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The surface-exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor
Stefano L, Racchetti G, Bianco F, Passini N, Gupta RS, Panina Bordignon P, Meldolesi J.. Journal of neurochemistry, 2009-04-29
Topic: Brain proteins, microglia and lab models
Plain-language summary
Triggering receptor expressed in myeloid (TREM) cells 2, a receptor expressed by myeloid cells, osteoclasts and microglia, is known to play a protective role in bones and brain. Mutations of the receptor (or of its coupling protein, DAP12) sustain in fact a genetic disease affecting the two organs, the polycystic lipomembraneous osteodysplasia with sclerosing leukoencephalopathy (PLOSL or Nasu-Hakola disease). So far, specific agonist(s) of TREM2 have not been identified and its (their) transduction mechanisms are largely unknown.
What this study adds
Evidence grade: Low
This laboratory study identifies Hsp60 as an agonist of the microglial TREM2 receptor, a receptor whose mutations cause a genetic disease affecting bone and brain. It is early mechanistic work and does not test any treatment in patients.
Taken from this record’s own fields, not from reading the paper. The grade is assigned from the abstract’s wording; what that means.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Stefano, L., Racchetti, G., Bianco, F., Passini, N., Gupta, R. S., Panina Bordignon, P., et al. (2009). The surface-exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor. Journal of neurochemistry. https://doi.org/10.1111/j.1471-4159.2009.06130.x
Vancouver
Stefano L, Racchetti G, Bianco F, Passini N, Gupta RS, Panina Bordignon P, et al. The surface-exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor. Journal of neurochemistry. 2009. doi:10.1111/j.1471-4159.2009.06130.x. PMID: 19457124.
BibTeX
@article{stefano2009-19457124,
author = {Stefano, L. and Racchetti, G. and Bianco, F. and Passini, N. and Gupta, R. S. and Panina Bordignon, P. and Meldolesi, J.},
title = {{The surface-exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor}},
journal = {Journal of neurochemistry},
year = {2009},
doi = {10.1111/j.1471-4159.2009.06130.x},
pmid = {19457124},
url = {https://doi.org/10.1111/j.1471-4159.2009.06130.x}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.
Key findings
- Mutations of the receptor (or of its coupling protein, DAP12) sustain in fact a genetic disease affecting the two organs, the polycystic lipomembraneous osteodysplasia with sclerosing leukoencephalopathy (PLOSL or Nasu-Hakola disease).
- So far, specific agonist(s) of TREM2 have not been identified and its (their) transduction mechanisms are largely unknown.
- Heat shock protein 60 (Hsp60) is a mitochondrial chaperone that can also be harboured at the cell surface.
- By using constructs including the extracellular domain of TREM2 and the Fc domain of IgGs we have identified Hsp60 as the only TREM2-binding protein exposed at the surface of neuroblastoma N2A cells and astrocytes, and lacking in U373 astrocytoma.
Why it matters
This laboratory study identifies Hsp60 as an agonist of the microglial TREM2 receptor, a receptor whose mutations cause a genetic disease affecting bone and brain. It is early mechanistic work and does not test any treatment in patients.
New to this subject? Start with our plain-English guide: Genetics →
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 randomized / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Journal of neurochemistry) |
| Journal's citation record | 3 / 4 | Journal of Neurochemistry: journal h-index 349 (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 | 1 / 5 | 2009 — within 20 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) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 152 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 8.0 citations a year over 19 year(s) since 2009 |
| Impact for its field and year | 3 / 6 | Cited 3.1× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 4 / 6 | Cited by 31 other studies in this library |
| Still being cited | 2 / 4 | Cited 29 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Jacopo Meldolesi: h-index 87 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | McMaster University: institution h-index 1,334 (OpenAlex) |
| Multicenter collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 19457124) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 46 / 100 | — |
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