Evidence map›Paper›PMID 31796108›Full record

ArticleActa neuropathologica communications2019

Secernin-1 is a novel phosphorylated tau binding protein that accumulates in Alzheimer's disease and not in other tauopathies.

Geoffrey Pires, Sacha McElligott, Shiron Drusinsky, Glenda Halliday, Marie-Claude Potier, Thomas Wisniewski, Eleanor Drummond

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  6. Distinct inflammatory profiles in young-onset versus late-onset Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  7. Article
  8. Risk of Alzheimer's disease in Down syndrome: Insights gained by multi-omics.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  9. Article
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  12. Article
  13. The influence of APOEActa neuropathologica · 2024
    Article
  14. Review
  15. Article
  16. Article
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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

7 authors at 4 institutions in 3 countries.

Geoffrey PiresCenter for Cognitive Neurology and Department of Neurology, New York University School of Medicine, 435 East 30th Street, Rm 1017, New York, NY, 10016, USA.
Sacha McElligottCenter for Cognitive Neurology and Department of Neurology, New York University School of Medicine, 435 East 30th Street, Rm 1017, New York, NY, 10016, USA.
Shiron DrusinskyCenter for Cognitive Neurology and Department of Neurology, New York University School of Medicine, 435 East 30th Street, Rm 1017, New York, NY, 10016, USA.
Glenda HallidayBrain & Mind Centre and Central Clinical School, Faculty of Medicine and Health, University of Sydney, 94 Mallett Street, Camperdown, NSW, 2050, Australia.
Marie-Claude PotierInstitut du Cerveau et de la Moelle épinière, CNRS UMR7225, INSERM U1127, UPMC, Hôpital de la Pitié-Salpêtrière, 47 Bd de l'Hôpital, Paris, France.
Thomas WisniewskiCenter for Cognitive Neurology and Department of Neurology, New York University School of Medicine, 435 East 30th Street, Rm 1017, New York, NY, 10016, USA. Thomas.wisniewski@nyulangone.org.
Eleanor DrummondCenter for Cognitive Neurology and Department of Neurology, New York University School of Medicine, 435 East 30th Street, Rm 1017, New York, NY, 10016, USA. eleanor.drummond@sydney.edu.au.
New York University · USNYU Langone Health · USUniversity of Sydney · AUSorbonne Université · FR

Funding

PSYCHOSOCIAL COREP30AG008051 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SHAO, YONGZHAO · 1990 to 2019
$36.1M
Research Education ComponentP30AG066512 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Mary Sherman Mittelman · 2020 to 2026
$28.4M
Characterization of Rapidly Progressive Alzheimer's DiseaseRF1AG058267 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HAINES, JONATHAN L, SAFAR, JIRI G. · 2017 to 2017
$4.0M
NIA NIH HHS AG008051NIA NIH HHS AG058267NIA NIH HHS P30 AG008051NIA NIH HHS P30 AG066512NIA NIH HHS RF1 AG058267
6 · The paper itself

Abstract

We recently identified Secernin-1 (SCRN1) as a novel amyloid plaque associated protein using localized proteomics. Immunohistochemistry studies confirmed that SCRN1 was present in plaque-associated dystrophic neurites and also revealed distinct and abundant co-localization with neurofibrillary tangles (NFTs). Little is known about the physiological function of SCRN1 and its role in Alzheimer's disease (AD) and other neurodegenerative diseases has not been studied. Therefore, we performed a comprehensive study of SCRN1 distribution in neurodegenerative diseases. Immunohistochemistry was used to map SCRN1 accumulation throughout the progression of AD in a cohort of 58 patients with a range of NFT pathology (Abundant NFT, n = 21; Moderate NFT, n = 22; Low/No NFT, n = 15), who were clinically diagnosed as having AD, mild cognitive impairment or normal cognition. SCRN1 accumulation was also examined in two cases with both Frontotemporal Lobar Degeneration (FTLD)-Tau and AD-related neuropathology, cases of Down Syndrome (DS) with AD (n = 5), one case of hereditary cerebral hemorrhage with amyloidosis - Dutch type (HCHWA-D) and other non-AD tauopathies including: primary age-related tauopathy (PART, [n = 5]), Corticobasal Degeneration (CBD, [n = 5]), Progressive Supranuclear Palsy (PSP, [n = 5]) and Pick's disease (PiD, [n = 4]). Immunohistochemistry showed that SCRN1 was a neuronal protein that abundantly accumulated in NFTs and plaque-associated dystrophic neurites throughout the progression of AD. Quantification of SCRN1 immunohistochemistry confirmed that SCRN1 preferentially accumulated in NFTs in comparison to surrounding non-tangle containing neurons at both early and late stages of AD. Similar results were observed in DS with AD and PART. However, SCRN1 did not co-localize with phosphorylated tau inclusions in CBD, PSP or PiD. Co-immunoprecipitation revealed that SCRN1 interacted with phosphorylated tau in human AD brain tissue. Together, these results suggest that SCRN1 is uniquely associated with tau pathology in AD, DS and PART. As such, SCRN1 has potential as a novel therapeutic target and could serve as a useful biomarker to distinguish AD from other tauopathies.

Indexed as

AgedAged, 80 and overAlzheimer DiseaseCerebral CortexFemaleHumansMaleMiddle AgedNerve Tissue ProteinsPhosphorylationProtein BindingTauopathiestau ProteinsMAPT protein, humanNerve Tissue ProteinsSCRN1 protein, humantau ProteinsAlzheimer’s diseaseNeurofibrillary tanglesPhosphorylated tauProtein-protein interactionSecernin-1Tauopathies

Identifiers

PMID31796108
PMCPMC6892024
OpenAlexW2992077194

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.