Evidence map›Paper›PMID 26733245›Full record

ArticlePhysiological reports2016

Immunofluorescence microscopy of SNAP23 in human skeletal muscle reveals colocalization with plasma membrane, lipid droplets, and mitochondria.

Juliette A Strauss, Christopher S Shaw, Helen Bradley, Oliver J Wilson, Thierry Dorval, James Pilling, Anton J M Wagenmakers

Open access · goldAbstract read
In one paragraph

Article in Physiological reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The synaptosome-associated protein 23 (SNAP23) is necessary for proper myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Muscle Lipid Droplets: Cellular Signaling to Exercise Physiology and Beyond.Trends in endocrinology and metabolism: TEM · 2020
    Review
  11. Article
  12. Article
  13. Article
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  15. Review
  16. 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

7 authors at 5 institutions in 4 countries.

Juliette A StraussResearch Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool, UK.
Christopher S ShawCentre for Physical Activity and Nutrition Research, School of Exercise and Nutrition Sciences, Deakin University, Geelong, Victoria, Australia.
Helen BradleySchool of Sport, Exercise and Rehabilitation Sciences, University of Birmingham, Edgbaston, UK.
Oliver J WilsonInstitute for Sport, Physical Activity and Leisure, Carnegie Faculty, Leeds Beckett University, Leeds, UK.
Thierry DorvalDiscovery Sciences, AstraZeneca R&D, Cambridge, UK.
James PillingDiscovery Sciences, AstraZeneca R&D, Cambridge, UK.
Anton J M WagenmakersResearch Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool, UK a.j.wagenmakers@ljmu.ac.uk.
AstraZeneca (United Kingdom) · GBLiverpool John Moores University · GBDeakin University · AULeeds Beckett University · GBUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptosomal-associated protein 23 (SNAP23) is a SNARE protein expressed abundantly in human skeletal muscle. Its established role is to mediate insulin-stimulated docking and fusion of glucose transporter 4 (GLUT4) with the plasma membrane. Recent in vitro research has proposed that SNAP23 may also play a role in the fusion of growing lipid droplets (LDs) and the channeling of LD-derived fatty acids (FAs) into neighboring mitochondria for β-oxidation. This study investigates the subcellular distribution of SNAP23 in human skeletal muscle using immunofluorescence microscopy to confirm that SNAP23 localization supports the three proposed metabolic roles. Percutaneous biopsies were obtained from the m. vastus lateralis of six lean, healthy males in the rested, overnight fasted state. Cryosections were stained with antibodies targeting SNAP23, the mitochondrial marker cytochrome c oxidase and the plasma membrane marker dystrophin, whereas intramuscular LDs were stained using the neutral lipid dye oil red O. SNAP23 displayed areas of intense punctate staining in the intracellular regions of all muscle fibers and continuous intense staining in peripheral regions of the cell. Quantitation of confocal microscopy images showed colocalization of SNAP23 with the plasma membrane marker dystrophin (Pearson's correlation coefficient r = 0.50 ± 0.01). The intense punctate intracellular staining colocalized primarily with the mitochondrial marker cytochrome C oxidase (r = 0.50 ± 0.012) and to a lesser extent with LDs (r = 0.21 ± 0.01) visualized with oil red O. We conclude that the observed subcellular distribution of SNAP23 in human skeletal muscle supports the three aforementioned metabolic roles.

Indexed as

Cell MembraneHumansLipid DropletsMaleMicroscopy, FluorescenceMitochondriaMuscle, SkeletalQb-SNARE ProteinsQc-SNARE ProteinsYoung AdultQb-SNARE ProteinsQc-SNARE ProteinsSNAP23 protein, humanGlucose transporter 4intramuscular triglyceridelipid dropletsmitochondriasynaptosomal‐associated protein 23

Identifiers

PMID26733245
PMCPMC4760398
OpenAlexW2267602878

What Socratic holds

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LicenceCC BY
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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 Socratic graph.