Evidence map›Paper›PMID 12181300›Full record

ArticleThe Journal of physiology2002

Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle.

L Féasson, D Stockholm, D Freyssenet, I Richard, S Duguez, J S Beckmann, C Denis

Abstract read
In one paragraph

Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

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5 more citing papers are in PubMed but not listed here.

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.

L FéassonLaboratoire de Physiologie et Physiopathologie de l' Exercice et du Handicap, Faculté de Médecine, Saint Etienne, France. Leonard.Feasson@univ-st-etienne.fr
D Stockholm
D Freyssenet
I Richard
S Duguez
J S Beckmann
C Denis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular events by which eccentric muscle contractions induce muscle damage and remodelling remain largely unknown. We assessed whether eccentric exercise modulates the expression of proteinases (calpains 1, 2 and 3, proteasome, cathepsin B+L), muscle structural proteins (alpha-sarcoglycan and desmin), and the expression of the heat shock proteins Hsp27 and alphaB-crystallin. Vastus lateralis muscle biopsies from twelve healthy male volunteers were obtained before, immediately after, and 1 and 14 days after a 30 min downhill treadmill running exercise. Eccentric exercise induced muscle damage as evidenced by the analysis of muscle pain and weakness, creatine kinase serum activity, myoglobinaemia and ultrastructural analysis of muscle biopsies. The calpain 3 mRNA level was decreased immediately after exercise whereas calpain 2 mRNA level was increased at day 1. Both mRNA levels returned to control values by day 14. By contrast, cathepsin B+L and proteasome enzyme activities were increased at day 14. The alpha-sarcoglycan protein level was decreased immediately after exercise and at day 1, whereas the desmin level peaked at day 14. alphaB-crystallin and Hsp27 protein levels were increased at days 1 and 14. Our results suggest that the differential expression of calpain 2 and 3 mRNA levels may be important in the process of exercise-induced muscle damage, whereas expression of alpha-sarcoglycan, desmin, alphaB-crystallin and Hsp27 may be essentially involved in the subsequent remodelling of myofibrillar structure. This remodelling response may limit the extent of muscle damage upon a subsequent mechanical stress.

Indexed as

Heat-Shock ProteinsActinsAdaptation, PhysiologicalAdultalpha-Crystallinsbeta-CrystallinsCalpainCysteine EndopeptidasesCytoskeletal ProteinsDesminExerciseGene ExpressionHSP27 Heat-Shock ProteinsHumansLysosomesMaleActinsalpha-Crystallinsbeta-CrystallinsCalpainCysteine EndopeptidasesCytoskeletal ProteinsDesminHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanMembrane GlycoproteinsMolecular ChaperonesMultienzyme ComplexesMuscle ProteinsNeoplasm ProteinsProteasome Endopeptidase ComplexRNA, MessengerSarcoglycans

Identifiers

PMID12181300
PMCPMC2290467

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.