Evidence map›Paper›PMID 30816210›Full record

ArticleScientific reports2019

Serum amyloid A binds to fibrin(ogen), promoting fibrin amyloid formation.

Martin J Page, Greig J A Thomson, J Massimo Nunes, Anna-Mart Engelbrecht, Theo A Nell, Willem J S de Villiers, Maria C de Beer, Lize Engelbrecht, Douglas B Kell, Etheresia Pretorius

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 1 pooled it
10.6field-weighted citation impact, top 1% 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

56 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.

  1. Serum amyloid A concentrations, COVID-19 severity and mortality: An updated systematic review and meta-analysis.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2021
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  12. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
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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

10 authors at 3 institutions in 3 countries.

Martin J PageDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.
Greig J A ThomsonDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.
J Massimo NunesDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.
Anna-Mart EngelbrechtDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.
Theo A NellDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.ORCID 0000-0003-3905-827X
Willem J S de VilliersDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa.
Maria C de BeerDepartment of Physiology, Saha Cardiovascular Research Center and Barnstable Brown Diabetes Center, University of Kentucky, Lexington, KY, USA.
Lize EngelbrechtFluorescence Microscopy Unit, Central Analytical Facilities, Stellenbosch University, Stellenbosch, South Africa.
Douglas B KellDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa. dbk@liv.ac.uk.
Etheresia PretoriusDepartment of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 Matieland, 7602, Stellenbosch, South Africa. resiap@sun.ac.za.ORCID 0000-0002-9108-2384
Stellenbosch University · ZAUniversity of Kentucky · USUniversity of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L025752/1
6 · The paper itself

Abstract

Complex associations exist between inflammation and thrombosis, with the inflammatory state tending to promote coagulation. Fibrinogen, an acute phase protein, has been shown to interact with the amyloidogenic ß-amyloid protein of Alzheimer's disease. However, little is known about the association between fibrinogen and serum amyloid A (SAA), a highly fibrillogenic protein that is one of the most dramatically changing acute phase reactants in the circulation. To study the role of SAA in coagulation and thrombosis, in vitro experiments were performed where purified human SAA, in concentrations resembling a modest acute phase response, was added to platelet-poor plasma (PPP) and whole blood (WB), as well as purified and fluorescently labelled fibrinogen. Results from thromboelastography (TEG) suggest that SAA causes atypical coagulation with a fibrin(ogen)-mediated increase in coagulation, but a decreased platelet/fibrin(ogen) interaction. In WB scanning electron microscopy analysis, SAA mediated red blood cell (RBC) agglutination, platelet activation and clumping, but not platelet spreading. Following clot formation in PPP, the presence of SAA increased amyloid formation of fibrin(ogen) as determined both with auto-fluorescence and with fluorogenic amyloid markers, under confocal microcopy. SAA also binds to fibrinogen, as determined with a fluorescent-labelled SAA antibody and correlative light electron microscopy (CLEM). The data presented here indicate that SAA can affect coagulation by inducing amyloid formation in fibrin(ogen), as well as by propelling platelets to a more prothrombotic state. The discovery of these multiple and complex effects of SAA on coagulation invite further mechanistic analyses.

Indexed as

Acute-Phase ReactionAdultAgglutinationAlzheimer DiseaseAmyloidBlood CoagulationBlood PlateletsFemaleFibrinogenHumansMiddle AgedPlatelet ActivationPlatelet AggregationProtein BindingSerum Amyloid A ProteinThrombosisAmyloidFibrinogenSerum Amyloid A Protein

Identifiers

PMID30816210
PMCPMC6395759
OpenAlexW2915895757

What OpenQuestion holds

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LicenceCC BY
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.