Glatiramer acetate blocks the activation of THP-1 cells by interferon- γ

European Journal of Pharmacology

Volumn 342, Issue 2-3, 1998, Pages 303-310

  Li, Qingdi ^a,b,c   Milo, Ron ^a,c   Panitch, Hillel ^a,c   Swoveland, Peggy ^a,c   Bever Jr , Christopher T ^a,c  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MARYLAND DENTAL SCHOOL   (United States)

^c BALTIMORE VA MEDICAL CENTER   (United States)

Author keywords

Cathepsin B; Cytokine; Glatiramer acetate; HLA Class II; Multiple sclerosis; THP 1 cells

Indexed keywords

CATHEPSIN B; GAMMA INTERFERON; GLATIRAMER; HLA DQ ANTIGEN; HLA DR ANTIGEN; INTERLEUKIN 1; INTERLEUKIN 1BETA; LEUKOCYTE ANTIGEN; LIPOPOLYSACCHARIDE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; TUMOR NECROSIS FACTOR ALPHA;

ARTICLE; BINDING SITE; CHILD; CONTROLLED STUDY; CYTOKINE PRODUCTION; DOSE RESPONSE; FLOW CYTOMETRY; FLUORESCENCE; HUMAN; HUMAN CELL; LYMPHOCYTE ACTIVATION; MACROPHAGE; MULTIPLE SCLEROSIS; PRIORITY JOURNAL; T LYMPHOCYTE;

CATHEPSIN B; CELL LINE; CYTOKINES; FLOW CYTOMETRY; GENE EXPRESSION REGULATION; GENES, MHC CLASS II; HLA-DQ ANTIGENS; HLA-DR ANTIGENS; HUMANS; IMMUNOSUPPRESSIVE AGENTS; INTERFERON-GAMMA, RECOMBINANT; LYMPHOCYTE ACTIVATION; MULTIPLE SCLEROSIS; PEPTIDES; T-LYMPHOCYTES;

EID: 0032567802     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(97)01509-4     Document Type: Article

References (53)

