Proteinaceous cysteine protease inhibitors.
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.
Dubin
G
G
Faculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387, Krakow, Poland. gdubin@mol.uj.edu.pl
D029845:Amphibian Proteins; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015891:Cystatins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins; D018969:Insulin-Like Growth Factor Binding Proteins / Q000737:chemistry / Q000378:metabolism; D007704:Kininogens / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015843:Serpins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D029845:Amphibian Proteins; D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; C411656:Clitocypin protein, Clitocybe nebularis; D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D005656:Fungal Proteins; D051034:Inhibitor of Apoptosis Proteins; D018969:Insulin-Like Growth Factor Binding Proteins; D007704:Kininogens; D011506:Proteins; D015800:Protozoan Proteins; D015843:Serpins; D014764:Viral Proteins; C435145:chagasin, Trypanosoma; C106356:equistatin; C086430:inhibitor of apoptosis, Nucleopolyhedrovirus; C027525:saxitoxin-binding protein, Rana catesbeiana; C495491:staphostatin A, Staphylococcus epidermidis; C033668:calpastatin; C074641:interleukin-1beta-converting enzyme inhibitor