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Information on EC 3.4.17.10 - carboxypeptidase E
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3.4.17.10 carboxypeptidase ESpecify your search results
Word Map
- 3.4.17.10
-
cytopathic
-
carbapenemase-producing
- enterobacteriaceae
- clostridium
- perfringens
- enterotoxin
- viruses
- carbapenemase
- pneumonia
-
electrode
- klebsiella
- neuropeptides
-
cloud
-
outbreak
-
preconcentration
-
carriage
-
swab
- enterobacterales
-
cytopathogenic
-
carba
- meropenem
-
voltammetric
-
polyelectrolyte
-
carbapenem-resistant
-
cardiogenic
-
blaoxa-48
- colistin
-
oxa-48-like
-
alpha-amidating
-
esbls
- enteroviruses
- imipenem
- vim
- ertapenem
- proinsulin
-
antibiotic-associated
- claudin-4
-
blakpc
-
tcid50
-
blandm
-
extended-spectrum
-
kpc-producing
- medicine
-
spiritual
- diagnostics
- blaimp
-
esbl-producing
-
parapneumonic
-
hodge
-
eucast
- biotechnology
- drug development
-
macconkey
-
stewardship
The enzyme appears in viruses and cellular organisms
Synonyms
cpe, carboxypeptidase e, carboxypeptidase h, metallocarboxypeptidase, enkephalin convertase, membrane-bound carboxypeptidase, egl-21, carboxypeptidase e/h, prohormone processing carboxypeptidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase E
carboxypeptidase, enkephalin precursor
-
-
-
-
cobalt stimulated chromaffin granule carboxypeptidase
-
-
-
-
CPE
CPE-NFalpha1
CPH
-
-
-
-
enkephalin convertase
enkephalin precursor carboxypeptidase
-
-
-
-
enkephalin-precursor endopeptidase
-
-
-
-
insulin granule-associated carboxypeptidase
-
-
-
-
membrane-bound carboxypeptidase
-
-
-
-
neurotrophic factor-alpha1
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
Prohormone processing carboxypeptidase
-
-
-
-
additional information
carboxypeptidase E
-
-
-
-
carboxypeptidase E
-
-
CPE
-
-
-
-
CPE
-
-
enkephalin convertase
-
-
-
-
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of C-terminal arginine or lysine residues from polypeptides
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
81876-95-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing
-
-
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing in pancreatic beta-cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
the enzyme is a sorting receptor for the regulated secretory pathway. The sorting receptor function of the enzyme necessitates its interaction with glycosphingolipid-cholesterol rafts at the trans-Golgi network, thereby anchoring it in position to bind to its prohormone cargo
-
?
additional information
?
-
-
the enzyme is a sorting receptor that directs the prohormone pro-opiomelanocortin to the regulated secretory pathway and is also a prohormone processing enzyme in neuro/endocrine cells
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
FMRFamide-like peptide (FLP) precursors
-
-
?
additional information
?
-
-
neuropeptide-like protein (NLP) precursors
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
the CPE reaction trims off C-terminal basic residues of peptides
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E, a prohormone processing exopeptidase and sorting receptor for the regulated secretory pathway, interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function. Mammalian cell lines coexpressing carboxypeptidase E and dopamine transporter exhibit increased dopamine transporter-mediated dopamine uptake activity compared to cells expressing dopamine transporter alone. Moreover, coexpression of an interfering dopamine transporter-carboxyl terminus minigene inhibit the effects of carboxypeptidase E on dopamine transporter. Functional changes caused by carboxypeptidase E could be attributed to enhanced dopamine transporter expression and subsequent increase in dopamine transporter cell surface localization, due to decreased dopamine transporter degradation. In addition, carboxypeptidase E association could reduce the phosphorylation state of dopamine transporter on serine residues, potentially leading to reduced internalization, thus stabilizing plasmalemmal dopamine transporter localization
-
-
?
additional information
?
-
-
CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
-
-
?
additional information
?
-
-
catalyzes the removal of C-terminal amino acids from proteins and peptides
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules, both proteins form the separate functional sorting complex by anchoring in the cholesterol-rich membranes of the secretory granules, overview, secretogranin III can funtionally compensate for CPEin enzyme-defective mutant mice
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
biosynthesis of neuropeptides and peptide hormones
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
biosynthesis of insulin in pancreatic beta-cells
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
C-terminal histidine is removed at a very slow rate
-
-
?
additional information
?
-
-
carboxypeptidase E interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function, carboxypeptidase E plays a role in the regulation of dopamine transporter trafficking and dopamine transporter-mediated dopamine uptake, which may provide a novel target in the treatment of dopamine-governed diseases such as drug addiction and obesity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing in pancreatic beta-cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
the enzyme is a sorting receptor for the regulated secretory pathway. The sorting receptor function of the enzyme necessitates its interaction with glycosphingolipid-cholesterol rafts at the trans-Golgi network, thereby anchoring it in position to bind to its prohormone cargo
-
?
additional information
?
-
-
the enzyme is a sorting receptor that directs the prohormone pro-opiomelanocortin to the regulated secretory pathway and is also a prohormone processing enzyme in neuro/endocrine cells
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
FMRFamide-like peptide (FLP) precursors
-
-
?
additional information
?
-
-
neuropeptide-like protein (NLP) precursors
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
-
-
?
additional information
?
-
-
catalyzes the removal of C-terminal amino acids from proteins and peptides
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules, both proteins form the separate functional sorting complex by anchoring in the cholesterol-rich membranes of the secretory granules, overview, secretogranin III can funtionally compensate for CPEin enzyme-defective mutant mice
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
biosynthesis of neuropeptides and peptide hormones
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
biosynthesis of insulin in pancreatic beta-cells
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
C-terminal histidine is removed at a very slow rate
-
-
?
additional information
?
-
-
carboxypeptidase E interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function, carboxypeptidase E plays a role in the regulation of dopamine transporter trafficking and dopamine transporter-mediated dopamine uptake, which may provide a novel target in the treatment of dopamine-governed diseases such as drug addiction and obesity
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
NiCl2
Zn2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
excessive secretogranin III leads to a decrease in CPE-bound proopiomelanocortin-derived intermediate molecules
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
allyl isothiocyanate
-
mRNA for carboxypeptidase E is transiently increased in the first 6 h, after which is decreased to below baseline levels, after intracolonically administration of allyl isothiocyanate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
metabolic parameters of wild-type, heterozygous and homozygeous enzyme-deficient mutant mice, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
5 - 6
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
-
pH 4: about 20% of activity maximum, pH 6.5: about 15% of activity maximum
additional information
additional information
-
rapid decline in activity at pH values above pH 5.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transiently expressed in mouse embryos from embryonic day 5.5 to postnatal day 1
brenda
-
specifically expressed in enteroendocrine cell of the murine colon and ileum
brenda
-
CPE expression occurs in gastrin synthesizing cells and in gastrin-somatostatin progenitor cells
brenda
-
present in some dendrites and nerve terminals, which contain storage vesicles
brenda
-
carboxypeptidase E is expressed in chicken thymus of both young (8-day-old) and older (17-week-old) chickens and in broilers and laying hens
brenda
additional information
-
after mild chronic restraint stress, CPE protein and mRNA are significantly elevated in the hippocampal CA3 region, compared to naive littermate
brenda
-
CPE-DELTAN expression is up-regulated in embryonic hippocampal neurons in response to dexamethasone treatment
brenda
-
neuroendocrine chromaffin cell, sympathoadrenal chromaffin cell, chromaffin granule
brenda
an N-terminal-truncated CPE/NF-alpha1 variant, a 40-kDa protein, is exclusively expressed in embryonic neurons
brenda
-
beta cells lacking the insulin receptor show a decreased expression of CPE. CPE protein expression is up-regulated upon insulin stimulation
brenda
the enzyme colocalizes with and interacts with human growth hormone in AtT20 pituitary cells
brenda
additional information
-
2 forms: soluble and membrane-bound are present in most tissues
brenda
additional information
-
gene expression analysis in lung tumor tissue, overview
brenda
additional information
-
no activity: rat liver, rat spleen, rat lung, rat kidney, rat mammary gland
brenda
additional information
-
2 forms: soluble and membrane-bound are present in most tissues
brenda
additional information
-
no expression in mature somatostatin cells and in the majority of serotonin cells
brenda
additional information
-
unprocessed pro-enzyme accumulates in cortical neurons after ischemia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with brain-derived neurotrophic factor, BDNF, vesicles
brenda
-
enkephalin-containing chromaffin vesicles in the adrenal medulla, the enzyme is sorted into the secretory pathway via its C-terminal domain
brenda
additional information
-
the enzyme is sorted into the secretory pathway via its C-terminal domain
brenda
-
anchored to secretory granules via a C-terminal transmembrane insertion. The membrane-binding domain of the enzyme must adopt an alpha-helical configuration to bind to lipids and the enzyme may require another integral membrane chaperone protein to insert through the lipid bilayer in a transmembrane fashion
brenda
-
secretory granule membrane derived from trans-Golgi network, associated with detergent-resistant lipid domains, or rafts, within secretory granule membranes
brenda
-
the enzyme is sorted into the secretory pathway via its C-terminal domain
brenda
the enzyme is produced from pro-carboxypeptidase E and exists in soluble and membrane forms
brenda
-
the enzyme is sorted into the secretory pathway via its C-terminal domain
brenda
the enzyme is produced from pro-carboxypeptidase E and exists in soluble and membrane forms
brenda
-
the enzyme is sorted into the secretory pathway via its C-terminal domain
brenda
-
membrane-associated via a C-terminal amphipathic sequence
brenda
-
chromaffin granules
brenda
-
from neural lobe pituitary and intermediate lobe pituitary
brenda
-
the enzyme binds specifically to cholesterol-rich secretory granule membranes competing with secretogranin III, excessive secretogranin III leads to a decrease in CPE-bound proopiomelanocortin-derived intermediate molecules
brenda
the enzyme is produced from pro-carboxypeptidase E and exists in soluble and membrane forms
-
brenda
the enzyme is produced from pro-carboxypeptidase E and exists in soluble and membrane forms
-
brenda
additional information
-
co-existence of chromogranin A and carboxypeptidase E in identical neuroendocrine cells in the thymus
-
brenda
additional information
-
subcellular localization of wild-type and mutant enzymes in the retina, overview
-
brenda
additional information
-
subcellular localization of wild-type and mutant enzymes in the retina, overview
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the amino acid sequence of carboxypeptidase E appears to be highly conserved among chicken, mouse, and human. The C-terminal sequence of carboxypeptidase E, which serves as an anchor to the membrane of secretory granules, is perfectly conserved between birds and mammals
malfunction
physiological function
malfunction
-
cpe -/- mice is used as a model of EEC dysfunction. Using this model it is shown that CPE exhibits a relevant for EEC function and intestinal homeostasis
malfunction
-
in Neuro 2a cells that lack CPE, PC1/3 and PC2, proglucagon co-localise with the Golgi marker p115 as determined by quantitative immunofluorescence microscopy. siRNA-mediated knockdown of CPE disrupts regulated secretion of glucagon from pancreatic-derived alphaTC1-6 cells, but not of GLP-1 from intestinal cell-derived GLUTag cells
malfunction
in two types of carboxypeptidase E mutant mice, Cpefat/Cpefat and Cpe knockout, loss of normal carboxypeptidase E leads to a lot of disorders, including diabetes, hyperproinsulinemia, low bone mineral density and deficits in learning and memory
malfunction
in two types of carboxypeptidase E mutant mice, Cpefat/Cpefat and Cpe knockout, loss of normal carboxypeptidase E leads to a lot of disorders, including diabetes, hyperproinsulinemia, low bone mineral density and deficits in learning and memory
physiological function
-
carboxypeptidase E is classically known as an exopeptidase that cleaves carboxy-terminal basic aminoacids from neuropeptide and peptide hormone intermediates resulting in the production of bioactive peptides inneuroendocrine cells. Carboxypeptidase E that is expressed in the nervous and endocrine systems plays multiple non-enzymatic roles in addition to being an exopeptidase The soluble form of carboxypeptidase E acts as a processing enzyme. The membrane-bound form of carboxypeptidase E serves as a sorting receptor for some proneuropeptides and pro-brain derived neurotrophic factor to target them into the regulated secretory pathway.The cytoplasmic tail of the transmembrane form of carboxypeptidase E is shown to be a key molecule in the anchoring of adrenocorticotropic hormone and brain derived neurotrophic factor vesicles to the microtubule-based transport system for post-Golgi delivery of the vesicles to the release site
physiological function
-
carboxypeptidase E mediates the effects of nitric oxide synthase 1 adaptor protein on dendrite morphology
physiological function
-
carboxypeptidase E plays a role in regulating proper dendritic patterning, especially dendritic pruning and spine formation that are necessary for appropriate synaptogenesis and the establishment of neuronal network
physiological function
-
carboxypeptidase E, a prohormone processing exopeptidase and sorting receptor for the regulated secretory pathway, interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function. Mammalian cell lines coexpressing carboxypeptidase E and dopamine transporter exhibit increased dopamine transporter-mediated dopamine uptake activity compared to cells expressing dopamine transporter alone. Moreover, coexpression of an interfering dopamine transporter-carboxyl terminus minigene inhibit the effects of carboxypeptidase E on dopamine transporter. Functional changes caused by carboxypeptidase E could be attributed to enhanced dopamine transporter expression and subsequent increase in dopamine transporter cell surface localization, due to decreased dopamine transporter degradation. In addition, carboxypeptidase E association could reduce the phosphorylation state of dopamine transporter on serine residues, potentially leading to reduced internalization, thus stabilizing plasmalemmal dopamine transporter localization
physiological function
glutamatergic and acetylcholine synaptic vesicles in the hypothalamus and chromaffin cell-derived PC12 cells employ the transmembrane carboxypeptidase E cytoplasmic tail to interact with gamma-adducin for recruiting synaptic vesicles to the active and/or pre-active zone to facilitate neurotransmitter release. Carboxypeptidase E is a mediator in the process, that mediates localization of synaptic vesicles to the pre-active zone. Carboxypeptidase E has a non-enzymatic role in the control of classical neurotransmitter release in specific neuron
physiological function
-
glutathione S-transferase pull-down and immunoprecipitation analyses indicate that contactin-associated protein 2 is associated with carboxypeptidase E in vitro and in vivo. Both contactin-associated protein 2 and carboxypeptidase E are expressed predominantly in the CNS. Immunohistochemical analysis reveals that both contactin-associated protein 2- and carboxypeptidase E-like immunoreactivities are found to co-localize in the apical dendrites and cell bodies of rat cortical neurons. In subcellular localization analysis, contactin-associated protein 2- and carboxypeptidase E-like immunoreactivities are co-migrated in the fractions of Golgi/ER. The membrane-bound form of carboxypeptidase E functions as a sorting receptor of prohormones in the trans-Golgi network. Carboxypeptidase E may be a key molecule to regulate contactin-associated protein 2 trafficking to the cell membrane
physiological function
the severity of the coronary atherosclerosis estimated by Gensini score is significantly influenced by the presence of the A2925G mutant and G2855A mutant of the carboxypeptidase E gene
physiological function
-
CPE acts extracellularly through activation of ERK and AKT signaling pathways to up-regulate expression of the anti-apoptotic protein BCL-2 to mediate neuroprotection of neurons during stress
physiological function
-
CPE can mediate neuroprotection of the hippocampal neurons during mild chronic restraint stress and may play an important role in maintaining allostasis
physiological function
-
CPE-DELTA neuroprotects neurons against glutamate neuroexcitotoxicity and H2O2-induced oxidative stress.CPE-DELTAN acts by increasing the transcription and secretion of fibroblast growth factor (FGF2)
physiological function
-
sorting of proglucagon to secretory granules is mediated by carboxypeptidase E
physiological function
overexpression of the secreted form of CPE is accompanied by differential regulation of mRNAs connected to the motility-associated networks, among others adhesion kinase FAK, p21-activated kinase PAK, cell division cycle 42 (Cdc42), integrin, STAT3 as well as TGF-beta. Especially SLUG is downregulated in sCPE-overexpressing glioma cells, paralleled by reduced expression of matrix-metalloproteinases (MMP) and, in consequence, by decreased cell migration. Expression of SLUG is regulated by ERK since inhibition of ERK reverted sCPE-mediated SLUG downregulation and enhanced cell motility. In a mouse glioma model, overexpression of the sectreted form of CPE significantly prolonges survival
physiological function
the enzyme cleaves C-terminal basic amino acids from prohormone intermediates to produce mature peptide hormones and neuropeptides in the endocrine and central nervous systems. It also plays a critical role in prohormone sorting and secretory vesicle transportation. The enzyme exerts multiple non-enzymatic physiological roles in maintaining normal central nervous system function and in neurodevelopment. This includes potent neuroprotective and anti-depressant activities, as well as stem cell differentiation functions. In addition, N-terminal truncated variants of the enzyme regulate expression of important neurodevelopmental genes
physiological function
the enzyme cleaves C-terminal basic amino acids from prohormone intermediates to produce mature peptide hormones and neuropeptides in the endocrine and central nervous systems. It also plays a critical role in prohormone sorting and secretory vesicle transportation. The enzyme exerts multiple non-enzymatic physiological roles in maintaining normal central nervous system function and in neurodevelopment. This includes potent neuroprotective and anti-depressant activities, as well as stem cell differentiation functions. In addition, N-terminal truncated variants of the enzyme regulate expression of important neurodevelopmental genes
physiological function
the enzyme is involved in proneuropeptide processing. It is also a neurotrophic factor (NF-a1) and has important roles in neuroprotection, stem cell differentiation, and neurite outgrowth, independent of enzymatic activity
physiological function
the enzyme is involved in the biosynthesis of a wide range of neuropeptides and peptide hormones in endocrine tissues, and in the nervous system. Membrane carboxypeptidase E mediates the targeting of prohormones to the regulated secretory pathway, while soluble carboxypeptidase E acts as an exopeptidase and cleaves C-terminal basic residues from peptide intermediates to generate bioactive peptides. Carboxypeptidase E also participates in protein internalization, vesicle transport and regulation of signaling pathways
physiological function
the enzyme is involved in the biosynthesis of a wide range of neuropeptides and peptide hormones in endocrine tissues, and in the nervous system. Membrane carboxypeptidase E mediates the targeting of prohormones to the regulated secretory pathway, while soluble carboxypeptidase E acts as an exopeptidase and cleaves C-terminal basic residues from peptide intermediates to generate bioactive peptides. Carboxypeptidase E also participates in protein internalization, vesicle transport and regulation of signaling pathways
physiological function
the enzyme plays a critical role in prohormone sorting and secretory vesicle transportation
physiological function
the enzyme plays a critical role in prohormone sorting and secretory vesicle transportation
physiological function
the enzyme plays a key role in sorting prohormones, such as pro-opiomelanocortin, to regulated secretory vesicles. Human growth hormone directly interacts with carboxypeptidase E
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53000
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
the 55 kDa proenzyme is processed to the 53 kDa mature protein
side-chain modification
glycoprotein
-
alterations in the glycosylation status of the enzyme during ischemia, unprocessed pro-enzyme accumulates in cortical neurons after ischemia
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R283W
-
naturally occurring genetic variant of the enzyme, the mutant shows altered kinetics, heat stability, and pH optimum, and a 50% reduced activity compared to the wild-type enzyme
S202P
additional information
S202P
-
enzyme-defective mutant CPEfat/fat mice show a point mutation in the coding region of the gene encoding the enzyme, and lack enzyme activity completely, which affects peptide processing the mutant mice
S202P
-
inactive mutant, mice without carboxypeptidase E activity are overweight
additional information
-
the polymorphisms 801 C to T and 847 C to T are explored
additional information
-
a spontaneous Cpefat/fat mutant strain produces an inactive enzyme, which results in diminished cell survival after ischemic stress in the brain in vivo and in neuronal cells in vitro, overview
additional information
-
enzyme-defective CPEfat mice show elevated levels of secretogranin III and chromogranin A in the pituitary compensating for the lacking CPE sorting function, overview
additional information
-
metabolic analysis of female and male heterozygous and homozygeous enzyme-deficient mutant mice, CPEfat/fat, in comparison to the wild-type mice, the mutant mice show reduced pro-islet amyloid polypeptide processing activity and reduced levels of PC2-chaperone protein 7B2 and prohormone invertase PC2, but not PC1/3, in beta cells, overview
additional information
-
mutant mice lacking the enzyme and mutant mice with defective enzymes, Cpefat/fat and Cpefat/+ mutants, show abnormal electroretinography responses, overview
additional information
an N-terminal-truncated CPE/NF-alpha1 variant, a 40-kDa protein, is exclusively expressed in embryonic neurons
additional information
-
an N-terminal-truncated CPE/NF-alpha1 variant, a 40-kDa protein, is exclusively expressed in embryonic neurons
additional information
-
mutant mice lacking the enzyme and mutant mice with defective enzymes, Cpefat/fat and Cpefat/+ mutants, show abnormal electroretinography responses, overview
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from brain to homogeneity by 4-aminobenzoyl affinity chromatography
-
native enzyme from pituitary to homogeneity from pituitary gland by 4-aminobenzoyl-Arg affinity chromatography with elution at pH 8.0
-
recombinant GST-fusion protein from Escherichia coli strain BL21(DE3) by glutathione affinity, native pro- or mature enzyme from AtT20 cells, best at pH 5.5 in presence of Ca2+ by GST-secretogranin III affinity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a cDNA library is constructed with polyA+ RNA isolated from the neural complex, EST sequences are determined, cluster ID 00509, longest cDNA clone for Ci-CPE ciad075c14, accession no. AK113574
-
a GST-tagged CPE tail fragment is generated using the pGEX4T-2 vector, furthermore the vectors pEGFP-1C, pDsRed2 and pCMV-Myc are used to generate GFP, RFP and Myc fusion proteins
-
CPE gene and total gene quantitative expression analysis in lung tumor tissue, detailed overview
-
CPE tail fragments are subcloned into pGEX4T-2, pEGFP-C1 and pDsRed2, full-length CPE cDNA is inserted into pDsRed-Express-N1
-
DNA and amino acid sequence determination, localization on chromosome 4, several naturally occurring genetic variants exist
-
HEK 293 T cells are transiently transfected with dopamine transporter or together with carboxypeptidase E, carboxypeptidase E interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function. Mammalian cell lines coexpressing carboxypeptidase E and dopamine transporter exhibit increased dopamine transporter-mediated dopamine uptake activity compared to cells expressing dopamine transporter alone. Coexpression of an interfering dopamine transporter carboxyl terminus minigene inhibit the effects of carboxypeptidase E on dopamine transporter. Functional changes caused by carboxypeptidase E could be attributed to enhanced dopamine transporter expression and subsequent increase in dopamine transporter cell surface localization, due to decreased dopamine transporter degradation. Carboxypeptidase E association could reduce the phosphorylation state of dopamine transporter on serine residues, potentially leading to reduced internalization, thus stabilizing plasmalemmal dopamine transporter localization
-
high level expression in insect cells using the baculovirus transfection system, the recombinant enzyme is indistinguishable from the native enzyme, expression in bacteria results in inactive enzyme
-
interaction of the recombinant enzyme with recombinnat eosinophil cationic protein in the yeast two-hybrid system via residues 318-387 of CPE, overview, expression of the enzyme fused to the activation domain of Gal4 in GH3 cells
-
N-terminal-truncated carboxypeptidase E/neurotrophic factor-alpha1 variants in embryonic mouse brain. It has an important, enzymatically independent role in the regulation of genes critical for neurodevelopment
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after mild chronic restraint stress, CPE protein and mRNA are significantly elevated in the hippocampal CA3 region, compared to naïve littermate
-
CPE protein expression is up-regulated by insulin stimulation in beta cells lacking the insulin receptor
-
CPE-DELTAN expression is up-regulated in embryonic hippocampal neurons in response to dexamethasone treatment
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
carboxypeptidase E is used in an in vitro system for the production of bioactive peptides
diagnostics
drug development
-
carboxypeptidase E plays a role in the regulation of dopamine transporter trafficking and dopamine transporter-mediated dopamine uptake, which may provide a novel target in the treatment of dopamine-governed diseases such as drug addiction and obesity
medicine
diagnostics
-
CPE serves as a marker for pulmonary endocrine tumor cells in the lung, enzyme expression correlates with a good prognosis, while expression of gamma-glutamyl hydrolase is correlated with a poor prognosis, overview
diagnostics
carboxypeptidase E is a prediction marker for tumor recurrence in early-stage hepatocellular carcinoma
diagnostics
N-terminal truncated carboxypeptidase E (CPEDELTAN) expression is associated with poor prognosis of lung adenocarcinoma. CPEDELTAN may present a molecular biomarker for predicting recurrence and metastasis of lung adenocarcinoma
medicine
-
the polymorphism 801 C to T in the carboxypeptidase E exon5 gene may contribiute to the angiographical characteristics of coronary atherosclerosis
medicine
carboxypeptidase E is a prediction marker for tumor recurrence in early-stage hepatocellular carcinoma
medicine
N-terminal truncated carboxypeptidase E (CPEDELTAN) expression is associated with poor prognosis of lung adenocarcinoma. CPEDELTAN may present a molecular biomarker for predicting recurrence and metastasis of lung adenocarcinoma
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fricker, L.D.
Carboxypeptidase E
Annu. Rev. Physiol.
50
309-321
1988
Bos taurus, Rattus norvegicus
brenda
Grimwood, B.G.; Plummer, T.H.; Tarentino, A.L.
Carboxypeptidase H. A regulatory peptide-processing enzyme produced by human hepatoma Hep G2 cells
J. Biol. Chem.
264
15662-15667
1989
Homo sapiens
brenda
Darby, N.J.; Fricker, L.D.; Maruthainar, K.; Smyth, D.G.
A study of the substrate specificity of carboxypeptidase H
Pept. Chem. Biol. (Proc. Am. Pept. Symp. ,10th Meeting Date 1987, Marshall, G. R. , ed. )
613-614
1988
Sus scrofa
-
brenda
Rossier, J.R.; Barres, E.; Hutton, J.C.; Bicknell, R.J.
Radiometric assay for carboxypeptidase H (EC 3.4.17.10) and other carboxypeptidase B-like enzymes
Anal. Biochem.
178
27-31
1989
Rattus norvegicus
brenda
Hook, V.Y.H.; Affolter, H.U.
Identification of zymogen and mature forms of human carboxypeptidase H. A processing enzyme for the synthesis of peptide hormones
FEBS Lett.
238
338-342
1988
Homo sapiens
brenda
Hook, V.Y.H.; LaGamma, E.F.
Product inhibition of carboxypeptidase H
J. Biol. Chem.
262
12583-12588
1987
Bos taurus, Rattus norvegicus
brenda
Davidson, H.W.; Hutton, J.C.
The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing
Biochem. J.
245
575-582
1987
Rattus norvegicus
brenda
Fricker, L.D.; Evans, C.J.; Esch, F.S.; Herbert, E.
Cloning and sequence analysis of cDNA for bovine carboxypeptidase E
Nature
323
461-464
1986
Bos taurus
brenda
Fricker, L.D.; Snyder, S.H.
Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules
Proc. Natl. Acad. Sci. USA
79
3886-3890
1982
Bos taurus
brenda
Fricker, L.D.; Snyder, S.H.
Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase
J. Biol. Chem.
258
10950-10955
1983
Bos taurus
brenda
Fricker, L.D.; Devi, L.
Comparison of a spectrophotometric, a fluorometric, and a novel radiometric assay for carboxypeptidase E (EC 3.4.17.10) and other carboxypeptidase B-like enzymes
Anal. Biochem.
184
21-27
1990
Sus scrofa
brenda
Fricker, L.D.; Das, B.; Angeletti, R.H.
Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10)
J. Biol. Chem.
265
2476-2482
1990
Bos taurus
brenda
Hook, V.Y.H.; Mezey, E.; Fricker, L.D.; Pruss, R.M.; Siegel, R.E.; Brownstein, M.J.
Immunochemical characterization of carboxypeptidase B-like peptide-hormone-processing enzyme
Proc. Natl. Acad. Sci. USA
82
4745-4749
1985
Bos taurus, Rattus norvegicus
brenda
Deddish, P.A.; Skidgel, R.A.; Erds, E.G.
Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)
Biochem. J.
261
289-291
1989
Homo sapiens
brenda
Juvvadi, S.; Fan, X.; Nagle, G.T.; Fricker, L.D.
Characterization of Aplysia carboxypeptidase E
FEBS Lett.
408
195-200
1997
Aplysia californica
brenda
Manser, E.; Fernandez, D.; Loo, L.; Goh, P.Y.; Monfries, C.; Hall, C.; Lim, L.
Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression and processing in vitro
Biochem. J.
267
517-525
1990
Homo sapiens
brenda
Christie, D.L.; Palmer, D.J.
Identification and characterization of glycoproteins after extraction of bovine chromaffin-granule membranes with lithium di-iodosalicylate. Purification of glycoprotein II from the soluble fraction
Biochem. J.
270
57-61
1990
Bos taurus
brenda
Rodriguez, C.; Brayton, K.A.; Brownstein, M.; Dixon, J.E.
Rat preprocarboxypeptidase H. Cloning, characterization, and sequence of the cDNA and regulation of the mRNA by corticotropin-releasing factor
J. Biol. Chem.
264
5988-5995
1989
Mus musculus, Rattus norvegicus
brenda
Stone, T.E.; Li, J.P.; Bernasconi, P.
Purification and characterization of the Manduca sexta neuropeptide processing enzyme carboxypeptidase E
Arch. Insect Biochem. Physiol.
27
193-203
1994
Aplysia californica, Manduca sexta
brenda
Kumar, G.K.
Neuropeptide processing enzymes of the carotid body. Biochemical and immunological characterization of carboxypeptidase activity
Adv. Exp. Med. Biol.
410
319-323
1996
Felis catus
brenda
Hook, V.Y.H.
Arginine and lysine product inhibition of bovine adrenomedullary carboxypeptidase H, a prohormone processing enzyme
Life Sci.
47
1135-1139
1990
Bos taurus
brenda
Dhanvantari, S.; Arnaoutova, I.; Snell, C.R.; Steinbach, P.J.; Hammond, K.; Caputo, G.A.; London, E.; Loh, Y.P.
Carboxypeptidase E, a prohormone sorting receptor, is anchored to secretory granules via a C-terminal transmembrane insertion
Biochemistry
41
52-60
2002
Bos taurus
brenda
Dhanvantari, S.; Loh, Y.P.
Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor
J. Biol. Chem.
275
29887-29893
2000
Bos taurus
brenda
Wu, C.M.; Chang, H.T.; Chang, M.D.
Membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
Biochem. J.
382
841-848
2004
Homo sapiens
brenda
Marzban, L.; Soukhatcheva, G.; Verchere, C.B.
Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in beta-cells
Endocrinology
146
1808-1817
2005
Mus musculus
brenda
Fricker, L.D.
Carboxypeptidase E
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press
2
840-844
2004
Aplysia sp., Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
brenda
Hougaard, D.M.; Larsson, L.I.
Carboxypeptidase E in rat antropyloric mucosa: distribution in progenitor and mature endocrine cell types
Histochem. Cell Biol.
121
55-61
2004
Rattus norvegicus
brenda
He, P.; Varticovski, L.; Bowman, E.D.; Fukuoka, J.; Welsh, J.A.; Miura, K.; Jen, J.; Gabrielson, E.; Brambilla, E.; Travis, W.D.; Harris, C.C.
Identification of carboxypeptidase E and gamma-glutamyl hydrolase as biomarkers for pulmonary neuroendocrine tumors by cDNA microarray
Hum. Pathol.
35
1196-1209
2004
Homo sapiens
brenda
Hosaka, M.; Watanabe, T.; Sakai, Y.; Kato, T.; Takeuchi, T.
Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules
J. Cell Sci.
118
4785-4795
2005
Mus musculus
brenda
Zhou, A.; Minami, M.; Zhu, X.; Bae, S.; Minthorne, J.; Lan, J.; Xiong, Z.G.; Simon, R.P.
Altered biosynthesis of neuropeptide processing enzyme carboxypeptidase E after brain ischemia: molecular mechanism and implication
J. Cereb. Blood Flow Metab.
24
612-622
2004
Mus musculus, Rattus norvegicus
brenda
Zhu, X.; Wu, K.; Rife, L.; Cawley, N.X.; Brown, B.; Adams, T.; Teofilo, K.; Lillo, C.; Williams, D.S.; Loh, Y.P.; Craft, C.M.
Carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
J. Neurochem.
95
1351-1362
2005
Mus musculus, Mus musculus C57BL/6
brenda
Ozawa, A.; Cai, Y.; Lindberg, I.
Production of bioactive peptides in an in vitro system
Anal. Biochem.
366
182-189
2007
Homo sapiens
brenda
Arolas, J.L.; Vendrell, J.; Aviles, F.X.; Fricker, L.D.
Metallocarboxypeptidases: emerging drug targets in biomedicine
Curr. Pharm. Des.
13
349-366
2007
Mammalia
brenda
Singh, U.; Yu, Y.; Kalinina, E.; Konno, T.; Sun, T.; Ohta, H.; Wakayama, T.; Soares, M.J.; Hemberger, M.; Fundele, R.H.
Carboxypeptidase E in the mouse placenta
Differentiation
74
648-660
2006
Mus musculus
brenda
Fricker, L.D.
Neuropeptidomics to study peptide processing in animal models of obesity
Endocrinology
148
4185-4190
2007
Mus musculus
brenda
Sekiguchi, T.; Kawashima, T.; Satou, Y.; Satoh, N.
Further EST analysis of endocrine genes that are preferentially expressed in the neural complex of Ciona intestinalis: receptor and enzyme genes associated with endocrine system in the neural complex
Gen. Comp. Endocrinol.
150
233-245
2007
Ciona intestinalis
brenda
Husson, S.J.; Janssen, T.; Baggerman, G.; Bogert, B.; Kahn-Kirby, A.H.; Ashrafi, K.; Schoofs, L.
Impaired processing of FLP and NLP peptides in carboxypeptidase E (EGL-21)-deficient Caenorhabditis elegans as analyzed by mass spectrometry
J. Neurochem.
102
246-260
2007
Caenorhabditis elegans
brenda
Lim, J.; Berezniuk, I.; Che, F.Y.; Parikh, R.; Biswas, R.; Pan, H.; Fricker, L.D.
Altered neuropeptide processing in prefrontal cortex of Cpe (fat/fat) mice: implications for neuropeptide discovery
J. Neurochem.
96
1169-1181
2006
Mus musculus
brenda
Wegrzyn, J.; Lee, J.; Neveu, J.M.; Lane, W.S.; Hook, V.
Proteomics of neuroendocrine secretory vesicles reveal distinct functional systems for biosynthesis and exocytosis of peptide hormones and neurotransmitters
J. Proteome Res.
6
1652-1665
2007
Bos taurus
brenda
Park, J.J.; Cawley, N.X.; Loh, Y.P.
Carboxypeptidase E cytoplasmic tail-driven vesicle transport is key for activity-dependent secretion of peptide hormones
Mol. Endocrinol.
22
989-1005
2008
Mus musculus
brenda
Kimball, E.S.; Prouty, S.P.; Pavlick, K.P.; Wallace, N.H.; Schneider, C.R.; Hornby, P.J.
Stimulation of neuronal receptors, neuropeptides and cytokines during experimental oil of mustard colitis
Neurogastroenterol. Motil.
19
390-400
2007
Mus musculus
brenda
Billova, S.; Galanopoulou, A.S.; Seidah, N.G.; Qiu, X.; Kumar, U.
Immunohistochemical expression and colocalization of somatostatin, carboxypeptidase-E and prohormone convertases 1 and 2 in rat brain
Neuroscience
147
403-418
2007
Rattus norvegicus
brenda
Wang, J.; Zhang, Y.; Yang, Z.J.; Zhu, T.B.; Wang, L.S.; Chen, B.; Cao, K.J.; Huang, J.; Ma, W.Z.; Jia, E.Z.
Association of human carboxypeptidase E exon5 gene polymorphisms with angiographical characteristics of coronary atherosclerosis in a Chinese population
Acta Pharmacol. Sin.
29
736-744
2008
Homo sapiens
brenda
Woronowicz, A.; Koshimizu, H.; Chang, S.Y.; Cawley, N.X.; Hill, J.M.; Rodriguiz, R.M.; Abebe, D.; Dorfman, C.; Senatorov, V.; Zhou, A.; Xiong, Z.G.; Wetsel, W.C.; Loh, Y.P.
Absence of carboxypeptidase E leads to adult hippocampal neuronal degeneration and memory deficits
Hippocampus
18
1051-1063
2008
Mus musculus
brenda
Park, J.J.; Cawley, N.X.; Loh, Y.P.
A bi-directional carboxypeptidase E-driven transport mechanism controls BDNF vesicle homeostasis in hippocampal neurons
Mol. Cell. Neurosci.
39
63-73
2008
Rattus norvegicus
brenda
Zhang, X.; Zhu, J.; Loh, Y.P.; Berghman, L.R.
Carboxypeptidase E, an essential element of the regulated secretory pathway, is expressed and partially co-localized with chromogranin A in chicken thymus
Cell Tissue Res.
337
371-379
2009
Gallus gallus
brenda
Koshimizu, H.; Senatorov, V.; Loh, Y.P.; Gozes, I.
Neuroprotective protein and carboxypeptidase E
J. Mol. Neurosci.
39
1-8
2009
Mus musculus
brenda
Oiso, S.; Takeda, Y.; Futagawa, T.; Miura, T.; Kuchiiwa, S.; Nishida, K.; Ikeda, R.; Kariyazono, H.; Watanabe, K.; Yamada, K.
Contactin-associated protein (Caspr) 2 interacts with carboxypeptidase E in the CNS
J. Neurochem.
109
158-167
2009
Homo sapiens
brenda
Lou, H.; Park, J.J.; Cawley, N.X.; Sarcon, A.; Sun, L.; Adams, T.; Peng Loh, Y.
Carboxypeptidase E cytoplasmic tail mediates localization of synaptic vesicles to the pre-active zone in hypothalamic presynaptic terminals
J. Neurochem.
114
886-896
2010
Mus musculus (Q00493)
brenda
Woronowicz, A.; Cawley, N.X.; Chang, S.Y.; Koshimizu, H.; Phillips, A.W.; Xiong, Z.G.; Loh, Y.P.
Carboxypeptidase E knockout mice exhibit abnormal dendritic arborization and spine morphology in central nervous system neurons
J. Neurosci. Res.
88
64-72
2010
Mus musculus
brenda
Carrel, D.; Du, Y.; Komlos, D.; Hadzimichalis, N.M.; Kwon, M.; Wang, B.; Brzustowicz, L.M.; Firestein, B.L.
NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway
J. Neurosci.
29
8248-8258
2009
Rattus norvegicus
brenda
Jia, E.; Wang, J.; Yang, Z.; Zhu, T.; Wang, L.; Wang, H.; Li, C.; Chen, B.; Cao, K.; Huang, J.; Ma, W.
