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Information on EC 3.4.24.11 - neprilysin and Organism(s) Rattus norvegicus and UniProt Accession P07861
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- 3.4.24.11
- angiotensin
-
natriuretic
- alzheimer
-
angiotensin-converting
- phosphoramidon
- atrial
-
amyloid
- thiorphan
- cardiovascular
- hypertension
- bradykinin
- neuropeptides
- aminopeptidase
-
ejection
- airway
- anp
- ventricular
-
blocker
- captopril
- endothelins
-
opioids
- metallopeptidase
- tachykinins
-
renin-angiotensin
- hf
- valsartan
- enalapril
-
renin-angiotensin-aldosterone
- neurokinin
-
vasoactive
-
endothelin-converting
-
hfref
- naloxone
-
insulin-degrading
- bestatin
- kinin
-
diuretic
-
3.4.15.1
-
lily
-
aceis
- met-enkephalin
-
bronchoconstriction
- angioedema
- amastatin
-
angiotensin-1-7
-
kininase
- lisinopril
-
nt-probnp
- medicine
-
bronchoconstrictors
- pharmacology
- analysis
- molecular biology
-
angiotensin-receptor
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'
Synonyms
neprilysin, neutral endopeptidase, enkephalinase, calla, endopeptidase-24.11, neutral endopeptidase 24.11, common acute lymphoblastic leukemia antigen, nep 24.11, nep/cd10, abeta-degrading enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
antigen, CALLA (common acute lymphoblastic leukemia-associated)
-
-
-
-
CALLA
-
-
-
-
CALLA (common acute lymphoblastic leukemia-associated) antigens
-
-
-
-
CALLA antigen
-
-
-
-
CALLA glycoproteins
-
-
-
-
CD10
-
-
-
-
common acute lymphoblastic leukemia-associated antigens
-
-
-
-
Common acute lymphocytic leukemia antigen
-
-
-
-
Endopeptidase-2
-
-
-
-
endopeptidase-24.11
-
-
-
-
enkephalinase
glycoprotein, CALLA
-
-
-
-
kidney-brush-border neutral endopeptidase
-
-
-
-
kidney-brush-border neutral peptidase
-
-
-
-
kidney-brush-border neutral proteinase
-
-
-
-
membrane metalloendopeptidase
-
-
-
-
NEP
neutral endopeptidase
neutral endopeptidase 24.11
-
-
-
-
neutral metallendopeptidase
-
-
-
-
peptidase, endo-
-
-
-
-
peptidase, membrane metalloendo-
-
-
-
-
enkephalinase
-
-
-
-
NEP
-
-
-
-
neutral endopeptidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
82707-54-8
-
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
glutaryl-Ala-Ala-Phe-4-methoxy-2-naphthylamide + H2O
glutaryl-Ala-Ala + Phe-4-methoxy-2-naphthylamide
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
amyloid beta peptide Abeta42 + H2O
?
-
the peptide primarily undergoes degradation by NEP in vivo in the brain
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
-
-
-
?
D-Ala2-Leu5-enkephalin + H2O
Tyr-D-Ala-Gly + Phe-Leu
-
i.e. Tyr-D-Ala-Gly-Phe-Leu
-
-
?
glutaryl-Gly-Gly-Phe-2-naphthylamide + H2O
glutaryl-Gly-Gly-Phe + 2-naphthylamine
-
-
-
-
?
hippuryl-Arg-Arg-Ala-2-naphthylamide + H2O
hippuryl-Arg-Arg + Ala-2-naphthylamide
-
-
-
-
?
hippuryl-Arg-Arg-Leu-2-naphthylamide + H2O
hippuryl-Arg-Arg + Leu-2-naphthylamide
-
-
-
-
?
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O
His-Lys-Thr-Asp-Ser + Phe-Val-Gly + Leu-Met-NH2
-
-
-
-
?
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Ala + Phe-4-methylcoumarin 7-amide
-
-
-
?
Tyr-Gly-Gly-Phe-Met + H2O
Tyr-Gly-Gly + Phe-Met
-
i.e. methionine enkephalin
-
-
?
Atrial natriuretic factor + H2O
?
-
dominant enzyme in the hydrolysis of atrial natriuretic factor
-
-
?
additional information
?
-
-
the enzyme is the major inactivator of enkephalin in brain
-
-
?
additional information
?
-
-
the enzyme may participate in the regulation of blood pressure and water and sodium excretion through inactivation of kinins
-
-
?
additional information
?
-
-
in sepsis, the local concentration and action of adrenomedullin in tissue may be differentially regulated by NEP
-
-
?
additional information
?
