Evidence map›Paper›PMID 26790392›Full record

ArticleNature communications2016

D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile.

Sophie Valleix, Guglielmo Verona, Noémie Jourde-Chiche, Brigitte Nédelec, P Patrizia Mangione, Frank Bridoux, Alain Mangé, Ahmet Dogan, Jean-Michel Goujon, Marie Lhomme and 17 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Novel Circulating Biomarkers in Aortic Valve Stenosis.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Review
  5. Renal amyloidosis: a new time for a complete diagnosis.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study.International journal of molecular sciences · 2019
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Hereditary Lysozyme Amyloidosis Variant p.Leu102Ser Associates with Unique Phenotype.Journal of the American Society of Nephrology : JASN · 2017
    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

27 authors at 15 institutions in 5 countries.

Sophie ValleixUniversité Paris-Descartes, Sorbonne Paris Cité, Assistance Publique-Hôpitaux de Paris, Laboratoire de Biologie et Génétique Moléculaire, Hôpital Cochin, Paris 75014, France.
Guglielmo VeronaCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
Noémie Jourde-ChicheUniversité de Marseille, AP-HM, Hôpital de la Conception, Marseille 13005, France.
Brigitte NédelecINSERM, UMR_1163, Institut Imagine, Laboratoire de Génétique Ophtalmologique (LGO), Université Paris Descartes, Sorbonne Paris Cité, Paris 75015, France.
P Patrizia MangioneCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
Frank BridouxUniversité de Poitiers, CHU Poitiers, Department of Nephrology and Kidney Transplantation, Centre National de Référence Amylose AL et autres maladies par dépôts d'immunoglobulines monoclonales, Poitiers 86021, France.
Alain MangéInstitut de Recherche en Cancérologie de Montpellier (IRCM), Montpellier 34298, France.
Ahmet DoganDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55901, USA.
Jean-Michel GoujonUniversité de Poitiers, CHU Poitiers, Service d'Anatomie et Cytologie Pathologiques, Centre National de Référence Amylose AL et autres maladies par dépôts d'immunoglobulines monoclonales, Poitiers 86021, France.
Marie LhommeLipidomic core, ICANalytics, Institute of Cardiometabolism and Nutrition, ICAN, Pitié-Salpôtrière Hospital, F-75013 Paris, France.
Carolane DauteuilleSorbonne Universités, UPMC Univ Paris 06, Institute of Cardiometabolism and Nutrition (ICAN), UMR_S 1166, Hôpital de la Pitié, Paris 75013, France.
Michèle ChabertSorbonne Universités, UPMC Univ Paris 06, INSERM, Université Paris-Descartes, Sorbonne Paris Cité, UMR_S 1138, Centre de Recherche des Cordeliers, Paris 75006, France.
Riccardo PorcariCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
Christopher A WaudbyInstitute of Structural and Molecular Biology, University College London and Birkbeck College, University of London, London WC1E 6BT, UK.
Annalisa ReliniDepartment of Physics, University of Genoa, Via Dodecaneso 33, Genoa 16146, Italy.
Philippa J TalmudCentre for Cardiovascular Genetics, Institute of Cardiovascular Science, University College London, London WC1E 6JF, UK.
Oleg KovrovDepartment of Medical Biosciences, Umeå University, Umeå SE-901 87, Sweden.
Gunilla OlivecronaDepartment of Medical Biosciences, Umeå University, Umeå SE-901 87, Sweden.
Monica StoppiniDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, Pavia 27100, Italy.
John ChristodoulouInstitute of Structural and Molecular Biology, University College London and Birkbeck College, University of London, London WC1E 6BT, UK.
Philip N HawkinsCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
Gilles GrateauHôpital Tenon, AP-HP, Service de Médecine Interne, Centre de référence des amyloses d'origine inflammatoire et de la fièvre méditerranéenne familiale, Paris 75020, France.
Marc DelpechUniversité Paris-Descartes, Sorbonne Paris Cité, Assistance Publique-Hôpitaux de Paris, Laboratoire de Biologie et Génétique Moléculaire, Hôpital Cochin, Paris 75014, France.
Anatol KontushSorbonne Universités, UPMC Univ Paris 06, Institute of Cardiometabolism and Nutrition (ICAN), UMR_S 1166, Hôpital de la Pitié, Paris 75013, France.
Julian D GillmoreCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
Athina D KalopissisSorbonne Universités, UPMC Univ Paris 06, INSERM, Université Paris-Descartes, Sorbonne Paris Cité, UMR_S 1138, Centre de Recherche des Cordeliers, Paris 75006, France.
Vittorio BellottiCentre for Amyloidosis and Acute Phase Proteins, National Amyloidosis Centre, University College London, London NW3 2PF, UK.
University College London · GBFondation pour l’innovation en Cadiométabolisme et Nutrition · FRUmeå University · SEUniversité Paris Cité · FRUniversity of Pavia · ITCentre de Recherche des Cordeliers · FRCentre Hospitalier Universitaire de Poitiers · FRHôpital Cochin · FRHôpital de la Conception · FRHôpital Tenon · FRMayo Clinic · USSorbonne Université · FRUniversité de Montpellier · FRUniversité de Poitiers · FRUniversity of Genoa · IT

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
British Heart Foundation PG08/008Department of HealthMedical Research Council MC_U117533887Medical Research Council MR/K000187/1NCI NIH HHS P30 CA008748Telethon GGP14127Wellcome TrustWellcome Trust 097806/Z/11/Z
6 · The paper itself

Abstract

Apolipoprotein C-III deficiency provides cardiovascular protection, but apolipoprotein C-III is not known to be associated with human amyloidosis. Here we report a form of amyloidosis characterized by renal insufficiency caused by a new apolipoprotein C-III variant, D25V. Despite their uremic state, the D25V-carriers exhibit low triglyceride (TG) and apolipoprotein C-III levels, and low very-low-density lipoprotein (VLDL)/high high-density lipoprotein (HDL) profile. Amyloid fibrils comprise the D25V-variant only, showing that wild-type apolipoprotein C-III does not contribute to amyloid deposition in vivo. The mutation profoundly impacts helical structure stability of D25V-variant, which is remarkably fibrillogenic under physiological conditions in vitro producing typical amyloid fibrils in its lipid-free form. D25V apolipoprotein C-III is a new human amyloidogenic protein and the first conferring cardioprotection even in the unfavourable context of renal failure, extending the evidence for an important cardiovascular protective role of apolipoprotein C-III deficiency. Thus, fibrate therapy, which reduces hepatic APOC3 transcription, may delay amyloid deposition in affected patients.

Indexed as

Mutation, MissenseAdultAgedAged, 80 and overAmyloidosisApolipoprotein C-IIIBase SequenceCardiovascular DiseasesFemaleFranceHumansHyperlipoproteinemiasLipoproteins, HDLLipoproteins, VLDLMaleMiddle AgedApolipoprotein C-IIILipoproteins, HDLLipoproteins, VLDL

Identifiers

PMID26790392
PMCPMC4735822
OpenAlexW2269123435

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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.