Neprilysin
Thiorphan
Amyloid beta-Peptides
Insulysin
Enkephalin, Leucine-2-Alanine
Amyloid beta-Protein Precursor
Alzheimer Disease
Aspartic Acid Endopeptidases
Thermolysin
Peptide Fragments
Angiotensin I
Protease Inhibitors
Subtilisin
Glycopeptides
Angiotensins
Brain
Peptidyl-Dipeptidase A
Mice, Transgenic
Maze Learning
Amyloid
Lentivirus
Furans
Amyloid Precursor Protein Secretases
Dynorphin A processing enzyme: tissue distribution, isolation, and characterization. (1/1042)
Limited proteolysis of the dynorphin precursor (prodynorphin) at dibasic and monobasic processing sites results in the generation of bioactive dynorphins. In the brain and neurointermediate lobe of the pituitary, prodynorphin is processed to produce alpha and beta neo endorphins, dynorphins (Dyn) A-17 and Dyn A-8, Dyn B-13, and leucine-enkephalin. The formation of Dyn A-8 from Dyn A-17 requires a monobasic cleavage between Ile and Arg. We have identified an enzymatic activity capable of processing at this monobasic site in the rat brain and neurointermediate lobe of the bovine pituitary; this enzyme is designated "dynorphin A-17 processing enzyme." In the rat brain and neurointermediate lobe, a majority of the Dyn A processing enzyme activity is membrane-associated and can be released by treatment with 1% Triton X-100. This enzyme has been purified to apparent homogeneity from the membrane extract of the neurointermediate lobe using preparative iso-electrofocussing in a granulated gel pH 3.5 to 10, FPLC using anion exchange chromatography, and non-denaturing electrophoresis. The Dyn A processing enzyme exhibits a pI of about 5.8 and a molecular mass of about 65 kDa under reducing conditions. The Dyn A processing enzyme is a metalloprotease and has a neutral pH optimum. It exhibits substantial sensitivity to metal chelating agents and thiol agents suggesting that this enzyme is a thiol-sensitive metalloprotease. Specific inhibitors of other metallopeptidases such as enkephalinase [EC 3.4.24.11], the enkephalin generating neutral endopeptidase [EC 3.4.24.15], or NRD convertase do not inhibit the Dyn A processing enzyme activity. In contrast, specific inhibitors of angiotensin converting enzyme inhibit the activity. The purified enzyme is able to process a number of neuropeptides at both monobasic and dibasic sites. These characteristics are consistent with a role for the Dyn A processing enzyme in the processing of Dyn A-17 and other neuropeptides in the brain. (+info)Morphine preconditioning attenuates neutrophil activation in rat models of myocardial infarction. (2/1042)
Previous results from our laboratory have suggested that morphine can attenuate neutrophil activation in patients with acute myocardial infarction. To elucidate if morphine preconditioning (PC) has the same effects via activation of neutrophil endopeptidase 24.11 (NEP), we measured serum levels of intercellular adhesion molecule-1 (ICAM-1), gp100MEL14 and NEP in adult Wistar rats subjected to ten different protocols (n = 10 for each) at baseline, immediately after and 2 h after morphine PC. All groups were subjected to 30 min of occlusion and 2 h of reperfusion. Similarly, morphine-induced PC was elicited by 3-min drug infusions (100 micrograms/kg) interspersed with 5-min drug-free periods before the prolonged 30-min occlusion. Infarct size (IS), as a percentage of the area at risk (AAR), was determined by triphenyltetrazolium staining. Pretreatment with morphine increased NEP activities (9.86 +/- 1.98 vs. 5.12 +/- 1.10 nmol/mg protein in control group; p < 0.001). Naloxone (mu-opioid receptor antagonist) (4.82 +/- 1.02 nmol/mg protein) and phosphoramidon (NEP inhibitor) (4.66 +/- 1.00 nmol/mg protein) inhibited morphine-activated NEP, whereas glibenclamide (ATP-sensitive potassium channel antagonist) and chelerythrine (protein kinase C inhibitor) had no effects. The ICAM-1 and gp100MEL14 of the third sampling were lowest for those with morphine PC (280 +/- 30 ng/ml and 2.2 +/- 0.7 micrograms/ml; p < 0.001), but naloxone (372 +/- 38 ng/ml and 3.8 +/- 0.9 micrograms/ml) and phosphoramidon (382 +/- 40 ng/ml and 4.2 +/- 1.1 micrograms/ml) abolished the above phenomenon. IS/AAR were definitely lowest for those with morphine PC (24 +/- 7%; p < 0.05). Morphine preconditioning increases NEP activities to attenuate shedding of gp100MEL14 and to ICAM-1 and, thus, provides myocardial protection. (+info)Mechanism of weight gain suppressing effect of ER-40133, an angiotensin I converting enzyme inhibitor, in growing rats. (3/1042)
