Evidence map›Paper›PMID 22613794›Full record

ArticleBlood2012

The origin and function of platelet glycosyltransferases.

Hans H Wandall, Viktoria Rumjantseva, Anne Louise Tølbøll Sørensen, Sunita Patel-Hett, Emma C Josefsson, Eric P Bennett, Joseph E Italiano, Henrik Clausen, John H Hartwig, Karin M Hoffmeister

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

59 citing papers in PubMed, 101 citations in OpenAlex.

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  8. Complement, Coagulation, and Fibrinolysis: The Role of the Endothelium and Its Glycocalyx Layer in Xenotransplantation.Transplant international : official journal of the European Society for Organ Transplantation · 2024
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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.

Hans H WandallCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, Copenhagen N, Denmark. hhw@sund.ku.dk
Viktoria Rumjantseva
Anne Louise Tølbøll Sørensen
Sunita Patel-Hett
Emma C Josefsson
Eric P Bennett
Joseph E Italiano
Henrik Clausen
John H Hartwig
Karin M Hoffmeister
Harvard University · USBrigham and Women's Hospital · USUniversity of Copenhagen · DK

Funding

PREVENTION OF COLD INDUCED PLATELET STORAGE LESIONP01HL056949 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI WAGNER, DENISA D · 1996 to 2010
$26.2M
REGULATION OF LACTOSAMINYL GLYCAN BIOSYNTHESIS IN HEMATOPOIETIC CELLSP01HL107146 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI SACKSTEIN, ROBERT · 2011 to 2017
$17.7M
Carbohydrate-Mediated Platelet ClearanceR01HL089224 · NHLBI · VERSITI WISCONSIN, INC. · PI Karin Maria Hoffmeister · 2007 to 2026
$9.3M
Cytoskeletal Mechanisms of Platelet FormationR01HL068130 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI ITALIANO, JOSEPH E · 2001 to 2021
$8.1M
NHLBI NIH HHS HL089224NHLBI NIH HHS HL56949NHLBI NIH HHS HL68130NHLBI NIH HHS P01 HL056949NHLBI NIH HHS P01 HL107146NHLBI NIH HHS P01HL107146NHLBI NIH HHS R01 HL068130NHLBI NIH HHS R01 HL089224
6 · The paper itself

Abstract

Platelets are megakaryocyte subfragments that participate in hemostatic and host defense reactions and deliver pro- and antiangiogenic factors throughout the vascular system. Although they are anucleated cells that lack a complex secretory apparatus with distinct Golgi/endoplasmic reticulum compartments, past studies have shown that platelets have glycosyltransferase activities. In the present study, we show that members of 3 distinct glycosyltransferase families are found within and on the surface of platelets. Immunocytology and flow cytometry results indicated that megakaryocytes package these Golgi-derived glycosyltransferases into vesicles that are sent via proplatelets to nascent platelets, where they accumulate. These glycosyltransferases are active, and intact platelets glycosylate large exogenous substrates. Furthermore, we show that activation of platelets results in the release of soluble glycosyltransferase activities and that platelets contain sufficient levels of sugar nucleotides for detection of glycosylation of exogenously added substrates. Therefore, the results of the present study show that blood platelets are a rich source of both glycosyltransferases and donor sugar substrates that can be released to function in the extracellular space. This platelet-glycosylation machinery offers a pathway to a simple glycoengineering strategy improving storage of platelets and may serve hitherto unknown biologic functions.

Indexed as

AnimalsBlood PlateletsGalactosyltransferasesGlycosylationGlycosyltransferasesGolgi ApparatusHumansMaleMegakaryocytesMiceMice, Inbred C57BLMice, KnockoutMultigene FamilyN-AcetylgalactosaminyltransferasesN-Acetylneuraminic AcidPlatelet-Rich PlasmaGalactosyltransferasesGlycosyltransferasesN-AcetylgalactosaminyltransferasesN-Acetylneuraminic AcidPolypeptide N-acetylgalactosaminyltransferaseSialyltransferasesSiat7d protein, mouse

Identifiers

PMID22613794
PMCPMC3401214
OpenAlexW2077939074

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.