Sialylation Modulates Basophil Responsiveness to Galectin-3-dependent Activation

Clicks: 1
ID: 318898
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal

Ranked #85 of 88 articles by views in journal of leukocyte biology

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Basophils secrete histamine and IL-4/13 when co-cultured with human lung adenocarcinoma cells (A549 cells). Previous studies have revealed that this interaction is dependent on Galectin-3 expression on the surface of A549 cells (EC-Gal-3), IgE present on the surface of IL-3 primed basophils, and direct physical interaction between the two cell types, indicating a cognate interaction between IgE and Gal-3. Reciprocal secretion of pro-tumorigenic cytokines (IL-6/VEGF-A) from A549 cells also results. Here, we further define the biological parameters required for this mode of activation. EC-Gal-3 stimulus has ∼ 20-fold less IgE cross-linking capacity compared with standard anti-IgE. The capacity of IgE-bearing basophils to elicit an EC-Gal-3-mediated response correlates with their responsiveness to standard anti-IgE stimulation, which is known to vary widely among individuals. However, unlike standard anti-IgE stimulation, basophil releasability in response to EC-Gal-3 is influenced by glycosylation patterns on surface-bound IgE. Specifically, bulk sialylation on IgE molecules suppress cellular releasability. Whole cell basophil sialylation also suppresses EC-Gal-3 mediated activation. Gal-3 is an endogenous lectin with multivalent binding capacity and is implicated in a range of diseases involving immune modulation, organ fibrosis, and tumor metastasis. These results can help identify specific physiological and pathophysiological conditions by which IgE:Gal-3 interactions help drive disease processes including wound healing, cancer, and fibrosis, including that which occurs in asthma.
Reference Key
openalex_W7166033393 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Laurent Ehrlich, Donald W. MacGlashan, Robert Anthony, Michelle Conroy, Anja P. Bieneman, John T. Schroeder
Journal journal of leukocyte biology
Year 2026
DOI
10.1093/jleuko/qiag087
URL
https://doi.org/10.1093/jleuko/qiag087
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.