Evidence map›Paper›PMID 27129206›Full record

ArticleThe Journal of biological chemistry2016

Low or No Inhibitory Potency of the Canonical Galectin Carbohydrate-binding Site by Pectins and Galactomannans.

John Stegmayr, Adriana Lepur, Barbro Kahl-Knutson, Matilde Aguilar-Moncayo, Anatole A Klyosov, Robert A Field, Stina Oredsson, Ulf J Nilsson, Hakon Leffler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 64 citations in OpenAlex.

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  14. Galectin-1 and Galectin-3 in B-Cell Precursor Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2022
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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

9 authors at 2 institutions in 2 countries.

John StegmayrFrom the Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, 221 00 Lund, Sweden, the Department of Biology and john.stegmayr@med.lu.se.ORCID 0000-0002-8167-9259
Adriana LepurFrom the Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, 221 00 Lund, Sweden.
Barbro Kahl-KnutsonFrom the Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, 221 00 Lund, Sweden.
Matilde Aguilar-Moncayothe Department of Biological Chemistry, John Innes Centre, Norwich Research Park, NR4 7UH Norwich, United Kingdom, and.
Anatole A KlyosovGalectin Therapeutics, Newton, Massachusetts 02459.
Robert A Fieldthe Department of Biological Chemistry, John Innes Centre, Norwich Research Park, NR4 7UH Norwich, United Kingdom, and.
Stina Oredssonthe Department of Biology and.
Ulf J NilssonCentre for Analysis and Synthesis, Department of Chemistry, Lund University, Lund, Sweden.
Hakon LefflerFrom the Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, 221 00 Lund, Sweden, hakon.leffler@med.lu.se.ORCID 0000-0003-4482-8945
Lund University · SEJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618
6 · The paper itself

Abstract

Some complex plant-derived polysaccharides, such as modified citrus pectins and galactomannans, have been shown to have promising anti-inflammatory and anti-cancer effects. Most reports propose or claim that these effects are due to interaction of the polysaccharides with galectins because the polysaccharides contain galactose-containing side chains that might bind this class of lectin. However, their direct binding to and/or inhibition of the evolutionarily conserved galactoside-binding site of galectins has not been demonstrated. Using a well established fluorescence anisotropy assay, we tested the direct interaction of several such polysaccharides with physiological concentrations of a panel of galectins. The bioactive pectic samples tested were very poor inhibitors of the canonical galactoside-binding site for the tested galectins, with IC50 values >10 mg/ml for a few or in most cases no inhibitory activity at all. The galactomannan Davanat® was more active, albeit not a strong inhibitor (IC50 values ranging from 3 to 20 mg/ml depending on the galectin). Pure synthetic oligosaccharide fragments found in the side chains and backbone of pectins and galactomannans were additionally tested. The most commonly found galactan configuration in pectins had no inhibition of the galectins tested. Galactosylated tri- and pentamannosides, representing the structure of Davanat®, had an inhibitory effect of galectins comparable with that of free galactose. Further evaluation using cell-based assays, indirectly linked to galectin-3 inhibition, showed no inhibition of galectin-3 by the polysaccharides. These data suggest that the physiological effects of these plant polysaccharides are not due to inhibition of the canonical galectin carbohydrate-binding site.

Indexed as

Antineoplastic AgentsBinding SitesCell Line, TumorDrug Screening Assays, AntitumorFluorescence PolarizationGalactoseGalectinsHemagglutinationHumansInhibitory Concentration 50MannansPectinsPolysaccharidesProtein BindingAntineoplastic AgentsgalactomannanGalactoseGalectinsMannansPectinsPolysaccharidescancer therapydavanatfluorescence anisotropygalactomannangalectinglycobiologyhemagglutinationpectasolpectinpolysaccharide

Identifiers

PMID27129206
PMCPMC4933242
OpenAlexW2342884487

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.