3.4.17.22: metallocarboxypeptidase D
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For detailed information about metallocarboxypeptidase D, go to the full flat file.
Word Map on EC 3.4.17.22
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3.4.17.22
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nanoparticles
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agnps
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gold
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nitrate
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film
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fabric
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plasmonic
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electrode
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raman
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colloid
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staphylococcus
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aureus
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copper
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devices
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uv-vis
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impregnation
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nanostructures
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dress
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nanocomposite
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electrochemical
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fiber
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nanomaterials
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glass
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fourier
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grain
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infrared
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spherical
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bactericidal
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burn
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autoradiograph
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wavelength
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graphene
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mercury
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nanoscale
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teeth
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transparent
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silicon
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print
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biocompatibility
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nucleolar
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porous
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immerse
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titanium
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biomedical
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self-assembled
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medicine
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nanotube
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nanocrystals
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disinfect
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tunable
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dentin
- 3.4.17.22
- nanoparticles
-
agnps
- gold
- nitrate
-
film
-
fabric
-
plasmonic
-
electrode
-
raman
-
colloid
- staphylococcus
- aureus
- copper
- devices
-
uv-vis
-
impregnation
-
nanostructures
-
dress
-
nanocomposite
-
electrochemical
- fiber
-
nanomaterials
-
glass
-
fourier
- grain
-
infrared
-
spherical
-
bactericidal
- burn
-
autoradiograph
-
wavelength
-
graphene
- mercury
-
nanoscale
- teeth
-
transparent
-
silicon
-
print
-
biocompatibility
-
nucleolar
-
porous
-
immerse
-
titanium
-
biomedical
-
self-assembled
- medicine
-
nanotube
-
nanocrystals
-
disinfect
-
tunable
- dentin
Reaction
releases C-terminal Arg and Lys from polypeptides =
Synonyms
Carboxypeptidase D, carboxypeptidase-D, CPD, CPD-N, DCPD, duck carboxypeptidase D, gp180, metallocarboxypeptidase-D, More, p170, silver, svr
ECTree
3.4.17.22 metallocarboxypeptidase DAdvanced search results
results (
results (Source Tissue
Source Tissue on EC 3.4.17.22 - metallocarboxypeptidase D
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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it is demonstrated that CpD is up-regulated by TGF-beta in murine macrophage cell lines ANA-1 and RAW 264.7 but HepG2 cells - cells not primarily associated with innate immune responses- show only minimal regulation of CpD by TGF-beta
additional information
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ACTH-immunreactive cells outside clustered small cell island (CSCI) show a strong carboxypeptidase D immunoreactivity, whereas ACTH-immunreactive cells in clustered small cell island show uniformly weak reactivity
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following prolonged culture of primary hepatocytes, duck carboxypeptidase D expression but not enzyme expression is diminished, which impairs effective duck hepatitis B virus infection
CPD is greatly and selectively down regulated in duck hepatitis B virus infected primary hepatocytes
CPD is greatly and selectively down regulated in duck hepatitis B virus infected livers
it is demonstrated that CpD is up-regulated by TGF-beta in CD14 + human blood monocytes
Cpd and CPE are strictly co-localized in the mouse placenta from late mid-gestation to term. While there is no strict overlap between Cpe and Cpd transcripts at the early developmental stages, E8 and E10, from E12 onwards there is no obvious difference in the expression patterns of the two genes. Just like Cpe, Cpd is expressed primarily in decidua and in chorionic plate and yolk sac, with weak expression in the labyrinth. At E18, Cpd is expressed at a level higher than Cpe. In interspecies hybrid placental dysplasia placentas, the expression of Cpd overlapps with that of Cpe. There is no difference in the pattern of expression of Cpd in wild-type and fat placentas at E18. Strong expression in decidua and yolk sac, but weak and diffuse expression in the labyrinth
additional information
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CpD is significantly downregulated in CD14 positive cells isolated from patients with rheumatoid arthritis, Takayasus arteritis, multiple sclerosis, systemic lupus erythematosus as compared to healthy controls
additional information
CpD is significantly downregulated in CD14 positive cells isolated from patients with rheumatoid arthritis, Takayasus arteritis, multiple sclerosis, systemic lupus erythematosus as compared to healthy controls
additional information
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in ACTH-immunoreactive cells outside clustered small cell islands, intermediate/strong carboxypeptidase D immunoreactivity. Within clustered small cell islands and basophil invasion uniformly weak reactivity and common patterns for carboxypeptidase D
