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these findings suggest that CTSL functions as a carcinogenic factor and may contribute to Paclitaxel resistance in human ovarian cancer
Findings from this community-based cohort of young children show that surrogate markers for cardiovascular disease such as total fat mass, percent body fat, abdominal fat, body fat distribution, maximal oxygen uptake and pulse pressure were all associated with cystatin B (zeige CSTB Proteine). This was not found for cathepsin L or cathepsin D (zeige CTSD Proteine)
An association between higher serum cathepsin L and increased risk of cardiovascular mortality was found in two independent cohorts. Impaired kidney function appears to be an important moderator or mediator of these associations.
CTSL is an important protein which mediates cell invasion and migration of human glioma U251 cells.
Collectively, these data indicate that CTSL is an important contributor to tumor angiogenesis and that the CTSL inhibition may have therapeutic utility in the treatment of breast cancer patients.
Therefore, we show for the first time that the nuclear localization of Cat L and its substrate Cux1can be positively regulated by Snail NLS and importin beta1, suggesting that Snail, Cat L and Cux1 all utilize importin beta1 for nuclear import.
Data suggest substrate specificity of CTSL includes SNCA; CTSL truncates SNCA first at C-terminus before attacking internal beta-sheet-rich region between residues 30 and 100; three of four proteolysis sites contain glycine residues likely involved in beta-turn, where proteolysis leads to solvent exposure of internal residues and further proteolysis of amyloid. (CTSL = cathepsin L; SNCA = alpha-synuclein)
Cathepsin L knockdown induced by RNA interference significantly promoted curcumin-induced cytotoxicity, apoptosis, and cell cycle arrest. The knockdown also inhibited the migration and invasion of glioma cells. Cathepsin L may be a new target to enhance the efficacy of curcumin against cancers.
a positive feedback loop between Snail (zeige SNAI1 Proteine)-nuclear Cat L (zeige TRPV6 Proteine)-CUX1 (zeige CUX1 Proteine) drives epithelial mesenchymal transition, is reprted.
CtsB (zeige CTSB Proteine)/L as major regulators of lysosomal function and demonstrate that CtsB (zeige CTSB Proteine)/L may play an important role in intracellular cholesterol trafficking and in degradation of the key AD proteins
Exposure of J774A.1 cells to HOCl or HOSCN resulted in a significant decrease in the activity of the Cys (zeige DNAJC5 Proteine)-dependent cathepsins B and L, but not the Asp (zeige C3 Proteine)-dependent cathepsin D (zeige CTSD Proteine).
findings suggest that single chain-cathepsin L is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 (zeige SERPINB1 Proteine) and secondarily by asparagine endopeptidase.
CTSL plays an important role in the MHC class II-mediated peptide presentation in thymic epithelial cells, acting both in the invariant chain degradation and in the generation of MHC class II-bound peptide ligands presented by cortical thymic epithelial cells. Consequently, CTSL plays an important role in the positive selection of CD4 (zeige CD4 Proteine)+ T cell in thymus.
genetic blockade of cathepsin L activity is inferred to retard Myc (zeige MYC Proteine)-driven tumor growth, encouraging the potential utility of pharmacological inhibitors of cysteine cathepsins in treating late stage tumors.
Double immunofluorescence analysis showed that CTLA-2alpha was co-localized with cathepsin L, cathepsin C (zeige CTSC Proteine), and TINAGL1 (zeige TINAGL1 Proteine) in placenta.
CtsB and CtsL are essential in alpha-syn lysosomal degradation
The phenotypes of cathepsin L deficiency can be fully assigned to lack of canonically targeted cathepsin L, while the biogenesis and functionality of nucleo-cytosolic cathepsin L remain elusive.
in vivo functional evidence for overexpressed CTSL as a promoter of lung metastasis, whereas high CTSL levels are maintained during tumor progression due to stress-resistant mRNA translation.
cathepsin L has a protective role in mouse skin carcinogenesis
Cathepsin L is involved in nociception in mice, whereas peripheral autophagy and cathepsin L contribute, at least in part, to the antinociceptive effect of dimethoxybenzylidene in mice.
Endosomal acidification and cathepsin L activity is required for porcine enteric calicivirus replication.
CTSL1 is expressed by endometrial epithelia, placental areolae, and neonatal intestine, and it may function in the transport of macromolecules across these epithelia.
These results, together with those previously reported for other genes of this family, suggest that cathepsin genes play a role in defining economically important traits in pigs.
These results suggest that an antipain-sensitive protease or cathepsin L (or a related protease) is a candidate for pp25 degradation.
The cathepsin L deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease.
Cathepsin L has an previously uncharacterized biological role in the production of [Met]enkephalin, an endogenous peptide neurotransmitter
Secretory vesicle function of cathepsin L for biosynthesis of active enkephalin opioid peptide contrasts with its function in lysosomes for protein degradation.
The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. Multiple alternatively spliced transcript variants have been found for this gene.
, major excreted protein
, Cat L
, p39 cysteine proteinase
, cathepsin L
, cyclic protein 2
, Cathepsin L1
, cathepsin L1-like
, cathepsin L2 preproprotein
, cysteine proteinase-1
, Cathepsin L
, cathepsin V
, cathepsin L.1