Rosmarinic acid inhibits TCR-induced T cell activation and proliferation in an Lck-dependent manner

European Journal of Immunology

Volumn 33, Issue 4, 2003, Pages 870-879

  Won, Jonghwa ^a   Hur, Yun Gyoung ^a   Hur, Eun Mi ^a   Park, See Hyoung ^a   Kang, Mi Ae ^a   Choi, Youngbong ^a   Park, Changwon ^a   Lee, Keun Hyeung ^a,b   Yun, Yungdae ^a,c  

^a Mogam Biotechnology Research Institute   (South Korea)

^b Inha University   (South Korea)

^c Ewha Womans University   (South Korea)

Author keywords

Lck; Rosmarinic acid; Src homology 2; TCR signaling

Indexed keywords

4 O METHYLPHORBOL 13 ACETATE 12 MYRISTATE; CALCIUM ION; CYCLOSPORIN A; GAMMA INTERFERON; INTERLEUKIN 2; IONOMYCIN; PROTEIN TYROSINE KINASE; ROSMARINIC ACID; T LYMPHOCYTE RECEPTOR;

ARTICLE; CALCIUM MOBILIZATION; CELL PROLIFERATION; CONSENSUS SEQUENCE; CONTROLLED STUDY; DRUG MECHANISM; DRUG SCREENING; DRUG SPECIFICITY; DRUG STRUCTURE; HUMAN; HUMAN CELL; IC 50; IMMUNOSUPPRESSIVE TREATMENT; LYMPHOCYTE MEMBRANE; LYMPHOCYTE PROLIFERATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION; SPLEEN CELL; SRC HOMOLOGY DOMAIN; T LYMPHOCYTE ACTIVATION;

CALCIUM; CELLS, CULTURED; CINNAMATES; CYTOKINES; DEPSIDES; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; INTERLEUKIN-2; ION TRANSPORT; JURKAT CELLS; LYMPHOCYTE ACTIVATION; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); PHOSPHOPEPTIDES; PHOSPHORYLATION; PROMOTER REGIONS (GENETICS); PROTEIN-TYROSINE KINASES; RECEPTORS, ANTIGEN, T-CELL; SPLEEN; SRC HOMOLOGY DOMAINS; SURFACE PLASMON RESONANCE; T-LYMPHOCYTES; TRANS-ACTIVATION (GENETICS); ZAP-70 PROTEIN-TYROSINE KINASE;

EID: 0038068134     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200323010     Document Type: Article

References (38)

