p(HGNC:CTSD)

Entity

Name

CTSD

Namespace

hgnc

Namespace Version

20180906

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

On the protein level, TFEB lysosomal target genes LAMP1 and Cathep- sin D (CTSD) are also increased in the FTD frontal cortex relative to normal subjects, and TFEB protein levels trended increased with statistical significance in the CBD group PubMed:30108137

In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111

In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111

The consequences of impaired lysosome function, for example, may be observed in cathepsin D knockout mice and Drosophila melanogaster cathepsin D mutants which show neurodegeneration and associated accumulation of autophagosomes and lysosomes [33–35]. PubMed:18930136

The consequences of impaired lysosome function, for example, may be observed in cathepsin D knockout mice and Drosophila melanogaster cathepsin D mutants which show neurodegeneration and associated accumulation of autophagosomes and lysosomes [33–35]. PubMed:18930136

In contrast to the expression of Asp 2, cathepsin D does not cause an increase in the secretion of sAPPb (Fig. 2d). PubMed:10656250

Cathepsin D, a lysosomal protease, exhibited the capacity to degrade tau proteins in cultured hippocampal slices (Bednarski and Lynch, 1996). PubMed:23528736

Similarly, adding exogenous cathepsin D to homogenates of rat cortex at a neutral pH also generated tau fragments. Intriguingly, if a cysteine protease inhibitor was added to the assay, tau cleavage stopped at the 29-kDa fragment, suggesting that cathepsin D (an aspartyl protease) could cleave tau to a 29-kDa fragment after which other proteases may act to further degrade the protein. PubMed:24027553

In M1C neuroblastoma cells that inducibly express full-length wild-type tau (4R0N), treatment with CQ also significantly slowed down tau degradation, and caused its accumulation (92). Treatment of hippocampal slices with the cathepsin modulator ZPAD (which stimulates cathepsin D very strongly) appears to increase the proteolysis of full-length tau resulting in the production of smaller fragments, including a phosphorylated 29 kDa fragment (86, 89). This partial degradation of tau was inhibited by inclusion of a selective cathepsin D inhibitor (86). PubMed:24027553

Cathepsin D seems particularly important for degrading tau, as its expression was neuroprotective in a Drosophila tauopathy model. Levels of cathepsin D are elevated in flies expressing mutant human tau. If cathepsin D is genetically ablated, these tau flies exhibit enhanced neurotoxicity and a shorter lifespan (93). PubMed:24027553

In M1C neuroblastoma cells that inducibly express full-length wild-type tau (4R0N), treatment with CQ also significantly slowed down tau degradation, and caused its accumulation (92). Treatment of hippocampal slices with the cathepsin modulator ZPAD (which stimulates cathepsin D very strongly) appears to increase the proteolysis of full-length tau resulting in the production of smaller fragments, including a phosphorylated 29 kDa fragment (86, 89). This partial degradation of tau was inhibited by inclusion of a selective cathepsin D inhibitor (86). PubMed:24027553

Cathepsin D seems particularly important for degrading tau, as its expression was neuroprotective in a Drosophila tauopathy model. Levels of cathepsin D are elevated in flies expressing mutant human tau. If cathepsin D is genetically ablated, these tau flies exhibit enhanced neurotoxicity and a shorter lifespan (93). PubMed:24027553

Cathepsin D seems particularly important for degrading tau, as its expression was neuroprotective in a Drosophila tauopathy model. Levels of cathepsin D are elevated in flies expressing mutant human tau. If cathepsin D is genetically ablated, these tau flies exhibit enhanced neurotoxicity and a shorter lifespan (93). PubMed:24027553

Human brain tau can be degraded by the proteases, such as cathepsin-D, amino peptidases, human high temperature requirement serine protease A1 (HTRA1), thrombin, caspases, and calpains (Chesser et al. 2013; Kenessey et al. 1997) PubMed:29626319

The consequences of impaired lysosome function, for example, may be observed in cathepsin D knockout mice and Drosophila melanogaster cathepsin D mutants which show neurodegeneration and associated accumulation of autophagosomes and lysosomes [33–35]. PubMed:18930136

The consequences of impaired lysosome function, for example, may be observed in cathepsin D knockout mice and Drosophila melanogaster cathepsin D mutants which show neurodegeneration and associated accumulation of autophagosomes and lysosomes [33–35]. PubMed:18930136

The consequences of impaired lysosome function, for example, may be observed in cathepsin D knockout mice and Drosophila melanogaster cathepsin D mutants which show neurodegeneration and associated accumulation of autophagosomes and lysosomes [33–35]. PubMed:18930136