Evidence map›Paper›PMID 28791746›Full record

ArticleProtein science : a publication of the Protein Society2017

Systemic AA amyloidosis in the red fox (Vulpes vulpes).

Anna Rising, Ella Cederlund, Carina Palmberg, Henrik Uhlhorn, Stefan Gaunitz, Kerstin Nordling, Erik Ågren, Elisabet Ihse, Gunilla T Westermark, Lars Tjernberg and 3 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 49% 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

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

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

13 authors at 3 institutions in 1 country.

Anna RisingDepartment of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, 750 07, Sweden.
Ella CederlundDepartment of Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, Stockholm, 171 77, Sweden.
Carina PalmbergCenter of Proteomics Karolinska (PKKI), Karolinska Institutet, Stockholm, 171 77, Sweden.
Henrik UhlhornDepartment of Pathology and Wildlife Diseases, National Veterinary Institute (SVA), Uppsala, 751 89, Sweden.
Stefan GaunitzDepartment of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, Huddinge, 141 57, Sweden.
Kerstin NordlingDepartment of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, Huddinge, 141 57, Sweden.
Erik ÅgrenDepartment of Pathology and Wildlife Diseases, National Veterinary Institute (SVA), Uppsala, 751 89, Sweden.
Elisabet IhseDepartment of Immunology, Genetics and Pathology, Uppsala University, Uppsala, 751 85, Sweden.
Gunilla T WestermarkDepartment of Medical Cell Biology, Uppsala University, Uppsala, 751 23, Sweden.
Lars TjernbergDepartment of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, Huddinge, 141 57, Sweden.
Hans JörnvallDepartment of Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, Stockholm, 171 77, Sweden.
Jan JohanssonDepartment of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, 750 07, Sweden.
Per WestermarkDepartment of Immunology, Genetics and Pathology, Uppsala University, Uppsala, 751 85, Sweden.
Karolinska Institutet · SEUppsala University · SESwedish Veterinary Agency · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid A (AA) amyloidosis occurs spontaneously in many mammals and birds, but the prevalence varies considerably among different species, and even among subgroups of the same species. The Blue fox and the Gray fox seem to be resistant to the development of AA amyloidosis, while Island foxes have a high prevalence of the disease. Herein, we report on the identification of AA amyloidosis in the Red fox (Vulpes vulpes). Edman degradation and tandem MS analysis of proteolyzed amyloid protein revealed that the amyloid partly was composed of full-length SAA. Its amino acid sequence was determined and found to consist of 111 amino acid residues. Based on inter-species sequence comparisons we found four residue exchanges (Ser31, Lys63, Leu71, Lys72) between the Red and Blue fox SAAs. Lys63 seems unique to the Red fox SAA. We found no obvious explanation to how these exchanges might correlate with the reported differences in SAA amyloidogenicity. Furthermore, in contrast to fibrils from many other mammalian species, the isolated amyloid fibrils from Red fox did not seed AA amyloidosis in a mouse model.

Indexed as

Amino Acid SequenceAmyloidosisAnimalsEpidemiological MonitoringFemaleFoxesGene ExpressionKidneyMaleMiceSequence AlignmentSequence Homology, Amino AcidSerum Amyloid A ProteinSpleenSwedenSerum Amyloid A Proteinamyloiddiseaseprotein aggregationseedingserum amyloid A

Identifiers

PMID28791746
PMCPMC5654853
OpenAlexW2744502466

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.