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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.
exogenous CTSV inhibited Ang (show ANG Proteins) -induced hypertrophy in HCM cells by inhibiting PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins)
E2F1 (show E2F1 Proteins) directly binds to CTSL2 promoter and regulates CTSL2 gene expression.
using cathepsin V and cathepsin L as model enzymes, a series of chimeras were generated to identify noncatalytic regions that are responsible for the potent elastolytic activity of cathepsin V
inflammatory cues and monocyte-endothelial cell interactions upregulate cathepsin K (show CTSK Proteins) and V activity via a JNK (show MAPK8 Proteins) signaling axis
Findings indicate the unique function of cathepsin V for producing enkephalin and neuropeptide Y (NPY (show NPY Proteins)) neuropeptides required for neurotransmission in health and neurological diseases.
CTSL2 might be involved in progression of endometrial cancer.
functions of CTSL (show CTSL1 Proteins) and CTSV in the positive selection of CD4 (show CD4 Proteins)+ T cells
A proteolytically active variant of cathepsin V is localized to cell nucleus (in peri (show PLIN1 Proteins)-nucleolar pattern) in thyroid carcinoma cells.
stratum corneum thiol protease is identical with the recently described cathepsin L2 protease.
Human cathepsin V compensates for murine cathepsin L in mouse epidermis and hair follicles.
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may play an important role in corneal physiology. This gene is expressed in colorectal and breast carcinomas but not in normal colon, mammary gland, or peritumoral tissues, suggesting a possible role for this gene in tumor processes. Alternatively spliced variants, encoding the same protein, have been identified.
, cathepsin L
, cathepsin L1
, cathepsin L2 preproprotein
, cathepsin L2, preproprotein
, cathepsin U