Effects of ER-40133, an inhibitor of angiotensin converting enzyme (ACE), on weight gain and sodium and potassium balance were studied in growing SD male rats. Thirty-two animals (seven weeks of age) were divided into two groups; one received a standard diet containing 0.227% sodium and the other a low (0.065%) sodium diet. They were divided into four subgroups; one control group and three treated groups receiving 3, 10 or 30 mg/kg of ER-40133, by gavage, once a day for five consecutive days. Body weight gain (average of the standard and low sodium diet groups) was -32% in the 3 mg/kg group,-74% in 10 mg/kg group and -99% in 30 mg/kg group, when compared with the control group. There was a highly linear correlation between suppression of body weight gain and reduction in sodium and potassium retention for both groups of animals given the standard and low sodium diet. The reduced sodium retention, the primary effect of ACE inhibitors, accounted for about 30% of suppressed weight gain, and the reduced potassium retention, the secondary effect of sodium deficiency, could account for the rest about 70% of weight suppression by ER-40133. (+info)Identification of kallidin degrading enzymes in the isolated perfused rat heart. (4/1042)
Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found. (+info)Interaction between neutral endopeptidase and angiotensin converting enzyme inhibition in rats with myocardial infarction: effects on cardiac hypertrophy and angiotensin and bradykinin peptide levels. (5/1042)
Combined inhibition of neutral endopeptidase 24.11 (NEP) and angiotensin converting enzyme (ACE) is a candidate therapy for hypertension and cardiac failure. Given that NEP and ACE metabolize angiotensin (Ang) and bradykinin (BK) peptides, we investigated the effects of NEP inhibition and combined NEP and ACE inhibition on Ang and BK levels in rats with myocardial infarction. We administered the NEP inhibitor ecadotril (0, 0.1, 1, 10, and 100 mg/kg/day), either alone or together with the ACE inhibitor perindopril (0.2 mg/kg/day) by 12-hourly gavage from day 2 to 28 after infarction. Ecadotril increased urine cyclic GMP and BK-(1-9) excretion. Perindopril potentiated the effect of ecadotril on urine cyclic GMP excretion. Neither perindopril nor ecadotril reduced cardiac hypertrophy when administered separately, whereas the combination of perindopril and 10 or 100 mg/kg/day ecadotril reduced heart weight/body weight ratio by 10%. Administration of ecadotril to perindopril-treated rats decreased plasma Ang-(1-7) levels, increased cardiac BK-(1-9) levels, and increased Ang II levels in plasma, kidney, aorta, and lung. These data demonstrate interactions between the effects of NEP and ACE inhibition on remodeling of the infarcted heart and on Ang and BK peptide levels. Whereas increased cardiac BK-(1-9) levels may contribute to the reduction of cardiac hypertrophy, the reduction in plasma Ang-(1-7) levels and increase in Ang II levels in plasma and tissues may compromise the therapeutic effects of combined NEP/ACE inhibition. (+info)A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC.3.4.24.11). (6/1042)
A three-dimensional model of the 507-749 region of neutral endopeptidase-24.11 (NEP; E.C.3.4.24.11) was constructed integrating the results of secondary structure predictions and sequence homologies with the bacterial endopeptidase thermolysin. Additional data were extracted from the structure of two other metalloproteases, astacin and stromelysin. The resulting model accounts for the main biological properties of NEP and has been used to describe the environment close to the zinc atom defining the catalytic site. The analysis of several thiol inhibitors, complexed in the model active site, revealed the presence of a large hydrophobic pocket at the S1' subsite level. This is supported by the nature of the constitutive amino acids. The computed energies of bound inhibitors correspond with the relative affinities of the stereoisomers of benzofused macrocycle derivatives of thiorphan. The model could be used to facilitate the design of new NEP inhibitors, as illustrated in the paper. (+info)Enhanced natriuretic response to neutral endopeptidase inhibition in heart-transplant recipients. (7/1042)
