W. G. I., Bodden M. K., Windsor L. J., Birkedal-Hansen B., De Carlo A., Engler J. A. Matrix metalloprotcinases: a review. Critical Reviews in Oral Biology Medicine 1993; 4: 197–250
   PubMedGoogle Scholar
• Whilhelm S. M., Collier I. E., Marmer B. L., Eisen A. Z., Grant G. A., Goldberg G. I. SV40-transformed human lung fibroblasts secrete a 92-kDa type-IV collagenase which is identical to that secreted by normal human macrophages. Journal of Biological Chemistry 1989; 264: 17213–17221
   PubMed Web of Science ®Google Scholar
• Senior R. M., Griffin G. L., Fliszar C. J., Shapiro S. D., Goldgerg G. I., Welgus H. G. Human 92- and 72-Kilodalton type IV collagenases are elastases. Journal of Biological Chemistry 1991; 266: 7870–7875
   PubMed Web of Science ®Google Scholar
• Shipley J. M., Doyle G. A., Fliszar C. J., Ye Q. Z., Johnson L. L., Shapiro S. D., Welgus H. G., Senior R. M. The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats. Journal of Biological Chemistry 1996; 271: 4335–4341
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Hucherott S. A., Urbanski S. J., Edwards D. R. Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia. Pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans. British Journal of Cancer 1996; 73: 1401–1408
   PubMed Web of Science ®Google Scholar
• Steller-Stevenson W. G., Hewitt R., Corcoran M. Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic. [Review]. Seminars in Cancer Biology 1996; 7: 147–154
   PubMed Web of Science ®Google Scholar
• Stetler-Stevenson M., Mansoor A., Lim M., Fukushima P., Kehrl J., Marti G., Ptaszynski K., Wang J., Stetler-Stevenson W. G. Expression of matrix metalloprotcinases and tissue inhibitors of metalloproteinases in reactive and neoplastic lymphoid cells. Blood 1997; 89: 1708–1715
   PubMed Web of Science ®Google Scholar
• Matsuzaki A., Janowska-Wieczorck A. Unstimulated human acute myelogenous leukemia blasts secrete matrix metalloproteinases. Journal of Cancer Research and Clinical Oncology 1997; 123: 100–106
   PubMed Web of Science ®Google Scholar
• Sawicki A., Matsuzaki G., Janowska-Wieczorck A. Expression of the active form of MMP-2 on the surface of leukemic cells accounts for their in Vitro invasion. Journal of Cancer Research and Clinical Oncology 1998; 124: 245–252
   PubMed Web of Science ®Google Scholar
• Janowska-Wicezorek A., Marquez L. A., Matsuzaki A., Hashmi H. R., Larratt L. M., Boshkov L. M., Turner A. R., Zhang M. C., Edwards D. R., Kossakowska A. E. Expression of matrix metalloproteinases (MMP-2 and -9) and tissue inhibitors of metalloproteinases (TIMP-I and -2) in tissue myelogenous leukaemia blasts: comparison with normal bone marrow cells. British Journal of Hematology 1999; 105: 402–411
   PubMed Web of Science ®Google Scholar
• Guedez L., Lim M. S., Stetler-Stevenson W. G. The role id metalloproteinases and their inhibitors in hematological disorders. Critical Reviews in Oncogenesis 1996; 7: 205–225
   PubMed Web of Science ®Google Scholar
• Di Girolamo N., Tedla N., Lloyd A., Waketïeld D. Expression of matrix metalloproteinases by human plasma cells and B lymphocytes. European Journal of Immunology 1998; 28: 1773–1784
   PubMed Web of Science ®Google Scholar
• Aoudijt F., Esteve P. O., Desrosiers M., Potworowski E. F., St-Pierre Y. Gelatinase B (MMP-9) production and expression by stromal cells in the normal and adult thymus and experimental thymic lymphoma. International Journal of Cancer 1997; 71: 71–78
   PubMed Web of Science ®Google Scholar
• Aoudjit E., Potworowski E. F., St-Pierre Y. Bi-directional induction of matrix metalloproteinase - 9 and tissue inhibitor of matrix metalloproteinase - 1 during T-lymphoma/endothelial cell contact: implication of ICAM-I. Journal of Immunology 1998; 160: 2967–2973
