Evidence map›Paper›PMID 35852046›Full record

ArticleJournal of cachexia, sarcopenia and muscle2022

Sphingomyelinase activity promotes atrophy and attenuates force in human muscle fibres and is elevated in heart failure patients.

Karl Olsson, Arthur J Cheng, Mamdoh Al-Ameri, Nicolas Tardif, Michael Melin, Olav Rooyackers, Johanna T Lanner, Håkan Westerblad, Thomas Gustafsson, Joseph D Bruton and 1 more

Open access · goldAbstract read
In one paragraph

Article in Journal of cachexia, sarcopenia and muscle, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 1 synthesis or guideline pooled it, 9 citations in OpenAlex.

  1. Pooled it
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  5. 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

11 authors at 3 institutions in 2 countries.

Karl OlssonDepartment of Laboratory Medicine, Section of Clinical Physiology, Karolinska Institutet, Huddinge, Sweden.
Arthur J ChengDepartment of Physiology and Pharmacology, Biomedicum C5, Karolinska Institutet, Solna, Sweden.
Mamdoh Al-AmeriDepartment of Molecular Medicine and Surgery, Karolinska Institutet, Karolinska University Hospital Solna, Stockholm, Sweden.
Nicolas TardifDivision of Perioperative Medicine and Intensive Care, Karolinska University Hospital, Huddinge, Sweden.
Michael MelinDepartment of Laboratory Medicine, Section of Clinical Physiology, Karolinska Institutet, Huddinge, Sweden.
Olav RooyackersDivision of Perioperative Medicine and Intensive Care, Karolinska University Hospital, Huddinge, Sweden.
Johanna T LannerDepartment of Physiology and Pharmacology, Biomedicum C5, Karolinska Institutet, Solna, Sweden.
Håkan WesterbladDepartment of Physiology and Pharmacology, Biomedicum C5, Karolinska Institutet, Solna, Sweden.
Thomas GustafssonDepartment of Laboratory Medicine, Section of Clinical Physiology, Karolinska Institutet and Department of Clinical Physiology Karolinska Univ Hospital, Huddinge, Sweden.ORCID 0000-0002-1559-4206
Joseph D BrutonDepartment of Physiology and Pharmacology, Biomedicum C5, Karolinska Institutet, Solna, Sweden.
Eric RullmanDepartment of Laboratory Medicine, Section of Clinical Physiology, Karolinska Institutet and Department of Clinical Physiology Karolinska Univ Hospital, Huddinge, Sweden.ORCID 0000-0003-2854-7262
Karolinska Institutet · SEKarolinska University Hospital · SEYork University · CA

Funding

Swedish Heart Lung FoundationSwedish Research Council 2015-02338Swedish Research Council 2018-02576Swedish Research Council 2019-01629Swedish Research Council for Sports Science D2016-0036Swedish Research Council for Sports Science FO2017-0018Swedish Research Council for Sports Science FO2018-0019Swedish Research Council for Sports Science P2019-0060
6 · The paper itself

Abstract

backgroundActivation of sphingomyelinase (SMase) as a result of a general inflammatory response has been implicated as a mechanism underlying disease-related loss of skeletal muscle mass and function in several clinical conditions including heart failure. Here, for the first time, we characterize the effects of SMase activity on human muscle fibre contractile function and assess skeletal muscle SMase activity in heart failure patients.

methodsThe effects of SMase on force production and intracellular Ca

resultsSphingomyelinase reduced muscle fibre force production (-30%, P < 0.05) by impairing sarcoplasmic reticulum (SR) Ca

conclusionsThe present findings implicate activation of skeletal muscle SMase as a mechanism underlying human heart failure-related loss of muscle mass and function. Moreover, our findings strengthen the idea that SMase activation may underpin disease-related loss of muscle mass and function in other clinical conditions, acting as a common patophysiological mechanism for the myopathy often reported in diseases associated with a systemic inflammatory response.

Indexed as

Heart FailureSphingomyelin PhosphodiesteraseAgedAnimalsAtrophyHumansMiceMuscle Fibers, SkeletalProteasome Endopeptidase ComplexRibosomal ProteinsProteasome Endopeptidase ComplexRibosomal ProteinsSphingomyelin PhosphodiesteraseCa2+ sensitivity RNAseqHeart failureSkeletal muscleSphingomyelinas

Identifiers

PMID35852046
PMCPMC9530516
OpenAlexW4285799816

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.