Heart-transplant recipients (Htx) generally present with body fluid and sodium handling abnormalities and hypertension. To investigate whether neutral endopeptidase inhibition (NEP-I) increases endogenous atrial natriuretic peptide (ANP) and enhances natriuresis and diuresis after heart transplantation, ecadotril was given orally to 8 control subjects and 8 matched Htx, and levels of volume-regulating hormones and renal water, electrolyte, and cyclic guanosine monophosphate (cGMP) excretions were monitored for 210 minutes. Baseline plasma ANP, brain natriuretic peptide (BNP), and cGMP were elevated in Htx, but renin and aldosterone, like urinary parameters, did not differ between groups. NEP-I increased plasma ANP (Htx, 20.6+/-2.3 to 33.2+/-5.9 pmol/L, P<0.01; controls, 7.7+/-1. 2 to 10.6+/-2.6 pmol/L) and cGMP, but not BNP. Renin decreased similarly in both groups, whereas aldosterone decreased significantly only in Htx. Enhanced urinary sodium (1650+/-370% versus 450+/-150%, P=0.01), cGMP, and water excretions were observed in Htx and urinary cGMP positively correlated with natriuresis in 6 of the Htx subjects. Consistent with a normal circadian rhythm of blood pressure, without excluding a possible effect of NEP-I, mean systemic blood pressure increased similarly in both groups at the end of the study (6.9+/-2.0% versus 7.4+/-2.8% in controls and Htx). Thus, systemic hypertension, mild renal impairment, and raised plasma ANP levels are possible contributory factors in the enhanced natriuresis and diuresis with NEP-I in Htx. These results support a physiological role for the cardiac hormone after heart transplantation and suggest that long-term studies may be useful to determine the potential of NEP-I in the treatment of sodium retention and water retention after heart transplantation. (+info)Kallidin- and bradykinin-degrading pathways in human heart: degradation of kallidin by aminopeptidase M-like activity and bradykinin by neutral endopeptidase. (8/1042)
BACKGROUND: Since kinins kallidin (KD) and bradykinin (BK) appear to have cardioprotective effects ranging from improved hemodynamics to antiproliferative effects, inhibition of kinin-degrading enzymes should potentiate such effects. Indeed, it is believed that this mechanism is partly responsible for the beneficial effects of angiotensin-converting enzyme (ACE) inhibitors. In the heart, enzymes other than ACE may contribute to local degradation of kinins. The purpose of this study was to investigate which enzymes are responsible for the degradation of KD and BK in human heart tissue. METHODS AND RESULTS: Cardiac membranes were prepared from the left ventricles of normal (n=5) and failing (n=10) hearts. The patients had end-stage congestive heart failure as the result of coronary heart disease or idiopathic dilated cardiomyopathy. Heart tissue was incubated with KD or BK in the presence or absence of enzyme inhibitors. We found no difference in the enzymes responsible for kinin metabolism or their activities between normal and failing hearts. Thus KD was mostly converted into BK by the aminopeptidase M-like activity. When BK was used as substrate, it was converted into an inactive metabolite BK-(1-7) mostly (80% to 90%) by the neutral endopeptidase (NEP) activity, with ACE unexpectedly playing only a minor role. The low enzymatic activity of ACE in the cardiac membranes, compared with that of NEP, was not due to chronic ACE inhibitor therapy, because the cardiac ACE activities of patients, whether receiving ACE inhibitors or not, and of normal subjects were all equal. CONCLUSIONS: The present in vitro study shows that in human cardiac membranes, the most critical step in kinin metabolism, that is, inactivation of BK, appears to be mediated mostly by NEP. This observation suggests a role for NEP in the local control of BK concentration in heart tissue. Thus inhibition of cardiac NEP activity could be cardioprotective by elevating the local concentration of BK in the heart. (+info)The term "amyloid" refers specifically to the type of protein aggregate that forms these plaques, and is derived from the Greek word for "flour-like." Amyloidosis is the general term used to describe the condition of having amyloid deposits in the body, while Alzheimer's disease is a specific type of amyloidosis that is characterized by the accumulation of beta-amyloid peptides in the brain.
