Delta9-tetrahydrocannabinol selectively increases aspartyl cathepsin D proteolytic activity and impairs lysozyme processing by macrophages

International Journal of Immunopharmacology

Volumn 22, Issue 5, 2000, Pages 373-381

  Matveyeva, Marina ^a   Hartmann, Constance B ^a   Harrison, M Travis ^a   Cabral, Guy A ^a   McCoy, Kathleen L ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Antigen processing; Cathepsin; Delta9 tetrahydrocannabinol; Immunosuppression; Macrophage function; T cell activation

Indexed keywords

CATHEPSIN D; DRONABINOL; LYSOZYME; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MEMBRANE ANTIGEN;

ANIMAL CELL; ANTIGEN PRESENTATION; ANTIGEN PRESENTING CELL; ARTICLE; DISULFIDE BOND; DRUG EFFECT; HYBRIDOMA; IMMUNOMODULATION; MACROPHAGE; MACROPHAGE ACTIVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; T LYMPHOCYTE ACTIVATION;

ANIMALS; ANTIGEN PRESENTATION; CATHEPSIN D; CELLS, CULTURED; HISTOCOMPATIBILITY ANTIGENS CLASS II; MACROPHAGES; MICE; MURAMIDASE; T-LYMPHOCYTES; TETRAHYDROCANNABINOL;

EID: 0034191882     PISSN: 01920561     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0192-0561(99)00092-2     Document Type: Article

References (48)

