Evidence map›Paper›PMID 22427662›Full record

ArticleThe Journal of biological chemistry2012

Anti-inflammatory IgG production requires functional P1 promoter in β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1) gene.

Mark B Jones, Mehrab Nasirikenari, Amit A Lugade, Yasmin Thanavala, Joseph T Y Lau

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
3.2field-weighted citation impact, top 9% 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, 60 citations in OpenAlex.

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  16. Article
  17. IgG Fc Glycosylation in Human Immunity.Current topics in microbiology and immunology · 2019
    Review
  18. Review
  19. Review
  20. The Glycoscience of Immunity.Trends in immunology · 2018
    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

5 authors at 1 institution in 1 country.

Mark B JonesDepartment of Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
Mehrab Nasirikenari
Amit A Lugade
Yasmin Thanavala
Joseph T Y Lau
Roswell Park Comprehensive Cancer Center · US

Funding

Two-Spirit Films in Indigenous Cancer HealthP30CA016056 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI Christine B. Ambrosone · 1985 to 2026
$116.6M
REGULATION OF LACTOSAMINYL GLYCAN BIOSYNTHESIS IN HEMATOPOIETIC CELLSP01HL107146 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI RHEINHOLD, VERN · 2011 to 2017
$17.7M
ST6Gal Sialyltransferase in Innate and Adaptive Immune ResponseR01AI056082 · NIAID · ROSWELL PARK CANCER INSTITUTE CORP · PI LAU, JOSEPH TY · 2006 to 2015
$3.6M
Innate and adaptive immune response to bacterial infections in COPD patientsR56AI069379 · NIAID · ROSWELL PARK CANCER INSTITUTE CORP · PI THANAVALA, YASMIN · 2008 to 2009
$890k
NCI NIH HHS CA16056NCI NIH HHS P30 CA016056NHLBI NIH HHS P01 HL107146NHLBI NIH HHS P01HL107146NIAID NIH HHS R01 AI056082NIAID NIH HHS R01 AI069379NIAID NIH HHS R01AI38193NIAID NIH HHS R56 AI069379
6 · The paper itself

Abstract

The anti-inflammatory properties associated with intravenous immunoglobulin therapy require the sialic acid modification of the N-glycan of the Fc domain of IgG. Sialylation of the Fc fragment is mediated by β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1), acting on the Gal(β4)GlcNAc terminal structure of the biantennary N-glycans on the Fc domain. However, little is known regarding the in vivo regulation of Fc sialylation and its role in the progression of inflammatory processes. Here, we report that decreased Fc sialylation of circulatory IgG accompanies the acute phase response elicited by turpentine exposure or upon acute exposure to either nontypeable Haemophilus influenzae or ovalbumin. However, Fc sialylation was increased 3-fold from the base line upon transition to chronic inflammation by repeated exposure to challenge. The P1 promoter of the ST6Gal-1 gene is critical for Fc sialylation, but P1 does not drive ST6Gal-1 expression in B cells. The Siat1ΔP1 mouse, with a dysfunctional P1 promoter, was unable to produce sialylated Fc in the systemic circulation, despite the presence of Gal(β4)GlcNAc termini on the Fc glycans. The major contribution of P1 action is to synthesize ST6Gal-1 enzymes that are deposited into the systemic circulation. The data strongly indicate that this pool of extracellular ST6Gal-1 in the blood impacts the sialylation of IgG Fc and that defective Fc sialylation is likely a major contributing mechanism for the proinflammatory tendencies previously noted in Siat1ΔP1 animals.

Indexed as

Acute-Phase ReactionAnimalsAnti-Inflammatory Agentsbeta-D-Galactoside alpha 2-6-SialyltransferaseBlotting, WesternDisease Models, AnimalGene Expression Regulation, EnzymologicHaemophilus InfectionsHaemophilus influenzaeImmunoglobulin Fc FragmentsImmunoglobulin GMiceMice, Inbred C57BLMice, KnockoutN-Acetylneuraminic AcidOvalbuminAnti-Inflammatory Agentsbeta-D-Galactoside alpha 2-6-SialyltransferaseImmunoglobulin Fc FragmentsImmunoglobulin GN-Acetylneuraminic AcidOvalbuminPolysaccharidesSialyltransferasesTurpentine

Identifiers

PMID22427662
PMCPMC3346113
OpenAlexW2007633603

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.