Evidence map›Paper›PMID 25601960›Full record

ArticleJournal of lipid research2015

ABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner.

Yu Zhao, Masato Ishigami, Kohjiro Nagao, Kentaro Hanada, Nozomu Kono, Hiroyuki Arai, Michinori Matsuo, Noriyuki Kioka, Kazumitsu Ueda

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Structural mechanisms of CFTR function and dysfunction.The Journal of general physiology · 2018
    Review
  7. Article
  8. 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 3 institutions in 1 country.

Yu ZhaoInstitute for integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto 606-8502, Japan.
Masato IshigamiLaboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate School of Agriculture, Kyoto 606-8502, Japan.
Kohjiro NagaoInstitute for integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto 606-8502, Japan.
Kentaro HanadaDepartment of Biochemistry & Cell Biology, National Institute of Infectious Diseases, 1-23-1, Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.
Nozomu KonoGraduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
Hiroyuki AraiGraduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
Michinori MatsuoLaboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate School of Agriculture, Kyoto 606-8502, Japan.
Noriyuki KiokaLaboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate School of Agriculture, Kyoto 606-8502, Japan.
Kazumitsu UedaInstitute for integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto 606-8502, Japan; Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate School of Agriculture, Kyoto 606-8502, Japan. Electronic address: uedak@kais.kyoto-u.ac.jp.
Kyoto University · JPThe University of Tokyo · JPNational Institute of Infectious Diseases · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ABCB4, which is specifically expressed on the canalicular membrane of hepatocytes, exports phosphatidylcholine (PC) into bile. Because SM depletion increases cellular PC content and stimulates PC and cholesterol efflux by ABCA1, a key transporter involved in generation of HDL, we predicted that SM depletion also stimulates PC efflux through ABCB4. To test this prediction, we compared the lipid efflux activity of ABCB4 and ABCA1 under SM depletion induced by two different types of inhibitors for SM synthesis, myriocin and (1R,3S)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide, in human embryonic kidney 293 and baby hamster kidney cells. Unexpectedly, SM depletion exerted opposite effects on ABCB4 and ABCA1, suppressing PC efflux through ABCB4 while stimulating efflux through ABCA1. Both ABCB4 and ABCA1 were recovered from Triton-X-100-soluble membranes, but ABCB4 was mainly recovered from CHAPS-insoluble SM-rich membranes, whereas ABCA1 was recovered from CHAPS-soluble membranes. These results suggest that a SM-rich membrane environment is required for ABCB4 to function. ABCB4 must have evolved to exert its maximum activity in the SM-rich membrane environment of the canalicular membrane, where it transports PC as the physiological substrate.

Indexed as

AnimalsATP Binding Cassette Transporter 1ATP Binding Cassette Transporter, Subfamily BBiological Transport, ActiveCell MembraneCricetinaeHEK293 CellsHumansPhosphatidylcholinesSphingomyelinsABCA1 protein, humanATP Binding Cassette Transporter 1ATP Binding Cassette Transporter, Subfamily Bmultidrug resistance protein 3PhosphatidylcholinesSphingomyelins(1R,3S)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamideATP binding cassette proteinATP binding cassette transporter A1bile acidcholesterolhigh density lipoproteinmyriosin

Identifiers

PMID25601960
PMCPMC4340311
OpenAlexW2030871899

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.