Evidence map›Paper›PMID 24358354›Full record

ArticlePloS one2013

Co-expression of SERCA isoforms, phospholamban and sarcolipin in human skeletal muscle fibers.

Val A Fajardo, Eric Bombardier, Chris Vigna, Tahira Devji, Darin Bloemberg, Daniel Gamu, Anthony O Gramolini, Joe Quadrilatero, A Russell Tupling

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 80 citations in OpenAlex.

  1. Effects of electromyostimulation on sarcolipin and CaBiochemistry and biophysics reports · 2026
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  8. Hypermetabolism in mice carrying a near complete human chromosome 21.bioRxiv : the preprint server for biology · 2023
    Article
  9. Review
  10. Altered skeletal muscle sarco-endoplasmic reticulum CaAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2022
    Article
  11. Review
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  13. CaProceedings of the National Academy of Sciences of the United States of America · 2022
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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

9 authors at 2 institutions in 1 country.

Val A FajardoDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Eric BombardierDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Chris VignaDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Tahira DevjiDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Darin BloembergDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Daniel GamuDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
Anthony O GramoliniDepartment of Physiology, University of Toronto, Toronto, Ontario, Canada.
Joe QuadrilateroDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
A Russell TuplingDepartment of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada.
University of Waterloo · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP 106566
6 · The paper itself

Abstract

Sarcolipin (SLN) and phospholamban (PLN) inhibit the activity of sarco(endo)plasmic reticulum Ca(2+)-ATPases (SERCAs) by reducing their apparent affinity for Ca(2+). A ternary complex between SLN, PLN, and SERCAs results in super-inhibition of SERCA activity. Analysis of skeletal muscle homogenate has limited our current understanding of whether SLN and PLN regulate SERCA1a, SERCA2a, or both in skeletal muscle and whether SLN and PLN are co-expressed in skeletal muscle fibers. Biopsies from human vastus lateralis were analyzed through single fiber Western blotting and immunohisto/fluorescence staining to circumvent this limitation. With a newly generated SLN antibody, we report for the first time that SLN protein is present in human skeletal muscle. Addition of the SLN antibody (50 µg) to vastus lateralis homogenates increased the apparent Ca(2+) affinity of SERCA (K Ca, pCa units) (-Ab, 5.85 ± 0.02 vs. +Ab, 5.95 ± 0.02) and maximal SERCA activity (μmol/g protein/min) (-Ab, 122 ± 6.4 vs. +Ab, 159 ± 11) demonstrating a functional interaction between SLN and SERCAs in human vastus lateralis. Specifically, our results suggest that although SLN and PLN may preferentially regulate SERCA1a, and SERCA2a, respectively, physiologically they both may regulate either SERCA isoform. Furthermore, we show that SLN and PLN co-immunoprecipitate in human vastus lateralis homogenate and are simultaneously expressed in 81% of the fibers analyzed with Western blotting which implies that super-inhibition of SERCA may exist in human skeletal muscle. Finally, we demonstrate unequivocally that mouse soleus contains PLN protein suggesting that super-inhibition of SERCA may also be important physiologically in rodent skeletal muscle.

Indexed as

AdolescentAdultAnimalsCalciumCalcium-Binding ProteinsEnzyme ActivationGene ExpressionHumansIsoenzymesMaleMiceMuscle Fibers, Fast-TwitchMuscle Fibers, SkeletalMuscle Fibers, Slow-TwitchMuscle ProteinsMyosin Heavy ChainsCalciumCalcium-Binding ProteinsIsoenzymesMuscle ProteinsMyosin Heavy ChainsPhospholambanProteolipidssarcolipinSarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID24358354
PMCPMC3865254
OpenAlexW2035073601

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.