Association of the mutation for the human carboxypeptidase e gene exon 4 with the severity of coronary artery atherosclerosis
Mol. Biol. Rep.
36
245-254
2009
Homo sapiens (P16870), Homo sapiens
brenda
Zhang, H.; Li, S.; Wang, M.; Vukusic, B.; Pristupa, Z.B.; Liu, F.
Regulation of dopamine transporter activity by carboxypeptidase E
Mol. Brain
2
10
2009
Homo sapiens, synthetic construct
brenda
Murthy, S.R.; Thouennon, E.; Li, W.S.; Cheng, Y.; Bhupatkar, J.; Cawley, N.X.; Lane, M.; Merchenthaler, I.; Loh, Y.P.
Carboxypeptidase E protects hippocampal neurons during stress in male mice by up-regulating prosurvival BCL2 protein expression
Endocrinology
154
3284-3293
2013
Mus musculus
brenda
Kumar, S.; Tomar, A.K.; Singh, S.; Gill, K.; Dey, S.; Singh, S.; Yadav, S.
Heparin binding carboxypeptidase E protein exhibits antibacterial activity in human semen
Int. J. Biol. Macromol.
64
319-327
2014
Homo sapiens
brenda
McGirr, R.; Guizzetti, L.; Dhanvantari, S.
The sorting of proglucagon to secretory granules is mediated by carboxypeptidase E and intrinsic sorting signals
J. Endocrinol.
217
229-240
2013
Homo sapiens
brenda
Cheng, Y.; Cawley, N.; Loh, Y.
Carboxypeptidase E/NFalpha1: A New Neurotrophic Factor against Oxidative Stress-Induced Apoptotic Cell Death Mediated by ERK and PI3-K/AKT Pathways
PLoS ONE
8
e71578
2013
Mus musculus
brenda
Baer, F.; Foeh, B.; Pagel, R.; Schroeder, T.; Schlichting, H.; Hirose, M.; Lemcke, S.; Klinger, A.; Koenig, P.; Karsten, C.M.; Buening, J.; Lehnert, H.; Fellermann, K.; Ibrahim, S.M.; Sina, C.
Carboxypeptidase E modulates intestinal immune homeostasis and protects against experimental colitis in mice
PLoS ONE
9
e102347
2014
Mus musculus
brenda
Qin, X.Y.; Cheng, Y.; Murthy, S.R.; Selvaraj, P.; Loh, Y.P.
carboxypeptidase E-DELTAN, a neuroprotein transiently expressed during development protects embryonic neurons against glutamate neurotoxicity
PLoS ONE
9
e112996
2014
Mus musculus
brenda
Liew, C.W.; Assmann, A.; Templin, A.T.; Raum, J.C.; Lipson, K.L.; Rajan, S.; Qiang, G.; Hu, J.; Kawamori, D.; Lindberg, I.; Philipson, L.H.; Sonenberg, N.; Goldfine, A.B.; Stoffers, D.A.; Mirmira, R.G.; Urano, F.; Kulkarni, R.N.
Insulin regulates carboxypeptidase E by modulating translation initiation scaffolding protein eIF4G1 in pancreatic beta cells
Proc. Natl. Acad. Sci. USA
111
E2319-E2328
2014
Mus musculus
brenda
Ji, L.; Wu, H.T.; Qin, X.Y.; Lan, R.
Dissecting carboxypeptidase E properties, functions and pathophysiological roles in disease
Endocr. Connect.
6
R18-R38
2017
Homo sapiens (P16870), Mus musculus (Q00493)
brenda
Xiao, L.; Yang, X.; Sharma, V.K.; Loh, Y.P.
Cloning, gene regulation, and neuronal proliferation functions of novel N-terminal-truncated carboxypeptidase E/neurotrophic factor-alphaIl variants in embryonic mouse brain
FASEB J.
33
808-820
2019
Mus musculus (Q00493), Mus musculus
brenda
Xiao, L.; Yang, X.; Loh, Y.P.
Neurotrophic, gene regulation, and cognitive functions of carboxypeptidase E-neurotrophic factor-alpha1 and its variants
Front. Neurosci.
13
243
2019
Homo sapiens (P16870), Mus musculus (Q00493)
brenda
Armento, A.; Ilina, E.I.; Kaoma, T.; Muller, A.; Vallar, L.; Niclou, S.P.; Krueger, M.A.; Mittelbronn, M.; Naumann, U.
Carboxypeptidase E transmits its anti-migratory function in glioma cells via transcriptional regulation of cell architecture and motility regulating factors
Int. J. Oncol.
51
702-714
2017
Mus musculus (Q00493), Mus musculus
brenda
Mizutani, A.; Inoko, H.; Tanaka, M.
Carboxypeptidase E, identified as a direct interactor of growth hormone, is important for efficient secretion of the hormone
Mol. Cells
39
756-761
2016
Homo sapiens (P16870), Homo sapiens
brenda
Sun, J.; Meng, D.; Li, L.; Tian, X.; Jia, Y.; Wang, H.; Yu, H.; Sun, T.; Qu, A.; Shen, H.; Bao, J.; Zhang, G.
N-terminal truncated carboxypeptidase E expression is associated with poor prognosis of lung adenocarcinoma
Oncol. Lett.
12
4659-4664
2016
Homo sapiens (P16870), Homo sapiens
brenda
Huang, S.F.; Wu, H.D.; Chen, Y.T.; Murthy, S.R.; Chiu, Y.T.; Chang, Y.; Chang, I.C.; Yang, X.; Loh, Y.P.
Carboxypeptidase E is a prediction marker for tumor recurrence in early-stage hepatocellular carcinoma
Tumour Biol.
37
9745-9753
2016
Homo sapiens (P16870), Homo sapiens
brenda
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