1. Gupta, S., Weiss, A., Kumar, G., Wang, S. and Nel, A., The T cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase. Evidence for the existence of a second protein kinase C-dependent pathway in an Lck-negative Jurkat cell mutant. J. Biol. Chem. 1994. 269: 17349-17357.
2. Goldsmith, M. A. and Weiss, A., Isolation and characterization of a T-lymphocyte somatic mutant with altered signal transduction by the antigen receptor. Proc. Natl. Acad. Sci. USA 1987. 84: 6879-6883.
3. Straus, D. B. and Weiss, A., Genetic evidence for the involvement of the Ick tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 1992. 70: 585-593.
4. Molina, T. J., Kishihara, K., Siderovski, D. P., van Ewijk, W., Narendran, A., Timms, E., Wakeham, A., Paige, C. J., Hartmann, K. U., Veillette, A. and et al., Profound block in thymocyte development in mice lacking p56lck. Nature 1992. 357: 161-164.
5. Lewis, L. A., Chung, C. D., Chen, J., Parnes, J. R., Moran, M., Patel, V. P. and Miceli, M. C., The Lck SH2 phosphotyrosine binding site is critical for efficient TCR- induced processive tyrosine phosphorylation of the zeta-chain and IL-2 production. J. Immunol. 1997. 159: 2292-2300.
6. Xu, H. and Littman, D. R., A kinase-independent function of Lck in potentiating antigen-specific T cell activation. Cell 1993. 74: 633-643.
7. Straus, D. B., Chan, A. C., Patai, B. and Weiss, A., SH2 domain function is essential for the role of the Lck tyrosine kinase in T cell receptor signal transduction. J. Biol. Chem. 1996. 271: 9976-9981.
8. Pawson, T., Protein modules and signalling networks. Nature 1995. 373: 573-580.
9. Songyang, Z., Shoelson, S. E., Chaudhuri, M., et al., SH2 domains recognize specific phosphopeptide sequences. Cell 1993. 72: 767-778.
10. Kim, J., Hur EM and Yun, Y., Establishment of a binding assay system for screening of the inhibitors of p56Lck SH2 domain. J. Biochem. Mol. Biol. 1998. 31: 370-376.
11. Lee, T. R. and Lawrence, D. S., Acquisition of high-affinity, SH2-targeted ligands via a spatially focused library. J. Med. Chem. 1999. 42: 784-787.
12. src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance. Proc. Natl. Acad. Sci. USA 1993. 90: 4902-4906.
13. Gilmer, T., Rodriguez, M., Jordan, S. et al., Peptides inhibitors of src SH3-SH2-Phosphorylation Interaction. J. Biol. Chem. 1994. 269: 31711-31719.
14. Kiani, A., Rao, A. and Aramburu, J., Manipulating immune responses with immunosuppressive agents that target NFAT. Immunity 2000. 12: 359-372.
15. Wange, R. L. and Samelson, L. E., Complex complexes: signaling at the TCR. Immunity 1996. 5: 197-205.
16. Kane, L. P., Lin, J. and Weiss, A., Signal transduction by the TCR for antigen. Curr. Opin. Immunol. 2000. 12: 242-249.
17. Williams, B. L., Irvin, B. J., Sutor, S. L., Chini, C. C., Yacyshyn, E., Bubeck, W. J., Dalton, M., Chan A. C. and Abraham, R. T., Phosphorylation of Tyr319 in ZAP70 is required for T cell antigen receptor-dependent phospholipase C-gamma 1 and Ras activation. EMBO J. 1999. 18: 1832-1844.
18. Di Bartolo, V., Mege, D., Germain, V., Pelosi, M., Dufour, E., Michel, F., Magistrelli, G., Isacchi, A. and Acuto, O., Tyrosine 319, a newly identified phosphorylation site of ZAP70, plays a critical role in T cell antigen receptor signaling. J. Biol. Chem. 1999. 274: 6285-6294.
19. Reynolds, L. F., Smyth, L. A., Norton, T., Freshney, N., Downward, J., Kioussis, D. and Tibulewicz, V. L. J., Vav1 transduces T cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and -independent pathways. J. Exp. Med. 2002. 195: 1103-1114.
20. Hanke, J. H., Gardner, J. P., Dow, R. L., Changelian, P. S., Brissette, W. H., Weringer, E. J., Pollok, B. A. and Connelly, P. A., Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. J. Biol. Chem. 1996. 271: 695-701.
21. Zhu, X., Kim J. L., Newcomb, J. R., Rose, P. E., Stover, D. R., Toledo, L. M., Zhao, H. and Morgenstern, K. A., Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure 1999. 7: 651-661.
22. Pelosi, M., Di Bartolo, V., Mounier, V., Mege, D., Pascussi, J. M., Dufour, E., Blondel, A. and Acuto, O., Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck. J. Biol. Chem. 1999. 274: 14229-14237.
23. Choi, Y. B., Kim, C. K. and Yun, Y., Lad, an adapter protein interacting with the SH2 domain of p56lck, is required for T cell activation. J. Immunol. 1999. 163: 5242-5249.
24. Li, Y., He, X., Schembri-King, J., Jakes, S. and Hayashi, J., Cloning and characterization of human Lnk, an adaptor protein with pleckstrin homology and Src homology 2 domains that can inhibit T cell activation. J. Immunol. 2000. 164: 5199-5206.
25. 2+-dependent pathways of T cell antigen receptor-mediated signaling by inhibiting the PLCγ-1 and ITK activity. Blood 2003, in press.
26. Rajagopal, K., Sommers, C. L., Decker, D. C., Mitchell, E. O., Korthauer, U., Sperling, A. I., Kozak, C. A., Love, P. E. and Bluestone, J. A., RIBP, a novel Rlk/Txk- and itk-binding adaptor protein that regulates T cell activation. J. Exp. Med. 1999. 190: 1657-1668.
27. al-Sereiti, M. R., Abu-Amer, K. M. and Sen, P., Pharmacology of rosemary (Rosmarinus officinalis Linn.) and its therapeutic potentials. Indian J. Exp. Biol. 1999. 37: 124-130.
28. Peake, P. W., Pussell, B. A., Martyn, P., Timmermans, V. and Charlesworth, J. A., The inhibitory effect of rosmarinic acid on complement involves the C5 convertase. Int. J. Immunopharmacol. 1991. 13: 853-857.
29. Sahu, A., Rawal, N. and Pangburn, M. K., Inhibition of complement by covalent attachment of rosmarinic acid to activated C3b. Biochem. Pharmacol. 1999. 57: 1439-1446.
30. Englberger, W., Hadding, U., Etschenberg, E., Graf, E., Leyck, S., Winkelmann, J. and Parnham, M. J., Rosmarinic acid: a new inhibitor of complement C3-convertase with anti-inflammatory activity. Int. J. Immunopharmacol. 1988. 10: 729-737.
31. Zhou, L., Ritchie, D., Wang, E. Y., Barbone, A. G., Argentieri, D. and Lau, C. Y., Tepoxalin, a novel immunosuppressive agent with a different mechanism of action from cyclosporin A. J. Immunol. 1994. 153: 5026-5037.
32. Finkel, T., Reactive oxygen species and signal transduction. IUBMB Life 2001. 52: 3-6.
33. Devadas, S., Zaritskaya, L., Rhee, S. G., Oberley, L. and Williams, M. S., Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J. Exp. Med. 2002. 195: 59-70.
34. Furka, A., Sebestyen, F., Asgedom, M. and Dibo, G., General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Pept. Protein Res. 1991. 37: 487-493.
35. Fields, G. B., Tian, Z. and Barany, G. (Eds.) Sythetic peptide: A user's guide. Freeman, New York 1992, pp. 77-183.
36. Smith, D. B. and Johnson, K. S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 1988. 67: 31-40.
37. Strong, D. M., Ahmed, A. A., Thurman, G. B. and Sell, K. W., In vitro stimulation of murine spleen cells using a microculture system and a multiple automated sample harvester. J. Immunol. Methods 1973. 2: 279-291.
38. Sanglier, J. J., Quesniaux, V., Fehr, T., Hofmann, H., Mahnke, M., Memmert, K., Schuler, W., Zenke, G., Gschwind, L., Maurer, C. and Schilling, W., Sanglifehrins A, B, C, and D, novel cyclophilin-binding compounds isolated from Streptomyces sp. A92-308110. I. Taxonomy, fermentation, isolation and biological activity. J. Antibiot. (Tokyo) 1999. 52: 466-473.