Evidence map›Paper›PMID 9230073›Full record

ArticleThe Journal of cell biology1997

Sphingolipid transport to the apical plasma membrane domain in human hepatoma cells is controlled by PKC and PKA activity: a correlation with cell polarity in HepG2 cells.

M M Zegers, D Hoekstra

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Bile formation and secretion.Comprehensive Physiology · 2013
    Review
  9. Hepatocyte polarity.Comprehensive Physiology · 2013
    Review
  10. Article
  11. Signaling at the Golgi.Cold Spring Harbor perspectives in biology · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

2 authors at 2 institutions in 2 countries.

M M ZegersDepartment of Physiological Chemistry, Faculty of Medical Sciences, University of Groningen, The Netherlands.
D Hoekstra
Institute of Molecular Biology and Biophysics · RUUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of sphingolipid transport to the bile canalicular apical membrane in the well differentiated HepG2 hepatoma cells was studied. By employing fluorescent lipid analogs, trafficking in a transcytosis-dependent pathway and a transcytosis-independent ('direct') route between the trans-Golgi network and the apical membrane were examined. The two lipid transport routes were shown to operate independently, and both were regulated by kinase activity. The kinase inhibitor staurosporine inhibited the direct lipid transport route but slightly stimulated the transcytosis-dependent route. The protein kinase C (PKC) activator phorbol-12 myristate-13 acetate (PMA) inhibited apical lipid transport via both transport routes, while a specific inhibitor of this kinase stimulated apical lipid transport. Activation of protein kinase A (PKA) had opposing effects, in that a stimulation of apical lipid transport via both transport routes was seen. Interestingly, the regulatory effects of either kinase activity in sphingolipid transport correlated with changes in cell polarity. Stimulation of PKC activity resulted in a disappearance of the bile canalicular structures, as evidenced by the redistribution of several apical markers upon PMA treatment, which was accompanied by an inhibition of apical sphingolipid transport. By contrast, activation of PKA resulted in an increase in the number and size of bile canaliculi and a concomitant enhancement of apical sphingolipid transport. Taken together, our data indicate that apical membrane-directed sphingolipid transport in HepG2 cells is regulated by kinases, which could play a role in the biogenesis of the apical plasma membrane domain.

Indexed as

4-Chloro-7-nitrobenzofurazanActin CytoskeletonActinsBile CanaliculiBiological TransportCarcinoma, HepatocellularCarrier ProteinsCell MembraneCell PolarityCeramidesCyclic AMPCyclic AMP-Dependent Protein KinasesEnzyme ActivationEnzyme InhibitorsFluorescent DyesHumans4-Chloro-7-nitrobenzofurazanActinsCarrier ProteinsCeramidesCyclic AMPCyclic AMP-Dependent Protein KinasesEnzyme InhibitorsFluorescent DyesMicrofilament ProteinsN-(7-(4-nitrobenzo-2-oxa-1,3-diazole))-6-aminocaproyl sphingosineN-(N-(7-nitro-2,1,3-benzoxadiazol-4-yl)-epsilon-aminohexanoyl)sphingosylphosphorylcholineProtein Kinase CSphingolipidsSphingomyelinsStaurosporineTetradecanoylphorbol Acetatevillin

Identifiers

PMID9230073
PMCPMC2138192
OpenAlexW1973200119

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.