Evidence map›Paper›PMID 35914472›Full record

ArticleNeurobiology of aging2022

Elevated levels of tripeptidyl peptidase 1 do not ameliorate pathogenesis in a mouse model of Alzheimer disease.

David E Sleat, Isabella Maita, Whitney Banach-Petrosky, Katherine E Larrimore, Tonia Liu, Dana Cruz, Lukas Baker, Frederick R Maxfield, Benjamin Samuels, Peter Lobel

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Neurobiology of aging, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 47% of its field
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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Review
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

10 authors at 2 institutions in 1 country.

David E SleatCenter for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ, USA; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers Biomedical Health Sciences, Rutgers University, Piscataway, NJ, USA.
Isabella MaitaBehavioral and Systems Neuroscience, Department of Psychology, Rutgers University-New Brunswick, Piscataway, NJ, USA; Neuroscience Graduate Program, Rutgers-Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Whitney Banach-PetroskyCenter for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ, USA.
Katherine E LarrimoreCenter for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ, USA.
Tonia LiuBehavioral and Systems Neuroscience, Department of Psychology, Rutgers University-New Brunswick, Piscataway, NJ, USA.
Dana CruzDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, USA.
Lukas BakerDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, USA.
Frederick R MaxfieldDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, USA.
Benjamin SamuelsBehavioral and Systems Neuroscience, Department of Psychology, Rutgers University-New Brunswick, Piscataway, NJ, USA; Neuroscience Graduate Program, Rutgers-Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Peter LobelCenter for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ, USA; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers Biomedical Health Sciences, Rutgers University, Piscataway, NJ, USA.
Rutgers, The State University of New Jersey · USCornell University · US

Funding

Evaluation of the lysosomal protease tripeptidyl peptidase 1 as a potential therapeutic for Alzheimer DiseaseR21AG064595 · NIA · RBHS-ROBERT WOOD JOHNSON MEDICAL SCHOOL · PI LOBEL, PETER · 2019 to 2020
$437k
NIA NIH HHS R21 AG064595
6 · The paper itself

Abstract

One potential therapeutic strategy for Alzheimer disease (AD) is to promote degradation of amyloid beta (Aβ) and we previously demonstrated that the lysosomal protease tripeptidyl peptidase 1 (TPP1) can degrade Aβ fibrils in vitro. In this study, we tested the hypothesis that increasing levels of TPP1 might promote degradation of Aβ under physiological conditions, slowing or preventing its accumulation in the brain with subsequent therapeutic benefits. We used 2 approaches to increase TPP1 activity in the brain of J20 mice, an AD model that accumulates Aβ and exhibits cognitive defects: transgenic overexpression of TPP1 in the brain and a pharmacological approach employing administration of recombinant TPP1. While we clearly observed the expected AD phenotype of the J20 mice based on pathology and measurement of behavioral and cognitive defects, we found that elevation of TPP1 activity by either experimental approach failed to have any measurable beneficial effect on disease phenotype.

Indexed as

Alzheimer DiseaseTripeptidyl-Peptidase 1AminopeptidasesAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBrainDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDisease Models, AnimalMiceMice, TransgenicSerine ProteasesAminopeptidasesAmyloid beta-PeptidesAmyloid beta-Protein PrecursorDipeptidyl-Peptidases and Tripeptidyl-PeptidasesSerine ProteasesTripeptidyl-Peptidase 1Alzheimer diseaseAmyloid beta degradationCognitive/behavioral deficitsMouse modelsPathologyTripeptidyl peptidase 1

Identifiers

PMID35914472
PMCPMC11258943
OpenAlexW4284883889

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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 OpenQuestion graph.