Evidence map›Paper›PMID 10679012›Full record

ArticleMolecular biology of the cell2000

Detergent-insoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting.

C Lipardi, L Nitsch, C Zurzolo

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Membrane Heterogeneity Beyond the Plasma Membrane.Frontiers in cell and developmental biology · 2020
    Review
  4. With or without rafts? Alternative views on cell membranes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  5. Article
  6. Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014
    Review
  7. Membrane raft association is a determinant of plasma membrane localization.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Apical localization of PMCA2w/b is lipid raft-dependent.Biochemical and biophysical research communications · 2009
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

C LipardiCentro di Endocrinologia ed Oncologia Sperimentale del Consiglio Nazionale delle Ricerche-Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli "Federico II," 80131 Napoli, Italy.
L Nitsch
C Zurzolo
Institute for Experimental Endocrinology and Oncology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to Madin-Darby canine kidney cells, Fischer rat thyroid cells deliver the majority of endogenous glycosylphosphatidyl inositol (GPI)-anchored proteins to the basolateral surface. However, we report here that the GPI proteins Placental Alkaline Phosphatase (PLAP) and Neurotrophin Receptor-Placental Alkaline Phosphatase (NTR-PLAP) are apically localized in transfected Fischer rat thyroid cells. In agreement with the "raft hypothesis," which postulates the incorporation of GPI proteins into glycosphingolipids and cholesterol-enriched rafts, we found that both of these proteins were insoluble in Triton X-100 and floated into the lighter fractions of sucrose density gradients. However, disruption of lipid rafts by removal of cholesterol did not cause surface missorting of PLAP and NTR-PLAP, and the altered surface sorting of these proteins after Fumonisin B1 treatment did not correlate with reduced levels in Triton X-100 -insoluble fractions. Furthermore, in contrast to the GPI-anchored forms of both of these proteins, the secretory and transmembrane forms (in the absence of a basolateral cytoplasmic signal) were sorted to the apical surface without association with lipid microdomains. Together, these data demonstrate that the GPI anchor is required to mediate raft association but is not sufficient to determine apical sorting. They also suggest that signals present in the ectodomain of the proteins play a major role and that lipid rafts may facilitate the recognition of these signals in the trans-Golgi network, even though they are not required for apical sorting.

Indexed as

beta-CyclodextrinsCell PolarityFumonisinsAnimalsBiological TransportCarboxylic AcidsCell LineCell MembraneCentrifugation, Density GradientCholesterolCyclodextrinsGlycosphingolipidsGlycosylphosphatidylinositolsGolgi ApparatusLovastatinMembrane Proteinsbeta-CyclodextrinsCarboxylic AcidsCholesterolCyclodextrinsfumonisin B1FumonisinsGlycosphingolipidsGlycosylphosphatidylinositolsLovastatinMembrane Proteinsmethyl-beta-cyclodextrinOctoxynolphospholipase A2-activating proteinProteinsReceptors, Nerve Growth FactorRecombinant Fusion Proteins

Identifiers

PMID10679012
PMCPMC14791
OpenAlexW2141617312

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.