   PubMed Web of Science ®Google Scholar
• Aoudjit F., Masure S., Opdenakker G., Potworowski E. F., St-Pierre Y. (Gelatinase B (MMP-9), but not its inhibitor (TIMP-I). dictates the growth rate of Experimental thymic lymphoma. International Journal of Cancer 1999; 82: 743–747
   PubMed Web of Science ®Google Scholar
• Unemori E. N., Hibbs M. S., Amento E. P. Constitutive expression of a 92-kD Gelantinase (Type V Collagenase) by rheumatoid synovial lilbroblasts and its induction in normal human fibroblasts by inflammatory cytokines. Journal of Clinical Investigation 1991; 88: 1656–1662
   PubMed Web of Science ®Google Scholar
• Himelstein B. P., Canete-Soler R., Bernhard E. J., Muschell R. J. Induction of fibroblast 92 kDa gelatinase/ type IV collagenase expression by direct contact with metastatic tumor cells. Journal of Cell Science 1994; 107: 477–486
   PubMed Web of Science ®Google Scholar
• Sato H., Kida Y., Mai M., Endo Y., Sasaki T., Tanaka S., Seiki M. Expression of genes encoding type IV collagen-degrading metalloproteinases and tissue inhibitors of metalloproteinases in various human tumor cells. Oncogene 1992; 7: 77–83
   PubMed Web of Science ®Google Scholar
• Stetler-Stevenson W. G. Type IV collagenases in tumor invasion and metastasis. Cancer Metastasis Reviews 1990; 9: 289–303
   PubMed Web of Science ®Google Scholar
• Himelstein B. P., Canete-Soler R., Bernhard E. J., Dilks D. W., Muschel R. J. Metalloproteinases in tumor progression: the contribution of MMP-9. Invasion and Metastasis 1994; 95: 246–258
   Google Scholar
• Sier C. F., Kubben F. J., Ganesh S., Heerding M. M., Griffioen G., Hanemaaijer R., van Krieken J. H., Lamers C. B., Verspaget H. W. Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma. British Journal of Cancer 1996; 74: 413–417
   PubMed Web of Science ®Google Scholar
• Zucker S., Lysik R. M., Zarrabi M. H., Moll U. M. R. M(r) 92,000 type IV collagenase is increased in plasma of patients with colon cancer and breast cancer. Cancer Research 1993; 53: 140–146
   PubMed Web of Science ®Google Scholar
• Rao J. S., Steck P. A., Mohanam S., Stetler-Stevenson W. G., Liotta L. A., Sawaya R. Elevated levels of M(r) 92.000 type IV collagenase in human brain tumors. Cancer Research 1993; 53(10 suppl)2208–2211
   PubMed Web of Science ®Google Scholar
• Hanemaaijer R., Koolwijk P., le Clercq L., de Vree W. J. A., van Hinsbergh V. W. M. Regulation of matrix metalloproteinase expression in human vein and microvascular endothelial cells. Journal of Biochemistry 1993; 296: 803–809
   Google Scholar
• Montgomery A. M. P., Sabzevari H., Reisfeld R. A. Production and regulation of gelatinase B by human T-cells. Biochimical et Biophysica Acta 1993; 1176: 265–268
   PubMed Web of Science ®Google Scholar
• Watanabe H., Nakanishi I., Yamashita K., Hayakawa T., Okada Y. Matrix metalloproteinase-9 (92 kDa gelatinase/type IV collagenase) from U937 monoblastoid cells: correlation with cellular invasion. Cell Science 1993; 104: 991–999
   PubMed Web of Science ®Google Scholar
• Zhou H., Bernhard E. J., Fox F. E., Billings P. C. Induction of metalloproteinase activity in human T-lymphocytes. Biochemical et Biophysica Acta 1993; 11: 174–178
   Web of Science ®Google Scholar
• Schultze J. L., Seamon M. J., Michalak S., Gribben J. G., Nadler L. M. Autologous tumor infiltrating T cells cytotoxic for follicular lymphoma cells can be expanded in vitro. Blood 1997; 89: 3806–3816
   PubMed Web of Science ®Google Scholar
• Brew K., Dinakarpandian D., Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochimica et Biophysica Acta 2000; 1477: 267–283
