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
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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
3.4.23.5 cathepsin DAdvanced search results
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results (General Information
General Information on EC 3.4.23.5 - cathepsin D
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
malfunction
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murine cathepsin D deficiency is associated with dysmyelination/myelin disruption and accumulation of cholesteryl esters in the brain
malfunction
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mutations in cathepsin D result in the most severe, congenital form of neuronal ceroid lipofuscinoses with progressive intracellular accumulation of autofluorescent storage material, modest neurodegeneration in the brain areas related to visual function, and a retinal degenerative phenotype
malfunction
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pharmacological inhibition or knockout of cathepsin D during pneumococcal infection blocks macrophage apoptosis. Inhibition of cathepsin D has no effect on early bacterial killing but inhibits the late phase of apoptosis-associated killing of pneumococci in vitro. Cathepsin deficient mice demonstrate reduced macrophage apoptosis in vivo, with decreased clearance of pneumococci and enhanced recruitment of neutrophils to control pulmonary infection. Cathepsin D enhances Mcl-1 ubiquitination
malfunction
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absence of the enzyme results in increased resistance to acetic acid
malfunction
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enzyme deletion alters the severity of acute experimental pancreatitis
malfunction
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enzyme inhibition leads to an improvement in kidney function, a reduction in apoptosis and a decrease in tubular cell damage in kidneys with nephrotoxic or ischemia reperfusion-induced acute kidney injury
malfunction
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enzyme suppression has an inhibitory effect on cell apoptosis and the expression of proapoptotic proteins
malfunction
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inhibition of enzyme activity dramatically improves lipid metabolism and diminishes hepatic inflammation in non-alcoholic steatohepatitis
metabolism
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cathepsin D is the primary protease for the generation of adenohypophyseal vasoinhibins
metabolism
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cathepsin D plays a significant role in the removal of advanced glycation end product-modified proteins
physiological function
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altered activities of cathepsin D in the autistic brain may play an important role in the pathogenesis of autism
physiological function
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Cath-D stimulates cancer cell growth in an autocrine manner, and also plays a crucial paracrine role in the tumor microenvironment by stimulating fibroblast outgrowth and tumor angiogenesis
physiological function
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cathepsin D activity protects against development of type AA amyloid fibrils
physiological function
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cathepsin D is the main enzyme involved in the digestion of human hemoglobin
physiological function
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cathepsin D plays a critical role in cell proliferation
physiological function
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cathepsin D mediates a lysosomal pathway of macrophage apoptosis in pulmonary host defense against pneumococci
physiological function
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cathepsin D plays an important part in maintaining a normal skin barrier and is an important protein in chronic UV-damaged skin and skin barrier
physiological function
cathepsin D plays an important role in the innate immune response of grass carp
physiological function
cathepsin D plays key roles in immune response to exogenous pathogens and also acts as a digestive enzyme during the adaptation to a blood-feeding lifestyle
physiological function
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cathepsin D protects colorectal cancer cells from acetate-induced apoptosis through autophagy-independent degradation of damaged mitochondria
physiological function
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cathepsin D-induced caspase-8 activation represents a general mechanism to induce apoptosis in the absence of death receptor activation in a variety of immune and nonimmune cells
physiological function
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the enzyme translocates from the vacuole to the cytosol during acetic acid-induced apoptosis and is required for efficient mitochondrial degradation and for increased cell survival in response to this acid. The protective role of the enzyme in acetic acid-induced apoptosis depends on its catalytic activity and is independent of the yeast voltage-dependent anion channel Por1p but dependent on AAC proteins, the yeast adenine nucleotide translocator
physiological function
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mesenchymal stem cell homing towards cancer cells is increased by enzyme activity of cathepsin D
physiological function
the enzyme contributes to sea cucumber muscle autolysis
physiological function
the enzyme functions during metamorphosis
physiological function
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the enzyme is a key player in the development of hepatic inflammation and dyslipidemia
physiological function
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the enzyme is involved in the oxygen and glucose deprivation/reperfusion-induced apoptosis of astrocytes. Enzyme overexpression enhances cell apoptosis and the levels of apoptogenic proteins, including Bax and caspase-3
physiological function
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the enzyme plays a dual function in acetic acid-induced cell death depending on the genetic background
physiological function
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the enzyme plays a role in apoptosis during acute kidney injury
physiological function
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the enzyme plays a role in endothelial-pericyte interactions during alteration of the blood-retinal barrier in diabetic retinopathy
physiological function
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the enzyme plays an important immune role in Eriocheir sinensis to Spiroplasma eriocheiris challenge
physiological function
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the enzyme regulates cathepsin B activation and disease severity predominantly in inflammatory cells during experimental pancreatitis
physiological function
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the enzyme regulates tumor necrosis factor-related apoptosis-inducing ligand-induced cell death of MDA-MB-231 breast cancer cells
physiological function
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the major function of the enzyme is its involvement in general protein degradation and turnover within the lysosomal compartment. The enzyme plays a role in limited proteolysis of proteins regulating cell growth and/or tissue homeostasis, postnatal tissue homeostasis, neuronal ceroid lipofuscinosis, wound healing, epidermal differentiation and pathological conditions such as psoriasis, proliferation and regeneration in keratinocytes, processing of proteins involved in Alzheimer disease pathogenesis, post-partum cardiomyopathy resulting in heart failure, autism pathogenesis, innate immune responses and Parkinson disease, transport of phospholipids and cholesterol, and atherosclerotic lesions associated with proenzyme release from monocyte-derived macrophages
physiological function
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the presence of cathepsin D in the cytosol affects the inhibitory potency of stefin B, thus preventing the regulation of cysteine cathepsin activities in various biological processes
physiological function
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the enzyme translocates from the vacuole to the cytosol during acetic acid-induced apoptosis and is required for efficient mitochondrial degradation and for increased cell survival in response to this acid. The protective role of the enzyme in acetic acid-induced apoptosis depends on its catalytic activity and is independent of the yeast voltage-dependent anion channel Por1p but dependent on AAC proteins, the yeast adenine nucleotide translocator
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