Evidence map›Paper›PMID 39698259›Full record

ReviewACS pharmacology & translational science2024

Neprilysin-Mediated Amyloid Beta Clearance and Its Therapeutic Implications in Neurodegenerative Disorders.

Shailendra K Saxena, Saniya Ansari, Vimal K Maurya, Swatantra Kumar, Deepak Sharma, Hardeep S Malhotra, Sneham Tiwari, Chhitij Srivastava, Janusz T Paweska, Ahmed S Abdel-Moneim and 1 more

Abstract readReview
In one paragraph

Review in ACS pharmacology & translational science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Shailendra K SaxenaCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.ORCID https://orcid.org/0000-0003-2856-4185
Saniya AnsariCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.
Vimal K MauryaCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.
Swatantra KumarCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.
Deepak SharmaCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.
Hardeep S MalhotraDepartment of Neurology, King George's Medical University, Lucknow 226003, India.
Sneham TiwariF. M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, United States.
Chhitij SrivastavaDepartment of Neurosurgery, King George's Medical University, Lucknow 226003, India.
Janusz T PaweskaThe World Society for Virology (WSV), Northampton, Massachusetts 01060, United States.
Ahmed S Abdel-MoneimDepartment of Microbiology, College of Medicine, Taif University, Al-Taif 21944 Saudi Arabia.
Soniya NityanandCentre for Advanced Research (CFAR), Faculty of Medicine, King George's Medical University (KGMU), Lucknow 226003, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neprilysin (NEP) is a neutral endopeptidase, important for the degradation of amyloid beta (Aβ) peptides and other neuropeptides, including enkephalins, substance P, and bradykinin, in the brain, that influences various physiological processes such as blood pressure homeostasis, pain perception, and neuroinflammation. NEP breaks down Aβ peptides into smaller fragments, preventing the development of detrimental aggregates such as Aβ plaques. NEP clears Aβ plaques predominantly by enzymatic breakdown in the extracellular space. However, NEP activity may be regulated by a variety of factors, including its expression and activity levels as well as interactions with other proteins or substances present in the brain. The Aβ de novo synthesis results from the amyloidogenic and nonamyloidogenic processing of the amyloid precursor protein (APP). In addition to Aβ synthesis, enzymatic degradation and various clearance pathways also contribute to the degradation of the monomeric form of Aβ peptides in the brain. Higher production, dysfunction of degradation enzymes, defective clearance mechanisms, intracellular accumulation of phosphorylated tau proteins, and extracellular deposition of Aβ are hallmarks of neurodegenerative diseases. Strategies for promoting NEP levels or activity, such as pharmaceutical interventions or gene therapy procedures, are being studied as possible therapies for neurodegenerative diseases including Alzheimer's disease. Therefore, in this perspective, we discuss the recent developments in NEP-mediated amyloidogenic and plausible mechanisms of nonamyloidogenic clearance of Aβ. We further highlight the current therapeutic interventions such as pharmaceutical agents, gene therapy, monoclonal antibodies, and stem-cell-based therapies targeting NEP for the management of neurodegenerative disorders.

Identifiers

PMID39698259
PMCPMC11651204

What Socratic holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.