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Human Cathepsin D ELISA Kit for Sandwich ELISA - ABIN417608
Huber-Lang, Denk, Fulda, Erler, Kalbitz, Weckbach, Schneider, Weiss, Kanse, Perl: Cathepsin D is released after severe tissue trauma in vivo and is capable of generating C5a in vitro. in Molecular immunology 2012
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Li, Lu, Nguyen, Bae, Chapman, Feng, Hawkins, Pessin, Sears, Nguyen, Amidi, Watkins, Nguyen, Olefsky: Functional heterogeneity of CD11c-positive adipose tissue macrophages in diet-induced obese mice. in The Journal of biological chemistry 2010
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Vitner, Dekel, Zigdon, Shachar, Farfel-Becker, Eilam, Karlsson, Futerman: Altered expression and distribution of cathepsins in neuronopathic forms of Gaucher disease and in other sphingolipidoses. in Human molecular genetics 2010
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Schwartz-Roberts, Shajahan, Cook, Wärri, Abu-Asab, Clarke: GX15-070 (obatoclax) induces apoptosis and inhibits cathepsin D- and L-mediated autophagosomal lysis in antiestrogen-resistant breast cancer cells. in Molecular cancer therapeutics 2013
Poliakov, Strunnikova, Jiang, Martinez, Parikh, Lakkaraju, Thomas, Brooks, Redmond: Multiple A2E treatments lead to melanization of rod outer segment-challenged ARPE-19 cells. in Molecular vision 2014
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.
The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation.
Secreted PGRN (show GRN ELISA Kits) is incorporated into cells via sortilin (show SORT1 ELISA Kits) or cation-independent mannose 6-phosphate receptor (show IGF2R ELISA Kits), and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN (show GRN ELISA Kits) levels led to a cell-type-specific increase of insoluble TDP-43 (show TARDBP ELISA Kits). In the brain tissue of FTLD-TDP patients with PGRN (show GRN ELISA Kits) deficiency, CTSD and phosphorylated TDP-43 (show TARDBP ELISA Kits) 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 ELISA Kits) and Bid (show BID ELISA Kits) 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 ELISA Kits)% 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 ELISA Kits) and CTSD concentrations were found to have a diagnostic value in NPC (show NPC1 ELISA Kits). However, the CTSB (show CTSB ELISA Kits) and CTSD serum levels had no prognostic role for the outcome in nasopharyngeal carcinoma patients.
Fibroblasts from Niemann-Pick type C (NPC (show NPC1 ELISA Kits)) disease patients with low levels of NPC1 (show NPC1 ELISA Kits) 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).
Data show that co-silencing of tricho-rhino (show RHNO1 ELISA Kits)-phalangeal-syndrome (TRPS1 (show TRPS1 ELISA Kits)) and cathepsin D (Cath-D) in breast cancer cells (BCC) affects the transcription of cell cycle and proliferation.
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 ELISA Kits)-dependent cathepsins B and L, but not the Asp (show C3 ELISA Kits)-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 (show ALMS1 ELISA Kits).
Mouse prolactin (show PRL ELISA Kits) was proteolytically cleaved by Cath D between amino acids 148 and 149. N-terminal prolactin (show PRL ELISA Kits) fragment and Cath D expression increased during mammary gland involution.
Cathepsin D was not inherent to sperm themselves, but rather of epididymal origin and was presumably transported to the sperm surface via epididymosomes.
Association of polymorphisms in calpain 1 (show CAPN1 ELISA Kits), (mu/I) large subunit, calpastatin (show CAST ELISA Kits), 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