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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]
Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. [ 3 ] [ 4 ] [ 5 ] The protein is a cysteine cathepsin , a lysosomal cysteine protease that plays a major role in intracellular protein catabolism .
[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 and the R-domain , where the active site is located between them. [1]
Cathepsin L may refer to: Cathepsin L1, a human protease enzyme encoded by the CTSL gene and known for its role in viral entry; Cathepsin L2, a human protease enzyme ...
L-form bacteria, also known as L-phase bacteria, L-phase variants or cell wall-deficient bacteria (CWDB), are growth forms derived from different bacteria. They lack cell walls . [ 1 ] Two types of L-forms are distinguished: unstable L-forms , spheroplasts that are capable of dividing, but can revert to the original morphology, and stable L ...
Analysis by immunofluorescence corroborated that NETs contain proteins from azurophilic granules (neutrophil elastase, cathepsin G and myeloperoxidase), specific granules (lactoferrin), tertiary granules , and the cytoplasm; however, CD63, actin, tubulin and various other cytoplasmatic proteins are not present in NETs.
The production of cathelicidin is up-regulated by vitamin D. [31] [32] SAAP-148 (a synthetic antimicrobial and antibiofilm peptide) is a modified version of LL-37 that has enhanced antimicrobial activities compared to LL-37. In particular, SAAP-148 was more efficient in killing bacteria under physiological conditions. [33]
The alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. [1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 beta strands connected by 6 alpha helices.