-
-
neutral endopeptidase inhibition has natriuretic and aquaretic actions in cirrhosis without any effect on blood pressure and kidney perfusion due to a significant overexpression of thgis enzyme in renal cortex
-
-
?
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
amyloid beta peptide Abeta42 + H2O
?
-
the peptide primarily undergoes degradation by NEP in vivo in the brain
-
-
?
Atrial natriuretic factor + H2O
?
-
dominant enzyme in the hydrolysis of atrial natriuretic factor
-
-
?
additional information
?
-
-
the enzyme is the major inactivator of enkephalin in brain
-
-
?
additional information
?
-
-
the enzyme may participate in the regulation of blood pressure and water and sodium excretion through inactivation of kinins
-
-
?
additional information
?
-
-
in sepsis, the local concentration and action of adrenomedullin in tissue may be differentially regulated by NEP
-
-
?
additional information
?
-
-
neutral endopeptidase inhibition has natriuretic and aquaretic actions in cirrhosis without any effect on blood pressure and kidney perfusion due to a significant overexpression of thgis enzyme in renal cortex
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-phenethylphosphonyl-L-leucyl-L-tryptophan
NPLT, synthesis of the phosphoramidon derivative with enhanced permeability into the skin that shows inability to inhibit type I and type IV collagenase, but inhibits fibroblast elastase
AHU-377
-
LCZ696 comprises molecular moieties of valsartan, and of the NEP inhibitor prodrug AHU377 ((2R,4S)-5-biphenyl-4-yl-5-(3-carboxy-propionylamino)-2-methyl-pentanoic acid ethyl ester) (1:1 molar ratio). Oral administration of LCZ696 causes dose-dependent increases in atrial natriuretic peptide immunoreactivity due to NEP inhibition in Sprague-Dawley rats and provides sustained, dose-dependent blood pressure reductions in hypertensive double-transgenic rats
amyloid beta
-
infusion with amyloid beta(25-35) induces decrease of somatostatin-like immunoreactive content, somatostatin mRNA levels, phosphorylated-cAMP-response element binding protein CREB content and neprilysin levels
-
candoxatrilat
-
application restores vagal reflex bradycardia in old rats to levels similar to those in young neutral endopeptidase inhibitor-treated rats
Leu5-enkephalin
-
hydrolysis of succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
Met5-enkephalin
-
hydrolysis of succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
N-[N-[1(5)-carboxy-3-(4-hydroxyphenyl)propyl]-(5)-phenylalanyl]-(5)-isoserine
-
-
SCH48446
-
i.e. the diiodo analog of N-[N-[1(5)-carboxy-3-(4-hydroxyphenyl)propyl]-(5)-phenylalanyl]-(5)-isoserine
phosphoramidon
-
neprilysin inhibition potentiates substance P-mediated neutrophil oxygen radical production and may promote other inflammatory activities during magnesium deficiency. Magnesium deficiency plus treatment with phosphoramidon reduces neprilysin activity by 48%, phosphoramidon or magnesium deficiency alone only reduce its activity by 26% and 15%, respectively
phosphoramidon
-
the inhibitor induces a dramatic increase in amyloid-beta peptide levels
thiorphan
-
plasma and lung A-type natriuretic peptide levels in rats treated with lipopolysaccharide are significantly higher than those in the control group, but are significantly decreased by thiorphan administration. Natriuretic peptide receptor-A mRNA levels do not differ significantly among the groups. Natriuretic peptide receptor-C mRNA levels in animals treated with lipopolysaccharide plus thiorphan group are significantly higher than those in the other groups
thiorphan
-
the inhibitor induces a dramatic increase in amyloid-beta peptide levels
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
androgen
-
androgens positively regulate neural expression of neprilysin in adult male rats
-
dihydrotestosterone
-
induces a time-dependent increase in neprilysin expression. Dihydrotestosterone also significantly decreases levels of amyloid beta in androgen receptor-expressing cells transfected with amyloid precursor protein, but does not affect levels of either full-length or non-amyloidogenic, soluble amyloid precursor protein. The dihydrotestosterone-induced decrease of amyloid beta is blocked by pharmacological inhibition of neprilysin. The dihydrotestosterone-mediated increase in neprilysin expression and decrease in amyloid beta levels are not observed in rat pheochromocytoma cell 12 lacking androgen receptor and blocked in androgen receptor-expressing cells by the antagonists, cyproterone acetate and flutamide
minocycline
-
minocycline abrogates the amyloid beta(25-35)-induced decrease of somatostatin-like immunoreactive content, somatostatin mRNA levels, phosphorylated-cAMP-response element binding protein CREB content and neprilysin levels. Minocycline alone enhances these targets
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
six-week intermittent hypoxia increases NEP expression and activity, selectively in temporal cortex, but not in the hippocampus and frontal cortex. The increase in NEP activity and expression is reverted followed by two weeks recovery in normoxia
extracellular matrix, dermal papilla, and follicular epithelium
