Evidence map›Paper›PMID 26430549›Full record

ArticleWorm

Investigating heart-specific toxicity of amyloidogenic immunoglobulin light chains: A lesson from C. elegans.

Luisa Diomede, Paola Rognoni, Francesca Lavatelli, Margherita Romeo, Andrea di Fonzo, Claudia Foray, Fabio Fiordaliso, Giovanni Palladini, Veronica Valentini, Vittorio Perfetti and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Worm. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact, top 92% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018
    Review
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

12 authors at 5 institutions in 3 countries.

Luisa DiomedeDepartment of Molecular Biochemistry and Pharmacology; IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri" ; Milan, Italy.
Paola RognoniAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy.
Francesca LavatelliAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy.
Margherita RomeoDepartment of Molecular Biochemistry and Pharmacology; IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri" ; Milan, Italy.
Andrea di FonzoAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy.
Claudia ForayBio-imaging Unit, Department of Cardiovascular Research; IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri" ; Milano, Italy.
Fabio FiordalisoBio-imaging Unit, Department of Cardiovascular Research; IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri" ; Milano, Italy.
Giovanni PalladiniAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy ; Department of Molecular Medicine; University of Pavia ; Pavia, Italy.
Veronica ValentiniAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy.
Vittorio PerfettiMedical Oncology Unit; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy.
Mario SalmonaDepartment of Molecular Biochemistry and Pharmacology; IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri" ; Milan, Italy.
Giampaolo MerliniAmyloid Research and Treatment Center; Foundation IRCCS Policlinico San Matteo ; Pavia, Italy ; Department of Molecular Medicine; University of Pavia ; Pavia, Italy.
Amyloidosis Foundation · USIstituti di Ricovero e Cura a Carattere Scientifico · ITPoliclinico San Matteo Fondazione · ITMario Negri Institute for Pharmacological Research · ITLaboratoire d’Imagerie Biomédicale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abnormalities in protein folding are involved in many localized and systemic diseases, all of which are characterized by insoluble amyloid formation and deposition. In immunoglobulin light chain (LC) amyloidosis, the most frequent systemic form of amyloidosis, the amyloid involvement of the heart dictates the prognosis and the elucidation of the mechanism of heart targeting and toxicity is essential for designing and testing new effective treatments. To this end, the availability of an appropriate animal model is crucial. We recently described the use of C. elegans as an innovative experimental system to investigate in vivo the pathogenic effects of monoclonal LC. This idea stems from the knowledge that the worm's pharynx is an "ancestral heart" with the additional ability to recognize stressor compounds. The feeding of worms with LC purified from patients suffering from cardiomyopathy, selectively and permanently impaired the pharyngeal function. This irreversible damage resulted in time, in a significant reduction in the lifespan of worms. We also reported that the ability of LC to generate reactive oxygen species was associated with their toxic effects and was counteracted by anti-oxidant compounds. This new nematode-based assay represents a promising model for elucidating the heart-specific toxicity of LC and for a rapid screening of new therapeutic strategies.

Indexed as

amyloidosiscardiotoxicityC. elegansimmunoglobulin light chainspharynx

Identifiers

PMID26430549
PMCPMC4588172
OpenAlexW2023428012

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.