Evidence map›Paper›PMID 22441700›Full record

ArticleInnate immunity2012

Hepatic uptake and deacylation of the LPS in bloodborne LPS-lipoprotein complexes.

Baomei Shao, Robert S Munford, Richard Kitchens, Alan W Varley

Open access · bronzeAbstract read
In one paragraph

Article in Innate immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

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  11. Impact of High-Density Lipoproteins on Sepsis.International journal of molecular sciences · 2022
    Review
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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

4 authors at 2 institutions in 1 country.

Baomei ShaoDepartment of Internal Medicine, Division of Infectious Diseases, The University of Texas Southwestern Medical Center, Dallas, TX 75390-9113, USA.
Robert S Munford
Richard Kitchens
Alan W Varley
The University of Texas Southwestern Medical Center · USNational Institutes of Health · US

Funding

Endotoxin DetoxificationZIAAI001139 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MUNFORD, ROBERT · 2011 to 2022
$8.2M
Antibacterial Host DefenseZIAAI001138 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MUNFORD, ROBERT · 2011 to 2021
$4.4M
INTERACTIONS OF ENDOTOXIN WITH PLASMA AND CELLSR01AI018188 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI VARLEY, ALAN WAYNE · 1985 to 2011
$3.9M
LPS EFFLUX HOST CELLS TO PLASMA LIPOPROTEINSR01AI045896 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI KITCHENS, RICHARD L. · 2000 to 2009
$2.6M
INTERACTIONS OF ENDOTOXIN WITH PLASMA AND CELLSR37AI018188 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI MUNFORD, ROBERT S · 1992 to 2001
$729k
Interactions of Endotoxin with Plasma and CellsR56AI018188 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI MUNFORD, ROBERT S · 2007 to 2007
$523k
Intramural NIH HHS Z99 AI999999Intramural NIH HHS ZIA AI001138Intramural NIH HHS ZIA AI001139NIAID NIH HHS AI-018188NIAID NIH HHS AI-045896NIAID NIH HHS R01 AI018188NIAID NIH HHS R01 AI045896NIAID NIH HHS R37 AI018188NIAID NIH HHS R56 AI018188
6 · The paper itself

Abstract

Much evidence indicates that bacterial LPS (endotoxin) is removed from the bloodstream mainly by the liver, yet the hepatic uptake mechanisms remain uncertain and controversial. In plasma, LPS can be either 'free' (as aggregates, bacterial membrane fragments or loosely bound to albumin, CD14, or other proteins) or 'bound' (complexed with lipoproteins). Whereas most free LPS is taken up by Kupffer cells (KCs), lipoprotein-bound LPS has seemed to be cleared principally by hepatocytes. Here, we compared the liver's ability to take up and deacylate free LPS aggregates and the LPS in preformed LPS-high density lipoprotein (HDL) complexes. In mice examined from 1 h to 7 d after a small amount of fluorescent (FITC-)LPS was injected into a lateral tail vein, we found FITC-LPS almost entirely within, or adjacent to, KCs. As expected, FITC-LPS complexed with HDL (FITC-LPS-HDL) disappeared more slowly from the circulation and a smaller fraction of the injected dose of FITC-LPS was found in the liver. Unexpectedly, the FITC-LPS injected as FITC-LPS-HDL complexes was also found within sinusoids, adjacent to, or within, KCs. In other experiments, we found that both free and HDL-bound radiolabeled LPS underwent enzymatic deacylation by acyloxyacyl hydrolase (AOAH), the LPS-inactivating enzyme that is principally produced within the liver by KCs. Our observations suggest that KCs and AOAH play important roles in clearing and catabolizing both free LPS and the LPS in circulating LPS-HDL complexes.

Indexed as

AcylationAnimalsBiological TransportCarboxylic Ester HydrolasesCells, CulturedFluorescein-5-isothiocyanateHepatocytesKupffer CellsLipopolysaccharidesLipoproteinsMiceMice, Inbred C57BLMice, KnockoutPhagocytosisacyloxyacyl hydrolaseCarboxylic Ester HydrolasesFluorescein-5-isothiocyanateLipopolysaccharidesLipoproteins

Identifiers

PMID22441700
PMCPMC4120711
OpenAlexW2110791654

What OpenQuestion holds

Textmetadata
LicenceTDM
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.