1. Adams, D.O., Hamilton, T.A., 1992. Molecular basis of macrophage activation: Diversity and its origins. In: Lewis, L.E., McGee, J.O.'D. (Eds.), The Macrophage: The Natural Immune System. IRL Press, Oxford, pp. 75-105.
2. Aharoni R., Teitelbaum D., Arnon R. T suppressor hybridomas and interleukin-2-dependent lines induced by copolymer 1 or by spinal cord homogenate down-regulate experimental allergic encephalomyelitis. Eur. J. Immunol. 23:1993;17-25.
3. Arenzana-Seisdedos F., Mogensen S., Vuillier F. Autocrine secretion of tumor necrosis factor under the influence of interferon-γ amplifies HLA-DR gene induction in human monocytes. Proc. Natl. Acad. Sci. USA. 85:1988;6087-6091.
4. Arnon, R., Teitelbaum, D., 1988. Suppression of demyelinating disease by synthetic copolymers. In: Serlupi-Crescenzi, G. (Ed.), A Multidisciplinary Approach to Myelin Disease. Plenum Press, New York, pp. 234-250.
5. Auwerx J. The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation. Experimentia. 47:1991;22-30.
6. Barrett A.J., Kirschke H. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80:1981;535-561.
7. Bever C.T. Cathepsin B in peripheral blood mononuclear cells of multiple sclerosis patients. Trans. Am. Soc. Neurochem. 22:1991;208.
8. Bever C.T., Garver D.W. Increased cathepsin B activity in multiple sclerosis lesions. Trans. Am. Soc. Neurochem. 23:1992;214.
9. Bever C.T., Garver D.W. Cathepsin B activity in multiple sclerosis lesions: Cellular origins. Neurochem. Int. 21 (Suppl.):1992;C18.
10. Bever C.T., Garver D.W. Increased cathepsin B activity in multiple sclerosis brain. J. Neurol. Sci. 131:1995;71-73.
11. Bever C.T., Snyder D.S., Endres R.O., Morgan K.D., Postlethwaite A., Whitaker J.N. Activation of astrocytic lysosomal proteinases by factors released by mononuclear leukocytes. Neurochem. Res. 14:1989;37-41.
12. Bever C.T., Panitch H.S., Johnson K.P. Increased cathepsin B activity in peripheral blood mononuclear cells of multiple sclerosis patients. Neurology. 44:1994;745-748.
13. Brosnan C.F., Litwak M., Neighbour P.A., Lyman W.D., Carter T.H., Bornstein M.B., Bloom B.R. Immunogenic potentials of copolymer I in normal human lymphocytes. Neurology. 35:1985;1754-1759.
14. Cardozo C., Kurtz C., Lesser M. Degradation of rat lung collagens by cathepsin B. J. Lab. Clin. Med. 119:1992;169-175.
15. Chang R.J., Lee S.H. Effects of interferon-γ and tumor necrosis factor-α on the expression of an Ia antigen on a murine macrophage cell line. J. Immunol. 137:1986;2853-2856.
16. Cieri M., Bever C.T. Gamma interferon induced increases in cathepsin B activity are blocked by alpha and beta interferons (Type I interferon). FASEB J. 4:1990;A339.
17. Daibata M., Xu M., Humphreys R.E., Reyes V.E. More efficient peptide binding to MHC class II molecules during cathepsin B digestion of Ii than after Ii release. Mol. Immunol. 31:1994;255-260.
18. Durum, S.C., Oppenheim, J.J., 1989. Macrophage-derived mediators: Interleukin 1, tumor necrosis factor, interleukin 6, and related cytokines. In: Paul, W. (Ed.), Fundamental Immunology. Raven Press, New York, pp. 639-661.
19. Fisher M., Levine P.H., Weiner B.H. Monocyte and polymorphonuclear leukocyte toxic oxygen metabolite production in multiple sclerosis. Inflammation. 12:1988;123-131.
20. Hofman F.M., Hinton D.R., Johnson K. Tumor necrosis factor identified in multiple sclerosis brain. J. Exp. Med. 170:1989;607-612.
21. Johnson W.J., Kelley A., Connor J.R. Inhibition of IFN-γ-induced Ia antigen expression on synovial fibroblasts by IL-1. J. Immunol. 143:1989;1614-1618.
22. Johnson K.P., Brooks B.R., Cohen J.A. Copolymer 1 reduces relapse rate and improves disability in relapsing-remitting multiple sclerosis: Results of a phase III multicenter, double-blind, placebo-controlled trial. Neurology. 45:1995;1268-1276.
23. Keith A.B., Arnon R., Teitelbaum D. The effect of Cop1, a synthetic polypeptide, on chronic relapsing experimental allergic encephalomyelitis in guinea pigs. J. Neurol. Sci. 42:1979;267-274.
24. Li Q., Bever C.T. Gamma interferon induced increases in intracellular cathepsin B activity in PMA primed THP-1 cells are blocked by inhibitors of protein kinase C. Immunopharmacol. Immunotoxicol. 18:1996;375-396.
25. Li Q., Milo R., Bever C.T., Swoveland P., Panitch H. Protein kinase C regulates HLA class II molecule expressions and TNF-α production in THP-1 cells. FASEB J. 8:1994;A506.
26. Li Q., Falkler W.A., Bever C.T. Endotoxin induces increased intracellular cathepsin B activity in THP-1 cells. Immunopharmacol. Immunotoxicol. 19:1997;215-237.