the enzyme activity in the skin is elevated at early anagen, and decreased during catagen to telogen of the hair cycle
-
tissue NEP activity and its protein and mRNA expression are lower in the late phase of the septic shock compared to the early phase of the shock and the control
-
a large fraction of the enzyme is localized on intrinsic striatal neurons
-
tissue NEP activity and its protein and mRNA expression are lower in the late phase of the septic shock compared to the early phase of the shock and the control
-
tissue NEP activity and its protein and mRNA expression are lower in the late phase of the septic shock compared to the early phase of the shock and the control
additional information
expression and activity of NEP in cognitive-related brain structures of rats submitted to chronic intermittent hypoxia (CIH)
-
in globus pallidus and substantia nigra much of the enzyme is associated with presynaptic nerve terminals originating from efferent striatal neurons
-
highest activity in choroid plexus, substantia nigra, caudate putamen, globus pallidus, olfactory tubercle, nucleus accumbens. Moderate activity in amygdala, interpenducular nucleus, molecular layer of the cerebellum, periaqueductal gray matter, and the hippocampus
-
enzyme in sustantia nigra and globus pallidus is localized on nerve terminals originating from neurones in the caudate putamen
-
estrogen regulates neprilysin activity in brain. Ovariectomy leads to a 30% decrease in neprilysin activity at 45 or 85 days, but not 21 days, post surgery
-
ethanol induces a transitory increase in NEP activities in the frontal cortex and ventral tegmental area, and in the nucleus accumbens
-
no significant change in NEP activity and its protein and mRNA expression between late phase of the septic shock compared to the early phase of the shock and the control
-
tissue NEP activity and its protein and mRNA expression are lower in the late phase of the septic shock compared to the early phase of the shock and the control
-
androgens positively regulate neural expression of neprilysin in adult male rats
-
chromatin immunoprecipitation analysis demonstrates amyloid precursor protein binding to tht NEP promoter in primary neurons
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme possesses a single transmembrane spanning domain near the N-terminal of the molecule, the active site is located extracellularly, the N-terminal transmembrane region anchors the protein in the membranes, the majority of the protein, including the carboxy terminus is extracellular
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
-
neprilysin is a zinc metalloendopeptidase belonging to the M13 family
malfunction
-
application of inhibitors to NEP in rat brain produced dramatic elevations of endogenous amyloid beta peptide resulting in plaque deposition
metabolism
-
neprilysin-2 (NEP2), a NEP-like endopeptidase, cooperates with neprilysin (NEP) to control amyloid-beta peptide levels in the brain
physiological function
-
inhibition of NEP by the opiorphin homologs influence the physiology of a wide variety of tissues by causing extended binding time of peptide agonists to their receptors such as G-protein-coupled receptors (GPCRs)
physiological function
the role of neprilysin in regulating the hair cycle, a cyclic process of growing, regressing and resting phases, i.e. anagen, catagen, and telogen, respectively. The enzyme degrades elastin, which is associated with skin elasticity
physiological function
neprilysin (NEP) is responsible for degrading several substrates related to cognition
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NEP_RAT
750
1
85795
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H583F
H587F
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
six-week intermittent hypoxia increases NEP expression and activity, selectively in temporal cortex, but not in the hippocampus and frontal cortex. The increase in NEP activity and expression is reverted followed by two weeks recovery in normoxia
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
impaired cardiopulmonary vagal reflex control of heart rate is a feature of normal aging, and this deficit may be ameliorated by either atrium natriuretic peptide infusion or chronic neutral endopeptidase inhibition
pharmacology
-
inhibitor thiorphan might be effective for reducing elevated A-type natriuretic peptide levels in sepsis. Plasma and lung A-type natriuretic peptide levels in rats treated with lipopolysaccharide are significantly higher than those in the control group, but are significantly decreased by thiorphan administration. Natriuretic peptide receptor-A mRNA levels do not differ significantly among the groups. Natriuretic peptide receptor-C mRNA levels in animals treated with lipopolysaccharide plus thiorphan group are significantly higher than those in the other groups
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stephenson, S.L.; Kenny, A.J.
The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme endopeptidase-2 and by rat microvillar membranes
Biochem. J.
255
45-51
1988
Rattus norvegicus
Danilewicz, J.C.; Barclay, P.L.; Barnish, I.T.; Brown, D.; Campbell, S.F.; James, K.; Samuels, G.M.R.; Terrett, N.K.; Wythes, M.J.
UK-69,578, a novel inhibitor of EC 3.4.24.11 which increases endogenous ANF levels and is natriuretic and diuretic
Biochem. Biophys. Res. Commun.
164
58-65
1989
Rattus norvegicus
Erds, E.G.; Skidgel, R.A.
Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones
FASEB J.
3
145-151
1989
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Kanazawa, M.; Casley, D.J.; Sybertz, E.J.; Haslanger, M.F.; Johnston, C.I.
Localization and characterization of neutral metalloendopeptidase (EC 3.4.24.11), the degradative enzyme for atrial natriuretic peptide, in rat kidney using a radioiodinated neutral metalloendopeptidase inhibitor
J. Pharmacol. Exp. Ther.
261
1231-1237
1992
Rattus norvegicus
Zajac, J.M.; Charnay, Y.; Soleilhac, J.M.; Sales, N.; Roques, B.P.
Enkephalin-degrading enzymes and angiotensin-converting enzyme in human and rat meninges
FEBS Lett.
216
118-122
1987
Homo sapiens, Rattus norvegicus
Malfroy, B.; Burnier, J.
New substrates for enkephalinase (neutral endopeptidase) based on fluorescence energy transfer
Biochem. Biophys. Res. Commun.
143
58-66
1987
Rattus norvegicus
Malfroy, B.; Schofield, P.R.; Kuang, W.J.; Seeburg, P.H.; Mason, A.J.; Henzel, W.J.
Molecular cloning and amino acid sequence of rat enkephalinase
Biochem. Biophys. Res. Commun.
144
59-66
1987
Rattus norvegicus
Waksman, G.; Hamel, E.; Delay-Goyet, P.; Roques, B.P.
Neuronal localization of the neutral endopeptidase enkephalinase in rat brain revealed by lesions and autoradiography
EMBO J.
5
3163-3166
1986
Rattus norvegicus
Jackson, D.G.; Hersh, L.B.
Reaction of neutral endopeptidase 24.11 (enkephalinase) with arginine reagents
J. Biol. Chem.
261
8649-8654
1986
Rattus norvegicus
Malfroy, B.; Schwartz, J.C.
Properties of enkephalinase from rat kidney: comparison of dipeptidyl-carboxypeptidase and endopeptidase activities
Biochem. Biophys. Res. Commun.
106
276-285
1982
Mus musculus, Rattus norvegicus
Roques, B.P.; Noble, F.; Dauge, V.; Fournie-Zaluski, M.C.; Beaumont, A.
Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology
Pharmacol. Rev.
45
87-146
1993
Homo sapiens, Rattus norvegicus, Sus scrofa
Welches, W.R.; Broshihan, K.B.; Ferrario, C.M.
A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11
Life Sci.
52
1461-1480
1993
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Schulz, R.; Sakane, Y.; Berry, C.; Ghai, R.
Characterisation of neutral endopeptidase 3.4.24.11 (NEP) in the kidney: comparison between normotensive, genetically hypertensive and experimentally hypertensive rats
J. Enzyme Inhib.
4
347-358
1991
Rattus norvegicus
Spillantini, M.G.; Sicuteri, F.; Salmon, S.; Malfroy, B.
Characterization of endopeptidase 3.4.24.11 ( enkephalinase ) activity in human plasma and cerebrospinal fluid
Biochem. Pharmacol.
39
1353-1356
1990
Homo sapiens, Mus musculus, Rattus norvegicus
Li, C.; Hersh, L.B.
Neprilysin: assay methods, purification, and characterization
Methods Enzymol.
248
253-263
1995
Rattus norvegicus
Sansoe, G.; Aragno, M.; Mastrocola, R.; Cutrin, J.C.; Silvano, S.; Mengozzi, G.; Smedile, A.; Rosina, F.; Danni, O.; Rizzetto, M.
Overexpression of kidney neutral endopeptidase (EC 3.4.24.11) and renal function in experimental cirrhosis
Am. J. Physiol. Renal Physiol.
290
F1337-F1343
2006
Rattus norvegicus
Huang, J.; Guan, H.; Booze, R.M.; Eckman, C.B.; Hersh, L.B.
Estrogen regulates neprilysin activity in rat brain
Neurosci. Lett.
367
85-87
2004
Rattus norvegicus
Jiang, W.; Jiang, H.F.; Cai, D.Y.; Pan, C.S.; Qi, Y.F.; Pang, Y.Z.; Tang, C.S.
Relationship between contents of adrenomedullin and distributions of neutral endopeptidase in blood and tissues of rats in septic shock
Regul. Pept.