1. Lopez-Cepero M., Friedman M., Klein T., Friedman H. Tetrahydrocannabinol-induced suppression of macrophage spreading and phagocytic activity in vitro. J. Leukoc. Biol. 39:1986;679-686.
2. 9-tetrahydrocannabinol. J. Leukoc. Biol. 50:1991;423-426.
3. Burnette-Curley D., Marciano-Cabral F., Fischer-Stenger K., Cabral G.A. Delta-9-tetrahydrocannabinol inhibits cell contact-dependent cytotoxicity of bacillus Calmétte-Guérin-activated macrophages. Int. J. Immunopharmacol. 15:1993;371-382.
4. Coffey R.G., Yamamoto Y., Snella E., Pross S. Tetrahydrocannabinol inhibition of macrophage nitric oxide production. Biochem. Pharmacol. 52:1996;743-751.
5. 9-tetrahydrocannabinol is mediated through the inhibition of nuclear factor-κ B/Rel activation. Mol. Pharmacol. 50:1996;334-341.
6. 9-tetrahydrocannabinol suppresses macrophage costimulation by decreasing heat-stable antigen expression. Int. J. Immunopharmacol. 20:1998;415-428.
7. Klein T.W., Friedman H., Specter S. Marijuana, immunity and infection. J. Neuroimmunol. 83:1998;102-115.
8. Newton C., Klein T., Friedman H. The role of macrophages in THC-induced alteration of the cytokine network. Adv. Exp. Med. Biol. 437:1998;207-214.
9. 9-Tetrahydrocannabinol inhibition of tumor necrosis factor-α: suppression of post-translational events. J. Pharmacol. Exp. Ther. 267:1993;1558-1565.
10. Zheng Z.-M., Specter S., Friedman H. Inhibition by delta-9-tetrahydrocannabinol of tumor necrosis factor alpha production by mouse and human macrophages. Int. J. Immunopharmacol. 14:1992;1445-1452.
11. Maffei A., Harris P.E. Peptides bound to major histocompatiblity complex molecules. Peptides. 19:1998;179-198.
12. Cresswell P., Howard J.C. Antigen recognition. Curr. Opin. Immunol. 9:1997;71-74.
13. Geuze H.J. The role of endosomes and lysosomes in MHC class II functioning. Immunol. Today. 19:1998;282-287.
14. Bohley P., Seglan P.O. Proteases and proteolysis in lysosomes. Experientia. 48:1992;151-157.
15. van der Drift A.C.M., van Noort J.M., Kruse J. Catheptic processing of protein antigens: enzymatic and molecular aspects. Semin. Immunol. 2:1990;255-271.
16. Katunuma N., Matsunaga Y., Saibara T. Mechanism and regulation of antigen processing by cathepsin B. Adv. Enzyme Regul. 34:1994;145-158.
17. Frosch S., Bonifas U., Reske-Kunz A. The capacity of bone-marrow-derived macrophages to process bovine insulin is regulated by lymphokines. Int. Immunol. 5:1993;1551-1558.
18. Vidard L., Rock K.L., Benacerraf B. Diversity in MHC class II ovalbumin T cell epitopes generated by distinct proteases. J. Immunol. 149:1992;498-504.
19. Rodriguez G.M., Diment S. Destructive proteolysis by cysteine proteases in antigen presentation of ovalbumin. Eur. J. Immunol. 25:1995;1823-1827.
20. Collins D.S., Unanue E.R., Harding C.V. Reduction of disulfide bonds within lysosomes is a key step in antigen processing. J. Immunol. 147:1991;4054-4059.
21. Merkel B.J., Mandel R., Ryser H.J.-P., McCoy K.L. Characterization of fibroblasts with a unique defect in processing antigens with disulfide bonds. J. Immunol. 154:1995;128-136.
22. Kooistra T., Millard P.C., Lloyd J.B. Role of thiols in degradation of proteins by cathepsins. Biochem. J. 204:1982;471-477.
23. Mego J.L. Role of thiols, pH, and cathepsin D in the lysosomal catabolism of serum albumin. Biochem. J. 218:1984;775-783.
24. Nakagawa T., Roth W., Wong P., Nelson A., Farr A., et al. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science. 280:1998;450-453.
25. Nakagawa T., Brissette W.H., Lira P.D., Griffiths R.J., Petrushova N., et al. Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. Immunity. 10:1999;207-217.
26. Deussing J., Roth W., Saftig P., Peters C., Ploegh H.L., et al. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA. 95:1998;4516-4521.
27. 9-Tetrahydrocannabinol modulates antigen processing by macrophages. J. Pharmacol. Exp. Ther. 273:1995;1216-1223.
28. McCoy K.L., Matveyeva M., Carlisle S.J., Cabral G.A. Cannabinoid inhibition of the processing of intact lysozyme by macrophages: evidence for CB2 receptor participation. J. Pharmacol. Exp. Ther. 289:1999;1620-1625.
29. Takahashi T., Tang J. Cathepsin D from porcine and bovine spleen. Meth. Enzymol. 80:1981;565-581.
30. Kageyama T. Procathepsin E and cathepsin E. Meth. Enzymol. 248:1995;120-136.
31. Barrett A.J., Kirschke H. Cathepsin B, cathepsin H, and cathepsin L. Meth. Enzymol. 80:1981;535-561.
32. Short S., Merkel B.J., Caffrey R., McCoy K.L. Defective antigen processing correlates with a low level of intracellular glutathione. Eur. J. Immunol. 26:1996;3015-3020.
33. Singer D.F., Linderman J.J. The relationship between antigen concentration, antigen internalization, and antigenic complexes: modeling insights into antigen processing and presentation. J. Cell Biol. 111:1990;55-68.
34. van Noort J.M., Jacobs M.J.M. Cathepsin D, but not cathepsin B, releases T cell stimulatory fragments from lysozyme that are functional in the context of multiple murine class II MHC molecules. Eur. J. Immunol. 24:1994;2175-2180.
35. Lah T.T., Hawley M., Rock K.L., Goldberg A.L. Gamma-interferon causes a selective induction of lysosomal proteases, cathepsins B and L, in macrophages. FEBS Lett. 363:1995;85-89.
36. Lafuse W.P., Brown D., Castle L., Zwilling B.S. IFN-γ increases cathepsin H mRNA levels in mouse macrophages. J. Leukoc. Biol. 57:1995;663-669.
37. Rossman M.D., Maida B.T., Douglas S.D. Monocyte-derived macrophage and alveolar macrophage fibronectin production and cathepsin D activity. Cell Immunol. 126:1990;268-277.
38. Li Q., Falker W.A. Jr, Bever C.T. Jr. Endotoxin induces increased intracellular cathepsin B activity in THP-1 cells. Immunopharmacol. Immunotoxicol. 19:1997;3215-3237.
39. Matsuda L.A. Molecular aspects of cannabinoid receptors. Crit. Rev. Neurobiol. 11:1997;143-166.
40. 2 receptors. Pharmacol. Ther. 74:1997;129-180.
41. Bayewitch M., Avidor-Reiss T., Levy R., Barg J., Mechoulam R. The peripheral cannabinoid receptor: adenylate cyclase inhibition and G-protein coupling. FEBS Lett. 375:1995;143-147.
42. Schatz A.R., Lee M., Condie R.B., Pulaski J.T., Kaminski N.E. Cannabinoid receptors CB1 and CB2: a characterization of expression and adenylate cyclase modulation within the immune system. Toxicol. Appl. Pharmacol. 142:1997;278-287.
43. Childers S.R., Deadwyler S.A. Role of cyclic AMP in the actions of cannabinoid receptors. Biochem. Pharmacol. 52:1996;819-827.
44. Felder C.C., Joyce K.E., Briley E.M., Mansouri J., Mackie K., et al. Comparison of the pharmacology and signal transduction of the human cannabinoid CB1 and CB2 receptors. Mol. Pharmacol. 48:1995;443-450.
45. Howlett A.C. Pharmacology of cannabinoid receptors. Annu. Rev. Pharmacol. Toxicol. 35:1995;607-634.
46. Jbilo O., Derocq J.M., Segui M., Le Fur G., Casellas P. Stimulation of peripheral cannabinoid receptor CB2 induces MCP-1 and IL-8 gene expression in human promyelocytic cell line HL60. FEBS Lett. 448:1999;273-277.
47. 9-Tetrahydrocannabinol enhances the secretion of interleukin 1 from endotoxin-stimulated macrophages. J. Pharmacol. Exp. Ther. 270:1994;1334-1339.
48. Burstein S., Budrow J., Debatis M., Hunter S.A. Phospholipase participation in cannabinoid-induced release of free arachidonic acid. Biochem. Pharamacol. 48:1994;1253-1264.