27. Maciewicz R.A., Wotton S.F. Degradation of cartilage matrix components by the cysteine proteinases, Cathepsin B and L. Biomed. Biochim. Acta. 50:1991;561-564.
28. Martin R., Jaraquemada D., Flerlage M. Fine specificity and HLA restriction of myelin basic protein-specific cytotoxic T cell lines from mutiple sclerosis patients and healthy individuals. J. Immunol. 145:1990;540-548.
29. Matsunaga Y., Saibara T., Kido H., Katunuma N. Participation of cathepsin B in processing of antigen presentation to MHC class II. FEBS Lett. 324:1993;325-330.
30. Merrill J.E., Strom S.R., Ellison G.W. In vitro study of mediators of inflammation in multiple sclerosis. J. Clin. Immunol. 9:1989;84-96.
31. Milo R., Panitch H. Additive effects of copolymer-1 and interferon β-1b on the immune response to myelin basic protein. J. Neuroimmunol. 61:1995;185-193.
32. Mizuochi T., Yee S.T., Kasai M., Kakiuchi T., Muno D., Kominami E. Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant Chain. Immunol. Lett. 43:1994;189-193.
33. Old L.J. Polypeptide mediator network. Nature. 326:1987;330-331.
34. Ota K., Matsui M., Milford E.L. T-cell recognition of an immunodominant myelin basic protein epitope in multiple sclerosis. Nature. 346:1990;183-187.
35. Pette M., Fujita K., Wilkinson D. Myelin autoreactivity in multiple sclerosis: Recognition of myelin-basic protein in the context of HLA-DR2 products by T lymphocytes of multiple-sclerosis patients and healthy donors. Proc. Natl. Acad. Sci. USA. 87:1990;7968-7972.
36. Prineas J.W., Graham J.S. Multiple Sclerosis: Capping of surface immunoglobulin G on macrophages engaged in myelin breakdown. Ann. Neurol. 10:1981;149-158.
37. Racke M.K., Martin R., McFarland H. Copolymer-1 induced inhibition of antigen-specific T cell activation: Interference with antigen presentation. J. Neuroimmunol. 37:1992;75-84.
38. Reyes V.E., Lu S., Humphreys R.E. Cathepsin B cleavage of Ii from class II MHC alpha- and beta-chains. J. Immunol. 146:1991;3877-3880.
39. Rietschel E.T., Brade H. Bacterial endotoxins. Sci. Am. 267:1992;54.
40. Roche P.A., Cresswell P. Proteolysis of the class II associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc. Natl. Acad. Sci. USA. 88:1991;3150-3154.
41. Rosbo de Kerlero N., Mendel I., Milo R., Flechter S., Ben-Nun A. The autoimmune response to myelin oligodendrocyte glycoprotein (MOG) in multiple sclerosis and MOG-induced experimental autoimmune encephalomyelitis: Effect of copolymer-1. Eur. J. Neurol. 3 (Suppl. 4):1996;57-58.
42. Sela M., Arnon R., Teitelbaum D. Suppressive activity of Cop-1 in EAE and its relevance to multiple sclerosis. Bull. Inst. Pasteur (Paris). 88:1990;303-314.
43. Selmaj K.W., Raine C.S. Tumor necrosis factor mediates myelin and oligodendrocyte damage in vitro. Ann. Neurol. 23:1988;339-346.
44. Selmaj K.W., Farooq M., Norton W.T. Proliferation of astrocytes in vitro in response to cytokines: A primary role for tumor necrosis factor. J. Immunol. 144:1990;129-135.
45. Smith M.E., McFarlin D.E., Dhib-Jalbut S. Differential effect of interleukin-1β on Ia expression in astrocytes and microglia. J. Neuroimmunol. 46:1993;97-104.
46. + current expression in cultured oligodendrocytes. J. Membr. Biol. 124:1991;127-137.
47. Teitelbaum D., Meshorer A., Hirshfeld T. Suppression of experimental allergic encephalomyelitis by a synthetic polypeptide. Eur. J. Immunol. 1:1971;242-248.
48. Teitelbaum D., Milo R., Arnon R. Synthetic copolymer 1 inhibits human T-cell lines specific for myelin basic protein. Proc. Natl. Acad. Sci. USA. 89:1992;137-141.
49. Teitelbaum D., Fridkis-Hareli M., Arnon R., Sela M. Copolymer 1 inhibits chronic relapsing experimental allergic encephalomyelitis induced by proteolipid protein (PLP) peptides in mice and interferes with PLP-specific T cell responses. J. Neuroimmunol. 64:1996;209-217.
50. Traugott U., Reinherz E.L., Raine C.S. Multiple sclerosis distribution of T cells, T cell subsets and Ia-positive macrophages in lesions of different ages. J. Neuroimmunol. 4:1983;201-221.
51. Tsuchiya S., Yamabe M., Yamaguchi Y., Kobayashi Y., Konno T., Tada K. Establishment and characterization of a human acute monocytic leukemia cell line (THP-1). Int. J. Cancer. 26:1980;171-176.
52. Unanue E.R., Beller D.I., Lu C.Y. Antigen presentation: Comments on its regulation and mechanism. J. Immunol. 132:1984;1-4.
53. Yanagisawa K., Sato S., Miyatake T., Kominami E., Katsunuma N. Degradation of myelin protein by cathepsin B and inhibition by E-64 analogue. Neurochem. Res. 9:1984;691-694.