[Lysosomal cysteine proteinases at neoplastic transformation].
This review summarizes the data on classification, properties, structure and biological functions of mammalian papain-like lysosomal cysteine proteinases (cathepsins). The most studied are cathepsins B, H, L, S and K. The peculiarities of lysosomal cysteine proteinase regulation, particularly regulation by specific endogenous inhibitors are discussed. Involvement of these enzymes in development of physiological and pathological processes are considered. Special attention is paid to the role of cysteine proteinases and their inhibitors in neoplastic transformation. The possibility of use cathepsin endogenous inhibitors as basis for design antitumorogenic therapeutic substances are discussed.
Dilakian
E A
EA
Tsvetkova
I V
IV
D000818:Animals; D002403:Cathepsins / Q000145:classification / Q000187:drug effects / Q000378:metabolism*; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D006801:Humans; D008247:Lysosomes / Q000201:enzymology*
D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins