Histochemistry and Cell Biology

, Volume 148, Issue 5, pp 545–555 | Cite as

Human skeletal muscle type 1 fibre distribution and response of stress-sensing proteins along the titin molecule after submaximal exhaustive exercise

  • Satu O. A. Koskinen
  • Heikki Kyröläinen
  • Riina Flink
  • Harri P. Selänne
  • Sheila S. Gagnon
  • Juha P. Ahtiainen
  • Bradley C. Nindl
  • Maarit Lehti
Original Paper


Early responses of stress-sensing proteins, muscle LIM protein (MLP), ankyrin repeat proteins (Ankrd1/CARP and Ankrd2/Arpp) and muscle-specific RING finger proteins (MuRF1 and MuRF2), along the titin molecule were investigated in the present experiment after submaximal exhaustive exercise. Ten healthy men performed continuous drop jumping unilaterally on a sledge apparatus with a submaximal height until complete exhaustion. Five stress-sensing proteins were analysed by mRNA measurements from biopsies obtained immediately and 3 h after the exercise from exercised vastus lateralis muscle while control biopsies were obtained from non-exercised legs before the exercise. Decreased maximal jump height and increased serum creatine kinase activities as indirect markers for muscle damage and HSP27 immunostainings on muscle biopsies as a direct marker for muscle damage indicated that the current exercised protocol caused muscle damage. mRNA levels for four (MLP, Ankrd1/CARP, MuRF1 and MuRF2) out of the five studied stress sensors significantly (p < 0.05) increased 3 h after fatiguing exercise. The magnitude of MLP and Ankrd2 responses was related to the proportion of type 1 myofibres. Our data showed that the submaximal exhaustive exercise with subject’s own physical fitness level activates titin-based stretch-sensing proteins. These results suggest that both degenerative and regenerative pathways are activated in very early phase after the exercise or probably already during the exercise. Activation of these proteins represents an initial step forward adaptive remodelling of the exercised muscle and may also be involved in the initiation of myofibre repair.


Human skeletal muscle Exercise induced muscle damage Titin Stress-sensing proteins 



The authors thank all the test personnel for their work in the data collection. We also would like to express our special thanks to Ms. Aila Ollikainen and Mr. Risto Puurtinen for their assistance in the blood and muscle analyses. This work was supported by a grant from the Scientific Advisory Board for Defence, Finland, Academy of Finland (Research Council for Health, Grant No. 137981) and Foundation for Physical Activity and Public Health LIKES, Finland. Sheila S. Gagnon is supported in part as a doctoral student by Western University’s Bone and Joint Institute and the Collaborative Training Program in Musculoskeletal Health Research.

Compliance with ethical standards

Conflict of interest

The authors declare they have no conflict of interest.

Supplementary material

418_2017_1595_MOESM1_ESM.docx (3 mb)
Supplementary material 1 (DOCX 3062 kb)


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Copyright information

© Springer-Verlag GmbH Germany 2017

Authors and Affiliations

  1. 1.LIKES Research Centre for Physical Activity and HealthJyväskyläFinland
  2. 2.Unit of Biology of Physical Activity, Faculty of Sport and Health SciencesUniversity of JyväskyläJyväskyläFinland
  3. 3.Department of PsychologyUniversity of JyväskyläJyväskyläFinland
  4. 4.Hospital MehiläinenSports Injury ClinicHelsinkiFinland
  5. 5.Wolf Orthopaedic Biomechanics Laboratory, Fowler Kennedy Sport Medicine ClinicUniversity of Western OntarioLondonCanada
  6. 6.Neuromuscular Research Laboratory/Warrior Human Performance Research CenterUniversity of PittsburghPittsburghUSA

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