Evidence map›Paper›PMID 22144675›Full record

ArticleThe Journal of biological chemistry2012

Amyloid precursor protein revisited: neuron-specific expression and highly stable nature of soluble derivatives.

Qinxi Guo, Hongmei Li, Samson S K Gaddam, Nicholas J Justice, Claudia S Robertson, Hui Zheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 93 citations in OpenAlex.

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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

6 authors at 2 institutions in 2 countries.

Qinxi GuoHuffington Center on Aging, Baylor College of Medicine, Houston, Texas 77030, USA.
Hongmei Li
Samson S K Gaddam
Nicholas J Justice
Claudia S Robertson
Hui Zheng
Baylor College of Medicine · USInstitute on Aging · US

Funding

Vascular Mechanisms of Secondary Injury After Traumatic Brain InjuryP01NS038660 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI ROBERTSON, CLAUDIA S · 1999 to 2012
$12.1M
Knockin Mouse Models of Alzheimers DiseaseR01AG020670 · NIA · BAYLOR COLLEGE OF MEDICINE · PI Hui Zheng · 2002 to 2026
$9.1M
Pathophysiology of APP in vivo.R01AG032051 · NIA · BAYLOR COLLEGE OF MEDICINE · PI ZHENG, HUI · 2008 to 2017
$3.5M
Mechanism and therapy of AB-42-specific gamma-secretaseR01NS076117 · NINDS · SLOAN-KETTERING INST CAN RESEARCH · PI LI, YUEMING, ZHENG, HUI · 2011 to 2015
$2.8M
Role of APP in Synaptic RegulationR01AG033467 · NIA · BAYLOR COLLEGE OF MEDICINE · PI ZHENG, HUI · 2009 to 2013
$1.5M
NIA NIH HHS AG033467NIA NIH HHS R01 AG020670NIA NIH HHS R01 AG032051NIA NIH HHS R01 AG033467NINDS NIH HHS NS076117NINDS NIH HHS P01 NS038660NINDS NIH HHS P01 NS38660NINDS NIH HHS R01 NS076117
6 · The paper itself

Abstract

APP processing and amyloid-β production play a central role in Alzheimer disease pathogenesis. APP has been considered a ubiquitously expressed protein. In addition to amyloid-β, α- or β-secretase-dependent cleavage of APP also generates soluble secreted APP (APPsα or APPsβ, respectively). Interestingly, APPsβ has been shown to be subject to further cleavage to create an N-APP fragment that binds to the DR6 death receptor and mediates axon pruning and degeneration under trophic factor withdrawal conditions. By performing APP immunocytochemical staining, we found that, unexpectedly, many antibodies yielded nonspecific staining in APP-null samples. Screening of a series of antibodies allowed us to identify a rabbit monoclonal antibody Y188 that is highly specific for APP and prompted us to re-examine the expression, localization, and stability of endogenous APP and APPsβ in wild-type and in APPsβ knock-in mice, respectively. In contrast to earlier studies, we found that APP is specifically expressed in neurons and that its expression cannot be detected in major types of glial cells under basal or neuroinflammatory conditions. Both APPsα and APPsβ are highly stable in the central nervous system (CNS) and do not undergo further cleavage with or without trophic factor support. Our results clarify several key questions with regard to the fundamental properties of APP and offer critical cellular insights into the pathophysiology of APP.

Indexed as

Gene Expression RegulationAlzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsAntibodies, MonoclonalCentral Nervous SystemMiceMice, KnockoutNerve Tissue ProteinsNeuronsOrgan SpecificityProtein StabilityRabbitsReceptors, Tumor Necrosis FactorAmyloid beta-Protein PrecursorAntibodies, MonoclonalNerve Tissue ProteinsReceptors, Tumor Necrosis Factor

Identifiers

PMID22144675
PMCPMC3268404
OpenAlexW2003391115

What OpenQuestion holds

Textmetadata
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.