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These results suggest that the ecdysone response elements are vital for activation of the promoter by 20-hydroxyecdysone (20E) in the larval fat body and further support the crucial role of ecdysone signaling to control cathepsin D gene transcription.
Study demonstrate that PGRN (show GRN Proteins) interacts with the lysosomal protease CTSD and maintains its proper activity in vivo. Therefore, by regulating CTSD activity, PGRN (show GRN Proteins) may modulate protein homeostasis. This could potentially explain the TDP-43 (show TARDBP Proteins) aggregation observed in frontotemporal lobar degeneration with GRN (show GRN Proteins) mutations.
The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation.
Secreted PGRN (show GRN Proteins) is incorporated into cells via sortilin (show SORT1 Proteins) or cation-independent mannose 6-phosphate receptor (show IGF2R Proteins), and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN (show GRN Proteins) levels led to a cell-type-specific increase of insoluble TDP-43 (show TARDBP Proteins). In the brain tissue of FTLD-TDP patients with PGRN (show GRN Proteins) deficiency, CTSD and phosphorylated TDP-43 (show TARDBP Proteins) accumulated in neurons
CTSD, in need of its catalytic activity, may promote proliferation in advanced glycation end products-treated human umbilical vein endothelial cells independent of the autophagy-lysosome pathway.
Cathepsin D facilitates the TRAIL-induced apoptosis of MDA-MB-231 breast cancer cells in enzymatic activity-dependent manner. Caspase-8 (show CASP8 Proteins) and Bid (show BID Proteins) proteins are the CD targets. The modulatory role of CD in cell response to TRAIL was also confirmed in another breast cancer cell line SKBR3.
Gene expression level of CTSD is significantly higher in AD patients when compared to normal controls.
There was a significant difference between groups with and without endothelial dysfunction in terms of cathepsin D levels, and negative and significant correlations were found between brachial artery FMD (show FLNA Proteins)% and cathepsin D levels. Cathepsin D, which is known to be associated with atherosclerosis, may play a role in the proce
Serum CTSB (show CTSB Proteins) and CTSD concentrations were found to have a diagnostic value in NPC (show NPC1 Proteins). However, the CTSB (show CTSB Proteins) and CTSD serum levels had no prognostic role for the outcome in nasopharyngeal carcinoma patients.
Fibroblasts from Niemann-Pick type C (NPC (show NPC1 Proteins)) disease patients with low levels of NPC1 (show NPC1 Proteins) protein have high amounts of procathepsin D but reduced quantities of the mature protein, thus showing a diminished cathepsin D activity.
Data indicate that cathepsin D (CD) protein is elevated in the retinas of diabetic mice and serum of human patients with diabetic macular edema (DME).
These results suggested that Purkinje cells (PCs) were more vulnerable to CTSD deficiency in lysosomes than to autophagy impairment, and this vulnerability does not depend on the severity of axonal swelling.
Exposure of J774A.1 cells to HOCl or HOSCN resulted in a significant decrease in the activity of the Cys (show DNAJC5 Proteins)-dependent cathepsins B and L, but not the Asp (show C3 Proteins)-dependent cathepsin D.
these results suggest that inhibition of lysosomal proteases, such as CtsD, could be a new therapeutic approach to reduce renal fibrosis and slow progression of chronic kidney disease.
The neuroectoderm specific cathepsin D (Ctsd) knock-out mice survived about 5.5 days longer.
This study demonistrated that Mice heterozygous for cathepsin D deficiency exhibit mania-related behavior and stress-induced depression.
Post-translational modifications drive CatD into the nucleus to cleave Histone 3 in the involuting mammary gland.
Increased lysosomal storage in CatD KO mice causes oxidative damage in brain pericytes, subsequently resulting in an increased vessel diameter and enhanced permeability of the BBB.
Mouse prolactin (show PRL Proteins) was proteolytically cleaved by Cath D between amino acids 148 and 149. N-terminal prolactin (show PRL Proteins) fragment and Cath D expression increased during mammary gland involution.
Association of polymorphisms in calpain 1 (show CAPN1 Proteins), (mu/I) large subunit, calpastatin (show CAST Proteins), and cathepsin D genes with meat quality traits in double-muscled Piemontese cattle.
findings strongly suggest a link between the lysosomal dysfunction of cathepsin D and the etiology of Alzheimer's disease
The effect of heavy metal cations on the activity of cathepsin D, was studied.
This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease.
, cathepsin D
, aspartic protease
, cathepsin d
, preprocathepsin D
, ceroid-lipofuscinosis, neuronal 10
, lysosomal aspartyl peptidase
, lysosomal aspartyl protease
, cathepsin D (lysosomal aspartyl peptidase)
, cathepsin D (lysosomal aspartyl protease)
, prepro-cathepsin D, prepro-CD