Plaques, amyloid play a central role in the pathogenesis of many neurodegenerative diseases, and understanding their formation and clearance is an area of ongoing research. In addition to their role in Alzheimer's disease, amyloid plaques have been implicated in other conditions such as cerebral amyloid angiopathy, primary lateral sclerosis, and progressive supranuclear palsy.
Plaques, amyloid are composed of a variety of proteins, including beta-amyloid peptides, tau protein, and apolipoprotein E (apoE). The composition and structure of these plaques can vary depending on the underlying disease, and their presence is often associated with inflammation and oxidative stress.
In addition to their role in neurodegeneration, amyloid plaques have been implicated in other diseases such as type 2 diabetes and cardiovascular disease. The accumulation of amyloid fibrils in these tissues can contribute to the development of insulin resistance and atherosclerosis, respectively.
Overall, plaques, amyloid are a complex and multifaceted area of research, with many open questions remaining about their formation, function, and clinical implications. Ongoing studies in this field may provide valuable insights into the pathogenesis of various diseases and ultimately lead to the development of novel therapeutic strategies for these conditions.
In conclusion, plaques, amyloid are a hallmark of several neurodegenerative diseases, including Alzheimer's disease, and have been associated with inflammation, oxidative stress, and neurodegeneration. The composition and structure of these plaques can vary depending on the underlying disease, and their presence is often linked to the progression of the condition. Furthermore, amyloid plaques have been implicated in other diseases such as type 2 diabetes and cardiovascular disease, highlighting their potential clinical significance beyond neurodegeneration. Ongoing research into the mechanisms of amyloid plaque formation and clearance may lead to the development of novel therapeutic strategies for these conditions.
The symptoms of Alzheimer's disease can vary from person to person and may progress slowly over time. Early symptoms may include memory loss, confusion, and difficulty with problem-solving. As the disease progresses, individuals may experience language difficulties, visual hallucinations, and changes in mood and behavior.
There is currently no cure for Alzheimer's disease, but there are several medications and therapies that can help manage its symptoms and slow its progression. These include cholinesterase inhibitors, memantine, and non-pharmacological interventions such as cognitive training and behavioral therapy.
Alzheimer's disease is a significant public health concern, affecting an estimated 5.8 million Americans in 2020. It is the sixth leading cause of death in the United States, and its prevalence is expected to continue to increase as the population ages.
There is ongoing research into the causes and potential treatments for Alzheimer's disease, including studies into the role of inflammation, oxidative stress, and the immune system. Other areas of research include the development of biomarkers for early detection and the use of advanced imaging techniques to monitor progression of the disease.
Overall, Alzheimer's disease is a complex and multifactorial disorder that poses significant challenges for individuals, families, and healthcare systems. However, with ongoing research and advances in medical technology, there is hope for improving diagnosis and treatment options in the future.
Neprilysin
Endopeptidase
Bradykinin
Angiotensin (1-7)
Sacubitril
Atrial natriuretic peptide
Nicastrin
Brain natriuretic peptide 32
Valsartan
Milton Packer
Candoxatril
Ecadotril
Drug-induced angioedema
PITRM1
Gemopatrilat
Omapatrilat
MMEL1
Endothelin converting enzyme 1
Kell antigen system
A. Mark Richards
Epigenetics of neurodegenerative diseases
Selective androgen receptor modulator
Human genetic enhancement
Endopeptidase-2
NLN (gene)
Endopeptidase inhibitor
Oligopeptidase
Jean-Charles Schwartz
Cerebral amyloid angiopathy
NEP
Loss of neprilysin function promotes amyloid plaque formation and causes cerebral amyloid angiopathy<...
