Evidence map›Paper›PMID 25044109›Full record

ArticleBiochemical and biophysical research communications2014

Characterization of rat serum amyloid A4 (SAA4): a novel member of the SAA superfamily.

Christine Rossmann, Christian Windpassinger, Daniela Brunner, Alenka Kovacevic, Natascha Schweighofer, Roland Malli, Rufina Schuligoi, Andreas Prokesch, Barbara Kluve-Beckerman, Wolfgang F Graier and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. SAA4: An Underdog Within the Serum Amyloid a Superfamily?International journal of molecular sciences · 2026
    Review
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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

13 authors at 3 institutions in 2 countries.

Christine RossmannInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Christian WindpassingerInstitute of Human Genetics, Medical University of Graz, Graz, Austria.
Daniela BrunnerInstitute of Human Genetics, Medical University of Graz, Graz, Austria.
Alenka KovacevicInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Natascha SchweighoferInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Roland MalliInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Rufina SchuligoiInstitute of Experimental and Clinical Pharmacology, Medical University of Graz, Graz, Austria.
Andreas ProkeschInstitute of Cell Biology, Histology and Embryology, Medical University of Graz, Graz, Austria; Institute of Biochemistry, Graz University of Technology, Graz, Austria.
Barbara Kluve-BeckermanDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Wolfgang F GraierInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Dagmar KratkyInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Wolfgang SattlerInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
Ernst MalleInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria. Electronic address: ernst.malle@medunigraz.at.
Medical University of Graz · ATGraz University of Technology · ATIndiana University School of Medicine

Funding

Austrian Science Fund FWF F 3004Austrian Science Fund FWF F 3007Austrian Science Fund FWF P 19074
6 · The paper itself

Abstract

The serum amyloid A (SAA) family of proteins is encoded by multiple genes, which display allelic variation and a high degree of homology in mammals. The SAA1/2 genes code for non-glycosylated acute-phase SAA1/2 proteins, that may increase up to 1000-fold during inflammation. The SAA4 gene, well characterized in humans (hSAA4) and mice (mSaa4) codes for a SAA4 protein that is glycosylated only in humans. We here report on a previously uncharacterized SAA4 gene (rSAA4) and its product in Rattus norvegicus, the only mammalian species known not to express acute-phase SAA. The exon/intron organization of rSAA4 is similar to that reported for hSAA4 and mSaa4. By performing 5'- and 3'RACE, we identified a 1830-bases containing rSAA4 mRNA (including a GA-dinucleotide tandem repeat). Highest rSAA4 mRNA expression was detected in rat liver. In McA-RH7777 rat hepatoma cells, rSAA4 transcription was significantly upregulated in response to LPS and IL-6 while IL-1α/β and TNFα were without effect. Luciferase assays with promoter-truncation constructs identified three proximal C/EBP-elements that mediate expression of rSAA4 in McA-RH7777 cells. In line with sequence prediction a 14-kDa non-glycosylated SAA4 protein is abundantly expressed in rat liver. Fluorescence microscopy revealed predominant localization of rSAA4-GFP-tagged fusion protein in the ER.

Indexed as

AnimalsCell Line, TumorLiverPolymerase Chain ReactionPromoter Regions, GeneticRatsRats, Sprague-DawleySerum Amyloid A ProteinSAA4 protein, ratSerum Amyloid A ProteinInflammationLuciferase assayPromoter activityRat SAA

Identifiers

PMID25044109
PMCPMC4145149
OpenAlexW2075225234

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.