   PubMed Web of Science ®Google Scholar
• Blavier L., Henriet P., Imren S., Declerck Y. A. Tissue inhibitors of matrix metalloproteinases in cancer. Annals of the New York Academy of Sciences 1999; 878: 108–119
   PubMed Web of Science ®Google Scholar
• Gomez D. E., Alonso D. F., Yoshiji H., Thorgeirsson U. P. Tissue inhibitors of metalloproteinases: structure. regulation and biological functions. European Journal of Cell Biology 1997; 74: 111–122
   PubMed Web of Science ®Google Scholar
• Bode W., Fernandez-Catalan C., Grams F., Gormis-Ruth F. X., Nagase H., Tschesche H., Maskos K. Insights into MMP-TIMP interactions. Annals of the New York Academy of Sciences 1999; 878: 73–91
   PubMed Web of Science ®Google Scholar
• Baker A. H., George S. J., Zaltsman A. B., Murphy G., Newby A. C. Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. British Journal of Cancer 1999; 79: 1347–1355
   PubMed Web of Science ®Google Scholar
• Henriet P., Blavier L., Declerck Y. A. Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation. APMIS 1999; 107: 111–119
   PubMed Web of Science ®Google Scholar
• Kruger A., Fata J. E., Khokha R. Altered tumor growth and metastasis of a T cell lymphoma in TIMP-I transgenic mice. Blood 1997; 90: 1993–2000
   PubMed Web of Science ®Google Scholar
• Hayakawa T., Yamashita K., Tanzawa E., Uchijima E., Iwata K. Growth-promoting activity of tissue inhibitor of metalloproteinase-I (TIMP-I) for a wide range of cells. A possible new growth factor in serum. FEBS Letters 1992; 298: 29–32
   PubMed Web of Science ®Google Scholar
• Li G., Fridman R., Kim H. R. Tissue inhibitor of metalloproteinase-I inhibits apoptosis of human breast epithelial cells. Cancer Research 1999; 59: 6267–6275
   PubMed Web of Science ®Google Scholar
• Guedez L., Courtemanch L., Stetler-Stevenson M. Tissue inhibitor of metalloproteinase (TIMP-I) induces differentiation and an antiapoptotic phenotype in germinal center B cells. Blood 1998; 92: 1342–1349
   PubMed Web of Science ®Google Scholar
• Uchijima M., Sato H., Fujii M., Seiki M. Tax proteins of human T-cell leukemia virus type 1 and 2 induce expression of the gene encoding erythroid-potentiating activity (tissue inhibitor of metalloproteinases-I, TIMP-I). Journal of Biological Chemistry 1994; 269: 14946–14950
   PubMed Web of Science ®Google Scholar
• Holten-Andersen G., Murphy M. N., Nielsen H. J., Pedersen A. N., Christensen Hoyer I. J., Hansen G., Brunner N., Stephens R. W. Quantitation of TIMP-I in plasma of healthy blood donors and patients with advanced cancer. British Journal of Cancer 1999; 80: 495–503
   PubMed Web of Science ®Google Scholar
• McCarthy K., Maguire T., McGreal G., McDermott E., O'Higgins N., Duffy M. J. High levels of tissue inhibitor of metalloproteinase-I predict poor outcome in patients with breast cancer. International Journal of Cancer 1999; 84: 44–48
   PubMed Web of Science ®Google Scholar
• Fong K. M., Kida Y., Zimmerman P. V., Smith P. J. TIMP-I and adverse prognosis in non-small cell lung cancer. Clinical Cancer Research 1996; 2: 1369–1372
   PubMed Web of Science ®Google Scholar
• Guedez L., Stetler-Stevenson W. G., Wolff L., Wang J., Fukushima P., Mansoor A., Stetler-Stevenson M. In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1. Journal of Clinical Investigation 1998; 102: 2002–2010
   PubMed Web of Science ®Google Scholar
• Mansoor A., Birkedal-Hansen B., Lim M. S., Guedez L., Stetler-Stevenson W. G., Stetler-Stevenson M. TIMP-I expression correlates with histologic grade in B-cell lymphomas. Modern Pathology 1997; 10: 130A
   Google Scholar
