Evidence map›Paper›PMID 40747832›Full record

ReviewJournal of leukocyte biology2025

Posttranslational sialylation and its impact on neutrophil recruitment.

Katrin Nussbaumer, Jamey D Marth, Markus Sperandio

Abstract readReview
In one paragraph

Review in Journal of leukocyte biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

3 authors.

Katrin NussbaumerInstitute of Cardiovascular Physiology and Pathophysiology, Biomedical Center, Ludwig-Maximilian University, Großhaderner Str. 9, Planegg-Martinsried 82152, Munich, Germany.ORCID 0009-0001-7240-9599
Jamey D MarthSanford Burnham Prebys Medical Discovery Institute, La Jolla, 10901 N Torrey Pines Rd, La Jolla, CA 92037, United States.
Markus SperandioInstitute of Cardiovascular Physiology and Pathophysiology, Biomedical Center, Ludwig-Maximilian University, Großhaderner Str. 9, Planegg-Martinsried 82152, Munich, Germany.ORCID 0000-0002-7689-3613

Funding

Protein Glycosylation in the Coagulopathy and Inflammation of SepsisP01HL131474 · NHLBI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MAHAN, MICHAEL J · 2016 to 2025
$26.2M
GLYCOSYLTRANSFERASE FUNCTION IN DEVELOPMENT AND DISEASER01DK048247 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JAMEY MARTH · 1994 to 2026
$9.4M
Protein Sialylation and De-Sialyation in Cell Surface Glycoprotein Homeostasis and DiseaseR01AI151371 · NIAID · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARTH, JAMEY · 2021 to 2025
$2.4M
Regulation of Blood Glycoproteins by Lectin Receptors in Health and DiseaseR01HL158677 · NHLBI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI JAMEY MARTH · 2023 to 2026
$1.9M
German Research Foundation 449437943German Research Foundation #491676693German Research Foundation AI151371German Research Foundation B02 and B07German Research Foundation DK048247German Research Foundation HL131474German Research Foundation HL158677German Research Foundation TRR332German Research Foundation TRR359NHLBI NIH HHS P01 HL131474NHLBI NIH HHS R01 HL158677NIAID NIH HHS R01 AI151371NIDDK NIH HHS R01 DK048247
6 · The paper itself

Abstract

Neutrophils are essential components of the innate immune system, playing a critical role in responding to infections and inflammation. Their recruitment from blood circulation to affected tissues follows a well-coordinated multistep adhesion and activation cascade. Recent studies highlight the importance of posttranslational modifications, particularly sialylation, in regulating neutrophil recruitment. Sialic acids, negatively charged monosaccharides, are attached to glycoproteins and glycolipids on neutrophil surfaces, influencing their stability, signaling, and interactions with endothelial cells. Selectins, key mediators of neutrophil rolling, recognize sialylated ligands such as sialyl Lewis-X on the neutrophil surface enabling the initial capture and rolling process. Additionally, sialylation of chemokine receptors and integrins modulate neutrophil activation and firm adhesion. Beyond recruitment, sialylation affects neutrophil homeostasis, aging, and clearance, as well as their interactions with pathogens and tumor cells. Dysregulation of sialylation has been linked to autoimmune diseases, cancer progression, and infections, making it an interesting target for therapeutic interventions. This review focuses on the functional role of posttranslational sialylation in neutrophil biology, detailing its impact on leukocyte recruitment, immune modulation, and potential therapeutic applications.

Indexed as

Neutrophil InfiltrationNeutrophilsProtein Processing, Post-TranslationalSialic AcidsAnimalsHumansSelectinsSelectinsSialic Acidsadhesionchemokine receptorsneutrophilsposttranslational sialylationrolling

Identifiers

PMID40747832
PMCPMC12952227

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.