Lysosomal cysteine proteases: Structure, function and inhibition of cathepsins

被引:45
作者
Roberts, R
机构
[1] Ursinus Coll, Dept Biol, Collegeville, PA 19426 USA
[2] Ursinus Coll, Program Biochem & Mol Biol, Collegeville, PA 19426 USA
关键词
D O I
10.1358/dnp.2005.18.10.949485
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Lysosomal cysteine proteases, a subgroup of the cathepsin family, are critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. In the past decade, the number of identified human cathepsins has more than doubled and their known role in several pathologies has expanded rapidly. Increased understanding of the structure and mechanism of this class of enzymes has brought on a new fervor in the design of small molecule inhibitors with the hope of producing specific, therapeutic drugs for diseases such as arthritis, allergy, multiple sclerosis, atherosclerosis, Alzheimer's disease and cancer. (c) 2005 Prous Science. Ail rights reserved.
引用
收藏
页码:605 / 614
页数:10
相关论文
共 114 条
[41]   Structure-activity relationship study and drug profile of N-(4-fluorophenylsulfonyl)-L-valyl-L-leucinal (SJA6017) as a potent calpain inhibitor [J].
Inoue, J ;
Nakamura, M ;
Cui, YS ;
Sakai, Y ;
Sakai, O ;
Hill, JR ;
Wang, KKW ;
Yuen, PW .
JOURNAL OF MEDICINAL CHEMISTRY, 2003, 46 (05) :868-871
[42]   Multiple processing of procathepsin L to cathepsin L in vivo [J].
Ishidoh, K ;
Saido, TC ;
Kawashima, S ;
Hirose, M ;
Watanabe, S ;
Sato, N ;
Kominami, E .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1998, 252 (01) :202-207
[43]   Processing and activation of lysosomal proteinases [J].
Ishidoh, K ;
Kominami, E .
BIOLOGICAL CHEMISTRY, 2002, 383 (12) :1827-1831
[44]   CRYSTAL-STRUCTURES OF RECOMBINANT RAT CATHEPSIN-B AND A CATHEPSIN B-INHIBITOR COMPLEX - IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN [J].
JIA, ZC ;
HASNAIN, S ;
HIRAMA, T ;
LEE, X ;
MORT, JS ;
TO, R ;
HUBER, CP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (10) :5527-5533
[45]   Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis [J].
Joyce, JA ;
Baruch, A ;
Chehade, K ;
Meyer-Morse, N ;
Giraudo, E ;
Tsai, FY ;
Greenbaum, DC ;
Hager, JH ;
Bogyo, M ;
Hanahan, D .
CANCER CELL, 2004, 5 (05) :443-453
[46]   Insights into the roles of cathepsins in antigen processing and presentation revealed by specific inhibitors [J].
Katunuma, N ;
Matsunaga, Y ;
Himeno, K ;
Hayashi, Y .
BIOLOGICAL CHEMISTRY, 2003, 384 (06) :883-890
[47]   CATHEPSIN-S FROM BOVINE SPLEEN - PURIFICATION, DISTRIBUTION, INTRACELLULAR-LOCALIZATION AND ACTION ON PROTEINS [J].
KIRSCHKE, H ;
WIEDERANDERS, B ;
BROMME, D ;
RINNE, A .
BIOCHEMICAL JOURNAL, 1989, 264 (02) :467-473
[48]   Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase [J].
Klemencic, I ;
Carmona, AK ;
Cezari, MHS ;
Juliano, MA ;
Juliano, L ;
Guncar, G ;
Turk, D ;
Krizaj, I ;
Turk, V ;
Turk, B .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (17) :5404-5412
[49]   THE PRIMARY STRUCTURE AND TISSUE DISTRIBUTION OF CATHEPSIN-C [J].
KOMINAMI, E ;
ISHIDO, K ;
MUNO, D ;
SATO, N .
BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1992, 373 (07) :367-373
[50]  
LEMERE CA, 1995, AM J PATHOL, V146, P848