Evidence map›Paper›PMID 10393925›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix.

A L Schwarzman, N Singh, M Tsiper, L Gregori, A Dranovsky, M P Vitek, C G Glabe, P H St George-Hyslop, D Goldgaber

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  6. Increased cell-cell adhesion, a novel effect of R-(-)-deprenyl.Journal of neural transmission (Vienna, Austria : 1996) · 2005
    Article
  7. Article
  8. The ins and outs of presenilin 1 membrane topology.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  9. The presenilins turned inside out: implications for their structures and functions.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  10. Article
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  18. Presenilin-1 regulates the neuronal threshold to excitotoxicity both physiologically and pathologically.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  19. Article
  20. 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

9 authors at 5 institutions in 2 countries.

A L SchwarzmanDepartment of Psychiatry and Behavioral Sciences, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.
N Singh
M Tsiper
L Gregori
A Dranovsky
M P Vitek
C G Glabe
P H St George-Hyslop
D Goldgaber
University of Toronto · CADuke Medical Center · USDuke University Hospital · USState University of New York · USUniversity of California, Irvine · US

Funding

PAIN ANALGESIC RESPONSE IN OPIATE DEPENDENCER01DA013706 · NIDA · FRIENDS RESEARCH INSTITUTE, INC. · PI LING, WALTER NMN · 2001 to 2003
$1.7M
INHIBITION OF AMYLOID FORMATION BY TRANSTHYRETIN &APOER01AG013706 · NIA · STATE UNIVERSITY NEW YORK STONY BROOK · PI GOLDGABER, DMITRY Y · 1996 to 1999
–
NIA NIH HHS R01 AG13706NIDA NIH HHS R01 DA013706
6 · The paper itself

Abstract

Most familial early-onset Alzheimer's disease cases are caused by mutations in the presenilin 1 (PS1) gene. Subcellular localization of the endogenous PS1 is essential for understanding its function, interactions with proteins, and role in Alzheimer's disease. Although numerous studies revealed predominant localization of PS1 to endoplasmic reticulum and Golgi, there are conflicting reports on the localization of PS1 to the cell surface. We found that endogenous PS1 is highly expressed in T lymphocytes (Jurkat cells). Using a variety of methods, we present evidence that endogenous PS1 is localized to the cell surface in addition to intracellular membrane compartments. Moreover, PS1 appeared in high levels on the surface of lamellipodia upon adhesion of the cells to a collagen matrix. The redistribution of PS1 in adhered cells was strikingly similar to that of the well characterized adhesion protein CD44. Cell surface PS1 formed complexes in vivo with actin-binding protein filamin (ABP-280), which is known to form bridges between cell surface receptors and cytoskeleton and mediate cell adhesion and cell motility. Taken together, our results suggest a role of PS1 in cell adhesion and/or cell-matrix interaction.

Indexed as

CollagenAlgorithmsAlzheimer DiseaseAmino Acid SequenceCell AdhesionCell MembraneCell MovementConsensus SequenceContractile ProteinsCytoplasmExtracellular MatrixFilaminsHumansHyaluronan ReceptorsImmunohistochemistryJurkat CellsCollagenContractile ProteinsFilaminsHyaluronan ReceptorsMembrane ProteinsMicrofilament ProteinsPeptide LibraryPeptidesPresenilin-1PSEN1 protein, humanReceptors, Antigen, T-Cell

Identifiers

PMID10393925
PMCPMC22165
OpenAlexW2014144346

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.