Lysosomal cysteine proteases: structure, function and inhibition of cathepsins.
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.
Department of Biology and Program in Biochemistry and Molecular Biology, Ursinus College, Collegeville, PA 19426, USA. rroberts@ursinus.edu
Rebecca
R
Roberts
D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000145:classification / Q000187:drug effects / Q000502:physiology; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology*; D006801:Humans; D008247:Lysosomes / Q000201:enzymology
D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins; D003546:Cysteine Endopeptidases