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Cancer, Cathepsin D is a mitogen and "it attenuates the anti-tumor immune response of decaying chemokines to inhibit the function of dendritic cells". Cathepsins B and L are involved in matrix degradation and cell invasion. [3] Stroke [4] Traumatic brain injury [5] Alzheimer's disease [6] Arthritis [7]
Download as PDF; Printable version; In other projects Wikidata item; Appearance. move to sidebar hide. Cathepsin L may refer to: Cathepsin L1, a human ...
Cathepsin L1 is a member of the Peptidase C1 MEROPS family, which plays an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. [10]
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
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Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene. [5] [6] [7] [8]The protein is a human cysteine cathepsin, a lysosomal cysteine protease with endopeptidase activity.
E-64 is an epoxide which can irreversibly inhibit a wide range of cysteine peptidases.. The compound was first isolated and identified from Aspergillus japonicus in 1978. [1] It has since been shown to inhibit many cysteine peptidases such as papain, cathepsin B, cathepsin L, calpain and staphopain.
A calpain (/ ˈ k æ l p eɪ n /; [1] EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium-dependent, non-lysosomal cysteine proteases (proteolytic enzymes) expressed ubiquitously in mammals and many other organisms.