Information om | Engelska ordet CATHEPSIN

Exempel på hur man kan använda CATHEPSIN i en mening

• There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption.
• Both MCP-1 and RANTES induce formation of TRAP-positive, multinuclear cells from M-CSF-treated monocytes in the absence of RANKL, but produced osteoclasts that lacked cathepsin K expression and resorptive capacity.
• Cathepsin S is a member of the peptidase C1 family of cysteine cathepsins, a lysosomal cysteine protease that may participate in the degradation of antigenic proteins to peptides for presentation to the MHC class II.
• Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins.
• Neutrophil elastase is closely related to other cytotoxic immune serine proteases, such as the granzymes and cathepsin G.
• Analysis by immunofluorescence corroborated that NETs contain proteins from azurophilic granules (neutrophil elastase, cathepsin G and myeloperoxidase), specific granules (lactoferrin), tertiary granules (gelatinase), and the cytoplasm; however, CD63, actin, tubulin and various other cytoplasmatic proteins are not present in NETs.
• Cathepsin B may enhance the activity of other proteases, including matrix metalloproteinase, urokinase (serine protease urokinase plasminogen activator), and cathepsin D,.
• Cysteine endopeptidases are a group of enzymes that also include the more distantly related papain derived from papaya latex, bromelase (bromelain) extracted from pineapple stem, calpain, caspases, cathepsin B, and chymopapain.
• The mechanism of action by which nitroxoline inhibits cathepsin B may also suggest that further research of noncovalent, noncompetitive inhibitors of cathepsin B could be warranted.
• F2L is a naturally occurring acylated peptide derived from the N-terminal sequence of heme-binding protein 1 by cathepsin D cleavage that potently stimulates chemotaxis through FPR3 in monocytes and monocyte-derived dendritic cells.
• It inactivates many serine proteases, including trypsin, chymotrypsin, kallikrein, plasmin, granulocyte elastase, cathepsin, thrombin, and factors IXa, Xa, XIa, and XlIa.
• Among the encoded proteins are a caspase, a cathepsin B, several kinases, E3 ubiquitin ligases, a fatty acid elongase, a sphingomyelinase, a phosphate acyltransferase and a patatin-like phospholipase.
• Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis.
• SLPI inhibits human leukocyte elastase, human cathepsin G, human trypsin, neutrophil elastase, and mast cell chymase.
• Recombinant full length LEKTI inhibits the exogenous serine proteases trypsin, plasmin, subtilisin A, cathepsin G and human neutrophil elastase.
• Cleavage of the SARS-CoV-2 S2 spike protein required for viral entry into cells can be accomplished by proteases TMPRSS2 located on the cell membrane, or by cathepsins (primarily cathepsin L) in endolysosomes.
• The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin that may have a specific function in the mechanism or regulation of T-cell cytolytic activity.
• The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily.
• Members of Fruton's lab studied cathepsin C and several other peptidases, as well as proteinases that catalyzed transpeptidation, which was thought (and ultimately confirmed) to be part of the biosynthesis of proteins.
• This gene codes for cathepsin K, a lysosomal cysteine protease that is highly expressed in osteoclasts and plays a significant role in bone remodelling by degenerating the bone matrix proteins such as type I collagen, osteopontin, and osteonectin.

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