Proteinaceous cysteine protease inhibitors

被引:118
作者
Dubin, G [1 ]
机构
[1] Jagiellonian Univ, Fac Biotechnol, PL-30387 Krakow, Poland
关键词
protease; proteinase; peptidase; inhibitor;
D O I
10.1007/s00018-004-4445-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Studies of proteinaceous cysteine protease inhibitors originated with the discovery of cystatins in the 1960s. Since that time, a rich and fascinating world of proteins that control and regulate a multitude of important physiological processes, ranging from the basics of protein turnover to development and brain function, has been uncovered. Failures in such important and complex systems inevitably lead to pathologies. Many threatening diseases such as cancer or neurological disorders, to mention only some, are attributed to deregulation of protease-inhibitor balance. Moreover, important aspects of infection pathology and host defense rely on proteolysis and protease inhibition. Recent advances in the field of protease inhibitors have drawn attention to the possible use of this collected knowledge to control related pathological processes. This review attempts to familiarize the reader with proteinaceous cysteine protease inhibitors by providing an overview of current knowledge. The work primarily highlights biological processes in which the inhibitors are involved and focuses on pathologies resulting from aberrant protease-inhibitor balance, pointing out emerging possibilities for their correction.
引用
收藏
页码:653 / 669
页数:17
相关论文
共 154 条
[61]   Folding, stability, and secondary structure of a new dimeric cysteine proteinase inhibitor [J].
Kidric, M ;
Fabian, H ;
Brzin, J ;
Popovic, T ;
Pain, RH .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2002, 297 (04) :962-967
[62]  
KOIDE SS, 2000, PSEBM, V224, P124
[63]  
Lackner KJ, 1998, BRIT J RHEUMATOL, V37, P1164
[64]   The epilepsy, the protease inhibitor and the dodecamer: progressive myoclonus epilepsy, cystatin b and a 12-mer repeat expansion [J].
Lalioti, MD ;
Antonarakis, SE ;
Scott, HS .
CYTOGENETIC AND GENOME RESEARCH, 2003, 100 (1-4) :213-223
[65]   Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases [J].
Lenarcic, B ;
Krishnan, G ;
Borukhovich, R ;
Ruck, B ;
Turk, V ;
Moczydlowski, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (20) :15572-15577
[66]  
Lenarcic B, 1997, J BIOL CHEM, V272, P13899
[67]  
Lenarcic B, 1998, BIOL CHEM, V379, P105
[68]   Prolongation of transgene expression by coexpression of cytokine response modifier A in rodent liver after adenoviral gene transfer [J].
Li, XK ;
Kosuga, M ;
Tokieda, K ;
Kanaji, A ;
Fukuhara, Y ;
Hashimoto, M ;
Okabe, K ;
Yaginuma, H ;
Yamada, M ;
Suzuki, S ;
Okuyama, T .
MOLECULAR THERAPY, 2002, 5 (03) :262-268
[69]   The neuronal apoptosis inhibitory protein is a direct inhibitor of caspases 3 and 7 [J].
Maier, JKX ;
Lahoua, Z ;
Gendron, NH ;
Fetni, R ;
Johnston, A ;
Davoodi, J ;
Rasper, D ;
Roy, S ;
Slack, RS ;
Nicholson, DW ;
MacKenzie, AE .
JOURNAL OF NEUROSCIENCE, 2002, 22 (06) :2035-2043
[70]   THE 3-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN STEFIN-A [J].
MARTIN, JR ;
CRAVEN, CJ ;
JERALA, R ;
KROONZITKO, L ;
ZEROVNIK, E ;
TURK, V ;
WALTHO, JP .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 246 (02) :331-343