118
199-208
2004
Rattus norvegicus
Schmid, C.; Ghirlanda-Keller, C.; Gosteli-Peter, M.
Ascorbic acid decreases neutral endopeptidase activity in cultured osteoblastic cells
Regul. Pept.
130
57-66
2005
Rattus norvegicus (P07861)
de Gortari, P.; Vargas, M.A.; Martinez, A.; Garcia-Vazquez, A.I.; Uribe, R.M.; Chavez-Gutierrez, L.; Magdaleno, V.; Boileau, G.; Charli, J.L.; Joseph-Bravo, P.
Stage-specific modulation of neprilysin and aminopeptidase N in the limbic system during kindling progression
J. Mol. Neurosci.
33
252-261
2007
Rattus norvegicus
Thomas, C.J.; McAllen, R.M.; Salo, L.M.; Woods, R.L.
Restorative effect of atrial natriuretic peptide or chronic neutral endopeptidase inhibition on blunted cardiopulmonary vagal reflexes in aged rats
Hypertension
52
696-701
2008
Rattus norvegicus
Mak, I.T.; Kramer, J.H.; Chmielinska, J.J.; Khalid, M.H.; Landgraf, K.M.; Weglicki, W.B.
Inhibition of neutral endopeptidase potentiates neutrophil activation during Mg-deficiency in the rat
Inflamm. Res.
57
300-305
2008
Rattus norvegicus
Yao, M.; Nguyen, T.V.; Rosario, E.R.; Ramsden, M.; Pike, C.J.
Androgens regulate neprilysin expression: role in reducing beta-amyloid levels
J. Neurochem.
105
2477-2488
2008
Rattus norvegicus
Burgos-Ramos, E.; Puebla-Jimenez, L.; Arilla-Ferreiro, E.
Minocycline prevents Abeta(25-35)-induced reduction of somatostatin and neprilysin content in rat temporal cortex
Life Sci.
84
205-210
2009
Rattus norvegicus
Maeshiro, K.; Takamori, S.; Mifune, H.; Matsuo, T.; Kimura, N.Y.; Honda, J.; Shirouzu, K.
Changes in A-type natriuretic peptide and its receptors induced by a neutral endopeptidase inhibitor in a rat model of sepsis
Surg. Today
38
130-134
2008
Rattus norvegicus
Belyaev, N.; Nalivaeva, N.; Makova, N.; Turner, A.
Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: Implications for Alzheimer disease
EMBO Rep.
10
94-100
2009
Homo sapiens, Rattus norvegicus
Davies, K.P.
The role of opiorphins (endogenous neutral endopeptidase inhibitors) in urogenital smooth muscle biology
J. Sex Med.
6 Suppl 3
286-291
2009
Homo sapiens, Rattus norvegicus, Sus scrofa
Gu, J.; Noe, A.; Chandra, P.; Al-Fayoumi, S.; Ligueros-Saylan, M.; Sarangapani, R.; Maahs, S.; Ksander, G.; Rigel, D.F.; Jeng, A.Y.; Lin, T.H.; Zheng, W.; Dole, W.P.
Pharmacokinetics and pharmacodynamics of LCZ696, a novel dual-acting angiotensin receptor-neprilysin inhibitor (ARNi)
J. Clin. Pharmacol.
50
401-414
2010
Homo sapiens, Rattus norvegicus
Morales-Mulia, M.; de Gortari, P.; Amaya, M.I.; Mendez, M.
Activity and expression of enkephalinase and aminopeptidase N in regions of the mesocorticolimbic system are selectively modified by acute ethanol administration
J. Mol. Neurosci.
46
58-67
2012
Rattus norvegicus
Marr, R.A.; Hafez, D.M.
Amyloid-beta and Alzheimers disease: the role of neprilysin-2 in amyloid-beta clearance
Front. Aging Neurosci.
6
187
2014
Rattus norvegicus, Homo sapiens (P08473), Mus musculus (Q61391)
Morisaki, N.; Ohuchi, A.; Moriwaki, S.
The role of neprilysin in regulating the hair cycle
PLoS ONE
8
e55947
2013
Rattus norvegicus (P07861), Homo sapiens (P08473), Mus musculus (Q61391)
de Oliveira, R.W.; Julian, G.S.; Perry, J.C.; Tufik, S.; Chagas, J.R.
Chronic intermittent hypoxia induces changes on the expression and activity of neprilysin (EC 3.4.24.11) in the brain of rats
Neurosci. Lett.
678
43-47
2018
Rattus norvegicus (P07861), Rattus norvegicus Wistar-Hannover (P07861)
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