What is a neprilysin inhibitor? - Runtheyear2016.com
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NephMadness 2015: Cardio-Nephrology Region
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Brain natriuretic peptide - wikidoc
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Primary Care Update 2021 Las Vegas
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Publications - Salk Institute for Biological Studies
DeCS
MH DELETED MN ADDED MN
Find Research outputs - Augusta University Research Profiles
Department of Internal Medicine - Research output - National Yang Ming Chiao Tung University Academic Hub
SMART: Pfam domain Peptidase M1
Center for Cardiovascular Research - Research output
- Research Profiles at Washington University School of Medicine
The Egyptian Journal of Hospital Medicine
Angiotensin converting enzyme inhibitors. Medical search. Definitions
Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide | Molecular Neurodegeneration | Full Text
Find Research outputs - Manipal Academy of Higher Education, Manipal, India
International Master/Ph.D. Program in Medicine - Research output - Taipei Medical University
Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Marian van Groningen - Research output
- Erasmus University Rotterdam
Histamine, Bradykinin, and Their Antagonists | Goodman & Gilman's: The Pharmacological Basis of Therapeutics, 14e |...
Inhibitor13
- What is a neprilysin inhibitor? (runtheyear2016.com)
- Sacubitril is a prodrug, and on activation works as a neprilysin inhibitor. (runtheyear2016.com)
- Angiotensin Receptor-Neprilysin Inhibitor (ARNi) is a medicine resulting from the combination of two anti-hypertensive drugs (sacubitril and valsartan) that reduce blood pressure. (runtheyear2016.com)
- Sacubitril is a pro-drug that, upon activation, acts as a neprilysin inhibitor. (runtheyear2016.com)
- What is the mechanism of action of an angiotensin receptor neprilysin inhibitor? (runtheyear2016.com)
- Sacubitril/valsartan is the first agent to be approved in a new class of drugs called angiotensin receptor neprilysin inhibitor (ARNI). (runtheyear2016.com)
- Angiotensin receptor neprilysin inhibitor (ARNI) medicine works like ARBs and ACE inhibitors. (runtheyear2016.com)
- Sacubitril is a neprilysin inhibitor that is now coupled to a new partner (an ARB), hoping to shed a toxic past. (medscape.com)
- This trial tested whether a neprilysin inhibitor coupled to valsartan provided more benefit than enalapril in patients with heart failure. (medscape.com)
- That is why it is important to add neprilysin inhibition to either an ACE-inhibitor or an ARB. (medscape.com)
- LCZ696 is a combination of the neprilysin inhibitor sacubitril and valsartan. (medscape.com)
- Colucci, Wilson S. Angiotensin II receptor blocker and neprilysin inhibitor therapy in heart failure due to systolic dysfunction. (bvs.br)
- http://www.uptodate.com/contents/angiotensin-ii-receptor-blocker-and-neprilysin-inhibitor-therapy-in-heart-failure-due-to-systolic-dysfunction?source=search_result&search=ANGIOTENSIN+II+RECEPTOR+BLOCKERS+IN+HEART+FAILURE+DUE+TO+SYSTOLIC+DYSFUNCTION%3A+THERAPEUTIC+USE&selectedTitle=2~150 Acesso em: 8 dez 2014. (bvs.br)
Inhibition6
- Neprilysin inhibition generally led to a modest increase in BNP concentrations, but some assays registered no increase and others demonstrated a decrease. (runtheyear2016.com)
- Angiotensin-Neprilysin Inhibition in Patients With Mildly Reduced or Preserved Ejection Fraction and Worsening Heart Failure. (bvsalud.org)
- How will tolvaptan hold up to an old renin-angiotensin system behemoth with shiny new neprilysin inhibition rims? (medscape.com)
- So, the net effect of neprilysin inhibition is difficult to predict. (medscape.com)
- The inhibition of neprilysin alone (in the form of candoxatril) was studied back in 1993 and reported in the journal Clinical Science . (medscape.com)
