Evidence map›Paper›PMID 26124096›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

O-glycans direct selectin ligands to lipid rafts on leukocytes.

Bojing Shao, Tadayuki Yago, Hendra Setiadi, Ying Wang, Padmaja Mehta-D'souza, Jianxin Fu, Paul R Crocker, William Rodgers, Lijun Xia, Rodger P McEver

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-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

32 citing papers in PubMed, 55 citations in OpenAlex.

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  11. Increased plasmin-mediated proteolysis of L1CAM in a mouse model of idiopathic normal pressure hydrocephalus.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  12. Molecular therapy. Methods & clinical development · 2021
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  13. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
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  14. 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

10 authors at 3 institutions in 2 countries.

Bojing ShaoCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Tadayuki YagoCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Hendra SetiadiCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Ying WangCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104; Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104;
Padmaja Mehta-D'souzaCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Jianxin FuCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Paul R CrockerDivision of Cell Signaling and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.
William RodgersDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104;
Lijun XiaCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104; Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104;
Rodger P McEverCardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104; Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104; rodger-mcever@omrf.org.
Oklahoma Medical Research Foundation · USUniversity of Oklahoma Health Sciences Center · USUniversity of Dundee · GB

Funding

Protein-glycan Interactions in the Vascular SystemP01HL085607 · NHLBI · OKLAHOMA MEDICAL RESEARCH FOUNDATION · PI CUMMINGS, RICHARD D, MCEVER, RODGER PAUL · 2006 to 2015
$16.8M
Signal-dependent neutrophil adhesion to vascular surfacesR01HL034363 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MCEVER, RODGER PAUL · 1985 to 2017
$3.9M
CYTOPLASMIC REGULATION OF P-SELECTIN/PSGL-1 INTERACTIONSR37HL034363 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MCEVER, RODGER PAUL · 1998 to 2007
$3.3M
NHLBI NIH HHS HL034363NHLBI NIH HHS HL085607NHLBI NIH HHS P01 HL085607NHLBI NIH HHS R01 HL034363NHLBI NIH HHS R37 HL034363Wellcome TrustWellcome Trust WT103744MA
6 · The paper itself

Abstract

Palmitoylated cysteines typically target transmembrane proteins to domains enriched in cholesterol and sphingolipids (lipid rafts). P-selectin glycoprotein ligand-1 (PSGL-1), CD43, and CD44 are O-glycosylated proteins on leukocytes that associate with lipid rafts. During inflammation, they transduce signals by engaging selectins as leukocytes roll in venules, and they move to the raft-enriched uropods of polarized cells upon chemokine stimulation. It is not known how these glycoproteins associate with lipid rafts or whether this association is required for signaling or for translocation to uropods. Here, we found that loss of core 1-derived O-glycans in murine C1galt1(-/-) neutrophils blocked raft targeting of PSGL-1, CD43, and CD44, but not of other glycosylated proteins, as measured by resistance to solubilization in nonionic detergent and by copatching with a raft-resident sphingolipid on intact cells. Neuraminidase removal of sialic acids from wild-type neutrophils also blocked raft targeting. C1galt1(-/-) neutrophils or neuraminidase-treated neutrophils failed to activate tyrosine kinases when plated on immobilized anti-PSGL-1 or anti-CD44 F(ab')2. Furthermore, C1galt1(-/-) neutrophils incubated with anti-PSGL-1 F(ab')2 did not generate microparticles. In marked contrast, PSGL-1, CD43, and CD44 moved normally to the uropods of chemokine-stimulated C1galt1(-/-) neutrophils. These data define a role for core 1-derived O-glycans and terminal sialic acids in targeting glycoprotein ligands for selectins to lipid rafts of leukocytes. Preassociation of these glycoproteins with rafts is required for signaling but not for movement to uropods.

Indexed as

AnimalsHyaluronan ReceptorsLeukocytesLeukosialinLigandsMembrane GlycoproteinsMembrane MicrodomainsMicePolysaccharidesCd44 protein, mouseHyaluronan ReceptorsLeukosialinLigandsMembrane GlycoproteinsPolysaccharidesP-selectin ligand proteincell adhesioncell signalinginflammationneutrophiluropod

Identifiers

PMID26124096
PMCPMC4507194
OpenAlexW1680182901

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.