• Kossakowska A. E., Urbanski S. J., Edwards D. R. Tissue inhibitor of metalloproteinases-1 (TIMP-I) RNA is expressed at elevated levels in malignant non-Hodg-kin's lymphomas. Blood 1991; 77: 2475–2481
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Zhang M.-L., Ch, Brasher P., Urbanski S. J., Edwards D. R. TIMP-I is a predictor of survival in human non-Hodgkin's lymphomas. Modern Pathology 1999; 12: 140A
   Google Scholar
• Hayakawa T., Yamashita K., Ohuchi E., Shinagawa A. Cell growth-promoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2). Journal of Cell Science 1994; 107: 2373–2379
   PubMed Web of Science ®Google Scholar
• Nemeth J. A., Rafe A., Steiner M., Goolsby C. L. TIMP-2 growth-stimulatory activity: a concentration-and cell type-specific response in the presence of insulin. Experimental Cell Research 1996; 224: 110–115
   PubMed Web of Science ®Google Scholar
• Valente P, Fassina G, Melchiori A, Masiello L, Cilli M., Vacca A., Onisto M., Santi L., Stetler-Stevenson W. G., Albini A. TIMP-2 over-expression reduces invasion mid angiogenesis and protects B1610 melanoma cells from apoptosis. International Journal of Cancer 1998; 75: 246–253
   PubMed Web of Science ®Google Scholar
• Lim M. S., Guedez L., Stetler-Stevenson W. G., Staler-Stetler-Stevenson M. Tissue inhibitor of metalloproteinase-2 induces apoptosis in human T lymphocytes. Annals of the New-York Academy of Sciences 1999; 878: 522–523
   PubMed Web of Science ®Google Scholar
• Murphy G., Reynolds J. J. Extracellular matrix degradation. In Connective Tissue and its Heritable Disorders, P. M. Royce, B. Steinmann. Wiley-Liss. Inc., New York 1993; 287
   Google Scholar
• Leppert D., Waubant E., Galardy R., Bunnett N. W., Hauser S. L. T cell gelatinizes mediate basement membrane transmigration in vitro. Journal of immunology 1995; 156: 4379–4389
   Google Scholar
• Xia M., Leppert D., Hauser S. L., Sreedharan S. P., Nelson P. J., Krensky A. M., Goetzl E. J. Stimulus specificity of matrix metalloproteinase dependence of human T cell migration through a model basement membrane. Journal of Immunology 1996; 156: 160–167
   PubMed Web of Science ®Google Scholar
• Romanic A. M., Madri J. A. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. Journal of Cell Biology. 1994; 125: 1165–1178
   PubMed Web of Science ®Google Scholar
• Khan K. M. F., Falcone D. J. Role of laminin in matrix induction of macrophage urokinase-type plasminogen activator and 92-kDa metalloproteinase expression. Journal of Biology Chemistry 1997; 272: 8270–8275
   PubMed Web of Science ®Google Scholar
• Madri J. A., Graesser D., Haas T. The roles of adhesion molecules and proteinases in lymphocyte transendothelial migration. Biochemistry and Cell Biology 1996; 74: 749–757
   PubMed Web of Science ®Google Scholar
• Sato T, Ito A., Ogata Y., Nagase H., Mori Y. Tumor necrosis factor alpha (TNF alpha) induces pro-matrix metalloproteinase-9 production in human uterine cervical fibroblasts but interleukin I alpha antagonizes the inductive effect of TNF alpha. FEBS Letter 1996; 392: 175–178
   PubMed Web of Science ®Google Scholar
• Kurogi T., Nabeshima K., Kataoka Y., Okada Y., Koono O. M. Stimulation of gelatinase B and tissueinhibitors of metalloproteinase (TIMP) production in coculture of human osteosarcoma cells and human fibroblasts: gelatinase B production was stimulated via upregulation of fibroblasts growth factor (FGF) receptor. International Journal of Cancer 1996; 66: 82–90
   PubMed Web of Science ®Google Scholar
• Saren P., Welgus H. G., Kovanen P. T. TNF-alpha and lL-ibeta selectively induce expression of 92 kDa Gelatinase by human macrophages. Journal of Immunology 1996; 157: 4159–4165
   PubMed Web of Science ®Google Scholar
