ArticleGlycobiology2016
Galectins are human milk glycan receptors.
Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Orthogonal-Group-Controlled Site-Selective I-Branching of Poly-N-acetyllactosamine Chains Reveals Unique Binding Specificities of Proteins towards I-Antigens.Angewandte Chemie (International ed. in English) · 2025Article
- Article
- The potential immunomodulatory role of human milk oligosaccharides in prevention of viral infections and development of asthma in early life.Frontiers in immunology · 2025Review
- Article
- Exploring galectin interactions with human milk oligosaccharides and blood group antigens identifies BGA6 as a functional galectin-4 ligand.The Journal of biological chemistry · 2024Article
- Pectin: Health-promoting properties as a natural galectin-3 inhibitor.Glycoconjugate journal · 2024Review
- Human milk oligosaccharides regulate human macrophage polarization and activation in response toFrontiers in immunology · 2024Article
- Galectins as pivotal components in oncogenesis and immune exclusion in human malignancies.Frontiers in immunology · 2023Review
- Chemoproteomic mapping of human milk oligosaccharide (HMO) interactions in cells.RSC chemical biology · 2022Article
- Galectins-1, -3 and -9 Are Present in Breast Milk and Have a Role in Early Life Development.Nutrients · 2022Article
- Quantifying Biomolecular Interactions Using Slow Mixing Mode (SLOMO) Nanoflow ESI-MS.ACS central science · 2022Article
- Innate immune Galectin-7 specifically targets microbes that decorate themselves in blood group-like antigens.iScience · 2022Article
- Galectin-9 recognizes and exhibits antimicrobial activity toward microbes expressing blood group-like antigens.The Journal of biological chemistry · 2022Article
- Role of milk carbohydrates in intestinal health of nursery pigs: a review.Journal of animal science and biotechnology · 2022Review
- Galectin-3 Decreases 4-1BBL Bioactivity by Crosslinking Soluble and Membrane Expressed 4-1BB.Frontiers in immunology · 2022Article
- Human Milk Oligosaccharides in Cord Blood Are Altered in Gestational Diabetes and Stimulate Feto-Placental Angiogenesis In Vitro.Nutrients · 2021Article
- Influence of sulfonated and diet-derived human milk oligosaccharides on the infant microbiome and immune markers.The Journal of biological chemistry · 2020Article
- Microbiota-dependent and -independent effects of dietary fibre on human health.British journal of pharmacology · 2020Review
- I-branched carbohydrates as emerging effectors of malignant progression.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unique Binding Specificities of Proteins toward Isomeric Asparagine-Linked Glycans.Cell chemical biology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The biological recognition of human milk glycans (HMGs) is poorly understood. Because HMGs are rich in galactose we explored whether they might interact with human galectins, which bind galactose-containing glycans and are highly expressed in epithelial cells and other cell types. We screened a number of human galectins for their binding to HMGs on a shotgun glycan microarray consisting of 247 HMGs derived from human milk, as well as to a defined HMG microarray. Recombinant human galectins (hGal)-1, -3, -4, -7, -8 and -9 bound selectively to glycans, with each galectin recognizing a relatively unique binding motif; by contrast hGal-2 did not recognize HMGs, but did bind to the human blood group A Type 2 determinants on other microarrays. Unlike other galectins, hGal-7 preferentially bound to glycans expressing a terminal Type 1 (Galβ1-3GlcNAc) sequence, a motif that had eluded detection on non-HMG glycan microarrays. Interactions with HMGs were confirmed in a solution setting by isothermal titration microcalorimetry and hapten inhibition experiments. These results demonstrate that galectins selectively bind to HMGs and suggest the possibility that galectin-HMG interactions may play a role in infant immunity.
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Registered trials
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.