Evidence map›Paper›PMID 31742330›Full record

ArticleGlycobiology2020

Modulation of hepatocyte sialylation drives spontaneous fatty liver disease and inflammation.

Douglas M Oswald, Mark B Jones, Brian A Cobb

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. M2-Like Macrophages Exhibit Sialic Acid-Enhanced Efferocytosis via the Siglec CD22.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
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  7. Article
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  10. Review
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  15. Article
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  17. Article
  18. Suppression of age-related salivary gland autoimmunity by glycosylation-dependent galectin-1-driven immune inhibitory circuits.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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.

Douglas M OswaldDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Mark B JonesDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Brian A CobbDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
University School · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI Amar Desai · 1987 to 2026
$142.3M
Regulatory Mechanisms of Glycoprotein SialylationR01GM115234 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Brian A Cobb · 2016 to 2026
$5.1M
Immunology Training Program-PredoctoralT32AI089474 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2010 to 2025
$3.4M
NCI NIH HHS P30 CA043703NIAID NIH HHS T32 AI089474NIGMS NIH HHS R01 GM115234
6 · The paper itself

Abstract

Circulatory protein glycosylation is a biomarker of multiple disease and inflammatory states and has been applied in the clinic for liver dysfunction, heart disease and diabetes. With the notable exception of antibodies, the liver produces most of the circulatory glycoproteins, including the acute phase proteins released as a function of the inflammatory response. Among these proteins is β-galactoside α2,6-sialyltransferase (ST6Gal1), an enzyme required for α2,6-linked sialylation of glycoproteins. Here, we describe a hepatocyte-specific conditional knockout of ST6Gal1 (H-cKO) using albumin promoter-driven Cre-lox recombination. We confirm the loss of circulatory glycoprotein α2,6 sialylation and note no obvious dysfunction or pathology in young H-cKO mice, yet these mice show robust changes in plasma glycoprotein fucosylation, branching and the abundance of bisecting GlcNAc and marked changes in a number of metabolic pathways. As H-cKO mice aged, they spontaneously developed fatty liver disease characterized by the buildup of fat droplets in the liver, inflammatory cytokine production and a shift in liver leukocyte phenotype away from anti-inflammatory Kupffer cells and towards proinflammatory M1 macrophages. These findings connect hepatocyte and circulatory glycoprotein sialylation to the regulation of metabolism and inflammation, potentially identifying the glycome as a new target for liver-driven disease.

Indexed as

AnimalsGlycoproteinsGlycosylationHepatocytesInflammationMiceMice, KnockoutNon-alcoholic Fatty Liver DiseaseGlycoproteinshepatocyteinflammationliver metabolismmacrophageST6Gal1

Identifiers

PMID31742330
PMCPMC7175972
OpenAlexW2989916302

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.