• Johnatty R. N., Taub D. D., Reeder S. P., Turcovshi-Corrales S. M., Cottam D. W., Stephenson T. J., Rees R. C. Cytokine and chemokine regulation of proMMP-9 and TIMP-I production by human peripheral blood lymphocytes. Journal of Immunology 1997; 158: 2327–2333
   PubMed Web of Science ®Google Scholar
• Stüve O., Dooley N. P., Uhm J. H., Antel J. P., Francis G. S., Williams G., Yong V. W. Interferon beta-lb decreases the migration of T lymphocytes vitro: effects on matrix metalloproteinase-9. Annals of Neurology 1996; 40: 853–869
   PubMed Web of Science ®Google Scholar
• Yoshizaki T., Sato H., Furukawa M., Pagano J S. The expression of matrix metalloproteinase 9 is enhanced by Epstein-Barr virus latent membrane protein I. proceedings of the National Academy of Sciences of the United States of America 1998; 95: 3621–36268
   PubMed Web of Science ®Google Scholar
• Mertz P. M., De Witt D. L., Stetler-Stevenson W. G., Wahl L. M. Interlcukin 10 suppression of monocyte prostaglandin H synthase-2. Mechanism of inhibition of Prostaglandin-dependent matrix metalloproteinase production. Journal of Biology Chemistry 1994; 269: 21322–21329
   PubMed Web of Science ®Google Scholar
• Wahl L. M., Coreoran M. L. Regulation of monocyte/macrophage metalloproteinase production by cytokines. Journal of Periodontology 1993; 64: 467–473
   PubMed Web of Science ®Google Scholar
• Lacraz S., Nicod L., Chicheportiche R., Welgus H., Dayer J. M. IL-10 inhibits metalloproteinases and stimulates TIMP-I production in human mononuclear phagocytes. Journal of Clinical Investigation 1995; 98: 2304–2310
   Web of Science ®Google Scholar
• Sato T., Ito A., Mori Y. Interleukin 6 enhances the production of tissue inhibitor of metalloproteinases (TIMP) but not that of matrix metalloproteinases by human fibroblasts. Biochemistry and Biophysical Research Communications 1990; 170: 824–829
   PubMed Web of Science ®Google Scholar
• Kossakowska A. E., Edwards D. R., Prusinkiewiez C., Zhang M. C., Guo D., Urbanski S. J., Grogan T. S., Marquez L. A., Janowska-Wiezorek A. Interleukin-6 regulation of matrix metalloproteinase (MMP-2 and MMP-9) and tissue inhibitor of metalloprotcinase (TIMP-1) expression in malignant non-Hodgkin's lymphomas. Blood 1999; 94: 2080–2089
   PubMed Web of Science ®Google Scholar
• Seymour J. F., Talpaz M., Cabanillas F., Wetzler M., Kurzock R. Serum interleukin-6 levels correlate with prognosis in diffuse large cell lymphoma. Journal of Clinical Oncology 1995; 13: 575–582
   PubMed Web of Science ®Google Scholar
• Blay J. Y., Burdin N., Rousset F., Lenoir G., Biron P., Philip T., Banchereau J., Favrot M. C. Serum interleukin- 10 in lion-Hodgkin's lymphoma: a prognostic factor. Blood 1993; 82: 2169–2174
   PubMed Web of Science ®Google Scholar
• Cortes J., Kurzrock R. Interlcukin-10 in non-Hodgkin's lymphoma [Review]. Leukemia and Lymphoma 1997; 26: 251–259
   PubMed Web of Science ®Google Scholar
• Voorzanger N., Toituou R., Gareia E., Delecluse H. J., Roussel F., Joab I., Favrot M., Blay J. Y. Interleukin (IL)-10 and IL-6 are produced in vivo in non-Hodgkin's lymphoma cells and act as cooperative growth factors. Cancer Research 1996; 56: 5499–5505
   PubMed Web of Science ®Google Scholar
• Emilie D., Coumbaras J., Raphael M., Devergne O., Delecluse H. J., Gisselbrecht C., Michiels J. F., Van Damme J., Taga T., Kishimoto T., Crevon M. C., Galanaud P. Interleukin-6 production in high-grade B lymphomas: correlation with the presence of malignant immunoblasts in acquired immunodeficiency syndrome and in human immunodeficiency virus-seronegative patients. Blood 1992; 80: 498–504
   PubMed Web of Science ®Google Scholar