3.4.23.5: cathepsin D
This is an abbreviated version!
For detailed information about cathepsin D, go to the full flat file.
Word Map on EC 3.4.23.5
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3.4.23.5
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lysosomal
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pepstatin
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estrogen
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metastasis
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alzheimer
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proteinases
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aspartyl
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node
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vacuole
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lymph
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renin
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pepsin
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endosomes
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progesterone
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hydrolases
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endocytic
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phagosomes
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amyloid
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beta-glucuronidase
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plasminogen
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mannose
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6-phosphate
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axillary
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autophagosomes
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saposins
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lysosomal-associated
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leupeptin
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plasmepsins
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beta-hexosaminidase
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missorting
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mannose-6-phosphate
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chymosin
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lysotracker
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lipofuscinosis
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lc3-ii
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autophagy-lysosomal
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rab7
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ceroid
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estrogen-regulated
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immunoradiometric
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medicine
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lc3
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lamp-1
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node-negative
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trans-golgi
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upa
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endocytosed
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node-positive
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c-erbb-2
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autolysosomes
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cation-independent
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molecular biology
- 3.4.23.5
- lysosomal
- pepstatin
- estrogen
- metastasis
- alzheimer
- proteinases
-
aspartyl
- node
- vacuole
- lymph
- renin
- pepsin
- endosomes
- progesterone
- hydrolases
-
endocytic
-
phagosomes
-
amyloid
- beta-glucuronidase
- plasminogen
- mannose
- 6-phosphate
-
axillary
-
autophagosomes
-
saposins
-
lysosomal-associated
- leupeptin
-
plasmepsins
- beta-hexosaminidase
-
missorting
- mannose-6-phosphate
- chymosin
-
lysotracker
- lipofuscinosis
-
lc3-ii
-
autophagy-lysosomal
- rab7
-
ceroid
-
estrogen-regulated
-
immunoradiometric
- medicine
- lc3
- lamp-1
-
node-negative
-
trans-golgi
- upa
-
endocytosed
-
node-positive
-
c-erbb-2
-
autolysosomes
-
cation-independent
- molecular biology
Reaction
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin =
Synonyms
BmCatD, CAD 1, CAD 2, CAD 3, CapD, Cat D, CAT-D, CatD, Cath D, cath-D, cathD, cathepsin D, cathepsin D-like proteinase, cathepsin D1, cathepsin D2, CD1, CTSD, EC 3.4.4.23, matCTSD, PCD, Pep4p, preproCatD, pro-cathepsin, pro-cathepsin D, pro-CD, pro-CtsD, proCat, proCDrec, proCTSD, Proteinase A
ECTree
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Expression
Expression on EC 3.4.23.5 - cathepsin D
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15 days of starvation causes a 40% reduction in cathepsin D1 mRNA expression
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15 days of starvation does not cause significant changes in cathepsin D1 mRNA expression
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after 8 h Vibrio anguillarum challenge, the expression level of cathepsin D changes significantly in all examined tissues except mantle and hemocytes
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after challenge with Spiroplasma eriocheiris, the expression is significantly up-regulated from day 1 to 9
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cathepsin D expression and activity increases during epidermal differentiation
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cathepsin D expression in the buccal gland is increased 6.5-8.5fold after challenge with Escherichia coli or Staphylococcus aureus
cathepsin D expression shows an upward trend during embryonic development
cathepsin D is elevated in the frontal cortex, in pyramidal and granule cells of the hippocampus, and in cerebellar neurons of autistic subjects
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cathepsin D is not upregulated during apoptosis induced by 300 nM taxol or 0.01 mg doxorubicin or autophagy induced by 0.01 mM tamoxifen
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cathepsin D is overexpressed and hyper-secreted by epithelial breast cancer cells
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enzyme expression is upregulated in damaged tubular cells in nephrotoxic and ischemia reperfusion induced acute kidney injury. Enzyme expression is increased during acute tubular necrosis in transplanted kidneys
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enzyme expression levels are significantly increased in autolytic tissues
epidermal growth factor rapidly induces enzyme mRNA by 2-4fold. Cathepsin D is overexpressed in breast cancer
expression in mesenchymal stem cells is increased following co-culture with breast and colon cancer cells
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feeding after 15 days of starvation causes a 2.5fold increase in cathepsin D1 mRNA expression
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feeding after 15 days of starvation has no effect on cathepsin D1 mRNA expression
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manganese treatment causes significant increase of lysosomal enzyme cathepsin D
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senescence induced by ionizing radiation (6 Gy), 0.3 mM hydrogen peroxide or anticancer drugs (40 nM camptothecin, 0.03 mM etoposide, or 50 ng doxorubicin) is associated with up-regulation of cathepsin D
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Streptomyces pneumonia (strain D39) triggers activation of cathepsin D in macrophages about 2fold
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the enzyme expression is not influenced by the lysosomotropic agent Leu-Leu-OMe
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the enzyme expression is significantly upregulated in response to oxygen-glucose deprivation/reperfusion exposure
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the expression levels of cathepsin D in liver and head kidney increase gradually after 8 h and exceeded the background level after 24 h after challenge with Vibrio harveyi
there is a positive relationship between the expression and presence of cathepsin D at the extracellular compartment of the maternal-fetal interface and the invasiveness of the trophoblast during the postimplantation period
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