Evidence map›Paper›PMID 20304916›Full record

ArticleThe Journal of biological chemistry2010

Distribution and function of macrophage galactose-type C-type lectin 2 (MGL2/CD301b): efficient uptake and presentation of glycosylated antigens by dendritic cells.

Kaori Denda-Nagai, Satoshi Aida, Kengo Saba, Kiwamu Suzuki, Saya Moriyama, Sarawut Oo-Puthinan, Makoto Tsuiji, Akiko Morikawa, Yosuke Kumamoto, Daisuke Sugiura and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

53 citing papers in PubMed, 93 citations in OpenAlex.

  1. Science advances · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Macrophage Gal/GalNAc lectin 2 (MGL2)Scientific reports · 2022
    Article
  17. Resolution of Eczema with Multivalent Peptides.JID innovations : skin science from molecules to population health · 2022
    Article
  18. Article
  19. Article
  20. ASGR1 and Its Enigmatic Relative, CLEC10A.International journal of molecular sciences · 2020
    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

15 authors at 4 institutions in 2 countries.

Kaori Denda-NagaiLaboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Satoshi Aida
Kengo Saba
Kiwamu Suzuki
Saya Moriyama
Sarawut Oo-Puthinan
Makoto Tsuiji
Akiko Morikawa
Yosuke Kumamoto
Daisuke Sugiura
Akihiko Kudo
Yoshihiro Akimoto
Hayato Kawakami
Nicolai V Bovin
Tatsuro Irimura
The University of Tokyo · JPKyorin University · JPHoshi University · JPInstitute of Bioorganic Chemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dendritic cells (DCs) express cell surface lectins that are potentially involved in the recognition, uptake, and presentation of glycosylated foreign substances. A unique calcium-type (C-type) lectin, the macrophage galactose (Gal)-type C-type lectin (MGL/CD301) expressed on DCs, is thought to participate in the recognition of molecules from both altered self and pathogens due to its monosaccharide specificity for Gal and N-acetylgalactosamine (GalNAc). Although mice have two MGL genes, Mgl1 and Mgl2, their distinct roles have not been previously explored. The present report characterizes the properties of MGL2 by examining its distribution and its role in antigen presentation by DCs. We generated an MGL2-specific monoclonal antibody and examined MGL2 expression in tissues by immunohistochemistry and in isolated cells by flow cytometry. The cells reactive with this antibody were shown to be a portion of MGL1-expressing cells, mostly conventional DCs. Internalization of soluble polyacrylamide polymers (PAA) with alpha-GalNAc residues (GalNAc-PAA) by bone marrow-derived DCs (BM-DCs) was mediated by MGL2, as revealed by a comparison of Mgl1(-/-) and Mgl2(-/-) BM-DCs with wild-type BM-DCs. Biotinylated GalNAc-PAA conjugated to streptavidin (SAv) was more efficiently presented to SAv-primed T cells by BM-DCs than beta-N-acetylglucosamine-PAA conjugated to SAv or SAv alone as shown by thymidine uptake and cytokine production. This is the first report that demonstrates the involvement of GalNAc residues in antigen uptake and presentation by DCs that lead to CD4(+) T cell activation.

Indexed as

AnimalsAntigensBone Marrow CellsCHO CellsCricetinaeCricetulusDendritic CellsFemaleFlow CytometryGlycosylationImmunohistochemistryLectins, C-TypeLymphocyte ActivationMiceMice, Inbred C57BLTissue DistributionAntigensLectins, C-TypeMGL2 protein, mouse

Identifiers

PMID20304916
PMCPMC2885198
OpenAlexW2077567806

What OpenQuestion holds

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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.