Evidence map›Paper›PMID 1447295›Full record

ArticleThe Journal of cell biology1992

5'nucleotidase is sorted to the apical domain of hepatocytes via an indirect route.

M J Schell, M Maurice, B Stieger, A L Hubbard

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

47 citing papers in PubMed, 121 citations in OpenAlex.

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  7. Review
  8. Bile formation and secretion.Comprehensive Physiology · 2013
    Review
  9. Article
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  12. Review
  13. Article
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  15. Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B.American journal of physiology. Gastrointestinal and liver physiology · 2009
    Article
  16. Article
  17. Review
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

M J SchellDepartment of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
M Maurice
B Stieger
A L Hubbard
Johns Hopkins University · US

Funding

BIOLOGY OF DIFFERENTIATED SURFACE DOMAINS IN HEPATOCYTESR01GM029185 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HUBBARD, ANN L · 1985 to 1998
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NIGMS NIH HHS GM29185
6 · The paper itself

Abstract

In hepatocytes, all newly synthesized plasma membrane (PM) proteins so far studied arrive first at the basolateral domain; apically destined proteins are subsequently endocytosed and sorted to the apical domain via transcytosis. A mechanism for the sorting of newly synthesized glycophosphatidylinositol (GPI)-linked proteins has been proposed whereby they associate in lipid microdomains in the trans-Golgi network and then arrive at the apical domain directly. Such a mechanism poses a potential exception to the hepatocyte rule. We have used pulse-chase techniques in conjunction with subcellular fractionation to compare the trafficking of 5' nucleotidase (5NT), an endogenous GPI-anchored protein of hepatocytes, with two transmembrane proteins. Using a one-step fractionation technique to separate a highly enriched fraction of Golgi-derived membranes from ER and PM, we find that both 5NT and the polymeric IgA receptor (pIgAR) traverse the ER and Golgi apparatus with high efficiency. Using a method that resolves PM vesicles derived from the apical and basolateral domains, we find that 5NT first appears at the basolateral domain as early as 30 min of chase. However the subsequent redistribution to the apical domain requires > 3.5 h of chase to reach steady state. This rate of transcytosis is much slower than that observed for dipeptidylpeptidase IV, an apical protein anchored via a single transmembrane domain. We propose that the slow rate of transcytosis is related to the fact that GPI-linked proteins are excluded from clathrin-coated pits/vesicles, and instead must be endocytosed via a slower nonclathrin pathway.

Indexed as

5'-NucleotidaseAnimalsBiological TransportCell CompartmentationCell PolarityGlycoproteinsGlycosylationGlycosylphosphatidylinositolsGlycosyltransferasesGolgi ApparatusLiverMaleMembrane ProteinsRatsRats, Sprague-Dawley5'-NucleotidaseGlycoproteinsGlycosylphosphatidylinositolsGlycosyltransferasesMembrane Proteins

Identifiers

PMID1447295
PMCPMC2289718
OpenAlexW2134748481

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.