Evidence map›Paper›PMID 33315264›Full record

ReviewImmunology2021

The turning away of serum amyloid A biological activities and receptor usage.

Sara Abouelasrar Salama, Mieke Gouwy, Jo Van Damme, Sofie Struyf

Open access · bronzeAbstract readReview
In one paragraph

Review in Immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Host Serum Amyloid A1 FacilitatesMicroorganisms · 2025
    Article
  6. Article
  7. Serum Amyloid A: A Double-Edged Sword in Health and Disease.International journal of molecular sciences · 2025
    Review
  8. Article
  9. Elevated Serum Amyloid A2 and A4 in Patients With Guillain-Barré Syndrome.Journal of clinical neurology (Seoul, Korea) · 2025
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Fpr2 exacerbatesFrontiers in immunology · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Sara Abouelasrar SalamaLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.ORCID 0000-0002-0484-7765
Mieke GouwyLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.ORCID 0000-0002-4035-4810
Jo Van DammeLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.ORCID 0000-0002-6707-1167
Sofie StruyfLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.ORCID 0000-0003-4558-0769
Rega Institute for Medical Research · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serum amyloid A (SAA) is an acute-phase protein (APP) to which multiple immunological functions have been attributed. Regardless, the true biological role of SAA remains poorly understood. SAA is remarkably conserved in mammalian evolution, thereby suggesting an important biological function. Since its discovery in the 1970s, the majority of researchers have investigated SAA using recombinant forms made available through bacterial expression. Nevertheless, recent studies indicate that these recombinant forms of SAA are unreliable. Indeed, commercial SAA variants have been shown to be contaminated with bacterial products including lipopolysaccharides and lipoproteins. As such, biological activities and receptor usage (TLR2, TLR4) revealed through the use of commercial SAA variants may not reflect the inherent nature of this APP. Within this review, we discuss the biological effects of SAA that have been demonstrated through more solid experimental approaches. SAA takes part in the innate immune response via the recruitment of leucocytes and executes, through pathogen recognition, antimicrobial activity. Knockout animal models implicate SAA in a range of functions, such as regulation of T-cell-mediated responses and monopoiesis. Moreover, through its structural motifs, not only does SAA function as an extracellular matrix protein, but it also binds extracellular matrix proteins. Finally, we here also provide an overview of definite SAA receptor-mediated functions and highlight those that are yet to be validated. The role of FPR2 in SAA-mediated leucocyte recruitment has been confirmed; nevertheless, SAA has been linked to a range of other receptors including CD36, SR-BI/II, RAGE and P2RX7.

Indexed as

AnimalsCell MovementExtracellular Matrix ProteinsHumansImmunity, CellularImmunity, InnateMiceMice, KnockoutReceptors, ImmunologicSerum Amyloid A ProteinT-LymphocytesExtracellular Matrix ProteinsReceptors, ImmunologicSerum Amyloid A Proteinchemotaxisimmunityinflammationknockoutserum amyloid A

Identifiers

PMID33315264
PMCPMC8114209
OpenAlexW3111945554

What OpenQuestion holds

Textmetadata
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.