- Angiotensin Receptor-Neprilysin Inhibition in Chagas Cardiomyopathy With Reduced Ejection Fraction: ANSWER-HF. (who.int)
Angiotensin5
- What is angiotensin receptor-neprilysin? (runtheyear2016.com)
- Angiotensin receptor-neprilysin inhibitors (ARNIs) are a new class of drugs used for the treatment of heart failure. (runtheyear2016.com)
- A new drug class called angiotensin receptor-neprilysin inhibitors (ARNI's) combines an ARB drug with a new type of drug. (medlineplus.gov)
- In this regard, MD simulations validated the results of molecular docking simulations, demonstrating that both SAC and VAL had inhibitory potential towards the neprilysin and angiotensin receptors, respectively. (ac.rs)
- Application of System Biology to Explore the Association of Neprilysin, Angiotensin-Converting Enzyme 2 (ACE2), and Carbonic Anhydrase (CA) in Pathogenesis of SARS-CoV-2. (cdc.gov)
Inhibitors2
- What class of drugs are neprilysin inhibitors administered with? (runtheyear2016.com)
- Hence, there is much interest in using inhibitors of neprilysin in CKD . (medscape.com)
Inhibitory1
- The toxic past was a drug called omapatrilat, which has combined ACE and neprilysin inhibitory effects that initially showed promise in heart failure until angioedema stole the show and proved too hazardous. (medscape.com)
Cleaves1
- Neprilysin is a circulating and membrane-bound metalloprotease that cleaves peptides. (medscape.com)
Cerebral1
- The amount of the free-floating beta-amyloids responsible for damaging the brain is drastically decreased when neprilysin producing cells were injected into cerebral extracellular fluid. (runtheyear2016.com)
Promotes1
- Neprilysin promotes the speedy degradation of beta-amyloid peptides, reducing the amount of plaque deposits formed within the brain. (runtheyear2016.com)
Peptides1
- They work by blocking the action of neprilysin thus preventing the breakdown of natriuretic peptides. (runtheyear2016.com)
Common2
- Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. (bvsalud.org)
- The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. (embl.de)
Trial1
- Could Neprilysin Be Already Inhibited by BNP in the LIFE Trial? (wustl.edu)
Angiotensin Receptor-Neprilysin Inhibitors1
- A new drug class called angiotensin receptor-neprilysin inhibitors (ARNI's) combines an ARB drug with a new type of drug. (medlineplus.gov)
Enzyme4
- Activating AhR alleviates cognitive deficits of Alzheimer ' s disease model mice by upregulating endogenous Aβ catabolic enzyme Neprilysin . (nih.gov)
- We report here a novel strategy for lowering amyloid burden in the brain by peripherally expressing the Abeta-degrading enzyme neprilysin on leukocytes in the 3xTg-AD mouse model of Alzheimer's disease. (nih.gov)
- That neprilysin (NEP) is a major Aβ peptide-degrading enzyme in vivo is shown by higher Aβ peptide levels in the brain of an NEP knockout mouse. (nih.gov)
- Application of System Biology to Explore the Association of Neprilysin, Angiotensin-Converting Enzyme 2 (ACE2), and Carbonic Anhydrase (CA) in Pathogenesis of SARS-CoV-2. (cdc.gov)
Amyloid2
- This peripheral neprilysin reduced soluble brain Abeta peptide levels by approximately 30% and lowered the accumulation of amyloid beta peptides by 50-60% when transplantation was performed at both young and early adult age. (nih.gov)
- In addition, peripheral neprilysin expression reduced amyloid-dependent performance deficits as measured by the Morris water maze. (nih.gov)
Findings1
- These findings demonstrate that peripherally expressed neprilysin, and likely other Abeta-degrading enzymes, has the potential to be utilized as a therapeutic approach to prevent and treat Alzheimer's disease and suggest that this approach should be explored further. (nih.gov)