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Sialylation and Galectin-3 in Microglia-Mediated Neuroinflammation and Neurodegeneration
Puigdellívol M, Allendorf DH, Brown GC.. Frontiers in cellular neuroscience, 2020-06-09
Topic: Brain proteins, microglia and lab models
Microglia are brain macrophages that mediate neuroinflammation and contribute to and protect against neurodegeneration. The terminal sugar residue of all glycoproteins and glycolipids on the surface of mammalian cells is normally sialic acid, and addition of this negatively charged residue is known as "sialylation," whereas removal by sialidases is known as "desialylation." High sialylation of the neuronal cell surface inhibits microglial phagocytosis of such neurons, via: (i) activating sialic acid receptors (Siglecs) on microglia that inhibit phagocytosis and (ii) inhibiting binding of opsonins C1q, C3, and galectin-3. Microglial sialylation inhibits inflammatory activation of microglia via: (i) activating Siglec receptors CD22 and CD33 on microglia that inhibit phagocytosis and (ii) inhibiting Toll-like receptor 4 (TLR4), complement receptor 3 (CR3), and other microglial receptors.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Puigdellívol, M., Allendorf, D. H., & Brown, G. C. (2020). Sialylation and Galectin-3 in Microglia-Mediated Neuroinflammation and Neurodegeneration. Frontiers in cellular neuroscience. https://doi.org/10.3389/fncel.2020.00162
Vancouver
Puigdellívol M, Allendorf DH, Brown GC. Sialylation and Galectin-3 in Microglia-Mediated Neuroinflammation and Neurodegeneration. Frontiers in cellular neuroscience. 2020. doi:10.3389/fncel.2020.00162. PMID: 32581723.
BibTeX
@article{puigdellivol2020-32581723,
author = {Puigdellívol, M. and Allendorf, D. H. and Brown, G. C.},
title = {{Sialylation and Galectin-3 in Microglia-Mediated Neuroinflammation and Neurodegeneration}},
journal = {Frontiers in cellular neuroscience},
year = {2020},
doi = {10.3389/fncel.2020.00162},
pmid = {32581723},
url = {https://doi.org/10.3389/fncel.2020.00162}
}
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Key findings
- The terminal sugar residue of all glycoproteins and glycolipids on the surface of mammalian cells is normally sialic acid, and addition of this negatively charged residue is known as "sialylation," whereas removal by sialidases is known as "desialylation." High sialylation of the neuronal cell surface inhibits microglial phagocytosis of such neurons, via: (i) activating sialic acid receptors (Siglecs) on microglia that inhibit phagocytosis and (ii) inhibiting binding of opsonins C1q, C3, and galectin-3.
- Microglial sialylation inhibits inflammatory activation of microglia via: (i) activating Siglec receptors CD22 and CD33 on microglia that inhibit phagocytosis and (ii) inhibiting Toll-like receptor 4 (TLR4), complement receptor 3 (CR3), and other microglial receptors.
- When activated, microglia release a sialidase activity that desialylates both microglia and neurons, activating the microglia and rendering the neurons susceptible to phagocytosis.
- Activated microglia also release galectin-3 (Gal-3), which: (i) further activates microglia via binding to TLR4 and TREM2, (ii) binds to desialylated neurons opsonizing them for phagocytosis via Mer tyrosine kinase, and (iii) promotes Aβ aggregation and toxicity in vivo .
Why it matters
This review describes how sialylation on cells can inhibit microglial phagocytosis and inflammatory activation through receptors such as Siglecs. It is a conceptual overview and does not report a treatment, cure, or prevention for Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 46/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Frontiers in cellular neuroscience) |
| Journal's citation record | 2 / 4 | Frontiers in Cellular Neuroscience: journal h-index 175 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 2 / 5 | 2020 — within 10 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 141 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 17.6 citations a year over 8 year(s) since 2020 |
| Impact for its field and year | 3 / 6 | Cited 5.7× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 3 / 4 | Cited 70 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Guy Charles Brown: h-index 88 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | University of Cambridge: institution h-index 1,973 (OpenAlex) |
| Multi-centre collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 32581723) |
| Free to read | 2 / 2 | Free to read |
| Total | 46 / 100 | — |
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Read the original
- DOI: 10.3389/fncel.2020.00162
- PubMed: 32581723
- Original source →
- Free full text: Frontiers in Cellular Neuroscience →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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