Suppression of immune response via inhibition of cathepsin S
作者： Hidde L. Ploegh , Richard J. Riese , Harold A. Chapman , Matthew S. Bogyo , Paula R. Bryant
DOI:
关键词:
摘要: Methods and products for suppressing a class II MHC-restricted immune response in mammal, or mammalian cells, are described. The methods depend upon inhibiting invariant chain proteolysis by cathepsin S from MHC/invariant complexes, thereby reducing the competency of MHC molecules binding antigenic peptides, presentation peptides molecules, responses. may be employed treatment autoimmune diseases, allergic responses, organ tissue graft rejection. New pharmaceutical therapeutic compositions which peptide-based inhibitors also
google.it 参考文章(35)
H Kirschke, I Schmidt, B Wiederanders, Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15). Biochemical Journal. ,vol. 240, pp. 455- 459 ,(1986) , 10.1042/BJ2400455
Nahed K. Ahmed, Lorene A. martin, Lynnetta M. Watts, Jim Palmer, Larry Thornburg, Jeff Prior, Ronald E. Esser, Peptidyl fluoromethyl ketones as inhibitors of cathepsin B : implication for treatment of rheumatoid arthritis Biochemical Pharmacology. ,vol. 44, pp. 1201- 1207 ,(1992) , 10.1016/0006-2952(92)90385-V
Sakaki Toshiro, Takahashi Chizuko, Morinaka Yasuhiro, Ando Ryoichi, Tamao Yoshikuni, Alpha-Aminoketone derivatives ,(1993)
G.P. Shi, A.C. Webb, K.E. Foster, J.H. Knoll, C.A. Lemere, J.S. Munger, H.A. Chapman, Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. Journal of Biological Chemistry. ,vol. 269, pp. 11530- 11536 ,(1994) , 10.1016/S0021-9258(19)78156-3
Elliott Shaw, Sasank Mohanty, Adrijana Colic, Veronika Stoka, Vito Turk, The affinity-labelling of cathepsin S with peptidyl diazomethyl ketones. Comparison with the inhibition of cathepsin L and calpain. FEBS Letters. ,vol. 334, pp. 340- 342 ,(1993) , 10.1016/0014-5793(93)80707-2
K S Giacoletto, J A Manning, P A Morton, B D Schwartz, M L Zacheis, Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells. Journal of Immunology. ,vol. 154, pp. 137- 150 ,(1995)
D Brömme, A Steinert, S Friebe, S Fittkau, B Wiederanders, H Kirschke, The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B. Biochemical Journal. ,vol. 264, pp. 475- 481 ,(1989) , 10.1042/BJ2640475
Heidrun Kirschke, Bernd Wiederanders, [34] Cathepsin S and related lysosomal endopeptidases Methods in Enzymology. ,vol. 244, pp. 500- 511 ,(1994) , 10.1016/0076-6879(94)44036-0
D Brömme, J L Klaus, K Okamoto, D Rasnick, J T Palmer, Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. Biochemical Journal. ,vol. 315, pp. 85- 89 ,(1996) , 10.1042/BJ3150085
Fred H. Drake, Maxine Gowan, Judith A. Blake, Lisa M. Fitzgerald, Norman H. Lee, Gregg A. Hastings, Mark D. Adams, Ewen F. Kirkness, Claire M. Fraser, Human osteoclast derived cathepsin ,(1994)