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Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans
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2007 (English)In: American Journal of Physiology. Regulatory Integrative and Comparative Physiology, ISSN 0363-6119, E-ISSN 1522-1490, Vol. 293, no 2, p. R844-R853Article in journal (Refereed) Published
Abstract [en]

In this study the stress protein response to unaccustomed maximal eccentric exercise in humans was investigated. Eleven healthy males performed 300 maximal eccentric actions with the quadriceps muscle. Biopsies from vastus lateralis were collected at 30 min and 4, 8, 24, 96, and 168 h after exercise. Cellular regulation and localization of heat shock protein (HSP) 27, alpha B-crystallin, and HSP70 were analyzed by immunohistochemistry, ELISA technique, and Western blotting. Additionally, mRNA levels of HSP27, alpha B-crystallin, and HSP70 were quantified by Northern blotting. After exercise (30 min), 81 +/- 8% of the myofibers showed strong HSP27 staining (P < 0.01) that gradually decreased during the following week. alpha B-Crystallin mimicked the changes observed in HSP27. After exercise (30 min), the ELISA analysis showed a 49 +/- 13% reduction of the HSP27 level in the cytosolic fraction (P < 0.01), whereas Western blotting revealed a 15-fold increase of the HSP27 level in the myofibrillar fraction (P < 0.01). The cytosolic HSP70 level increased to 203 +/- 37% of the control level 24 h after exercise (P < 0.05). After 4 days, myofibrillar-bound HSP70 had increased approximately 10-fold (P < 0.01) and was accompanied by strong staining on cross sections. mRNA levels of HSP27, alpha B-crystallin, and HSP70 were all elevated the first day after exercise (P < 0.01); HSP70 mRNA showed the largest increase (20-fold at 8 h). HSP27 and alpha B-crystallin seemed to respond immediately to maximal eccentric exercise by binding to cytoskeletal/myofibrillar proteins, probably to function as stabilizers of disrupted myofibrillar structures. Later, mRNA and total HSP protein levels, especially HSP70, increased, indicating that HSPs play a role in skeletal muscle recovery and remodeling/adaptation processes to high-force exercise

Place, publisher, year, edition, pages
2007. Vol. 293, no 2, p. R844-R853
Keywords [en]
Adaptation; Physiological/physiology, Adult, Creatine Kinase/blood, Cytosol/metabolism, Exercise/*physiology, HSP70 Heat-Shock Proteins/genetics/*metabolism, Heat-Shock Proteins/genetics/*metabolism, Humans, Immunohistochemistry, Male, Myofibrils/*metabolism, Neoplasm Proteins/genetics/*metabolism, Pain/metabolism/physiopathology, Quadriceps Muscle/cytology/*physiology, RNA; Messenger/metabolism, Torque, alpha-Crystallin B Chain/genetics/metabolism
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Medical and Health Sciences Physiology Social Sciences Interdisciplinary Sport and Fitness Sciences
Research subject
Sports Science
Identifiers
URN: urn:nbn:se:oru:diva-4758DOI: 10.1152/ajpregu.00677.2006PubMedID: 17522120OAI: oai:DiVA.org:oru-4758DiVA, id: diva2:139057
Available from: 2008-11-24 Created: 2008-11-24 Last updated: 2018-01-13Bibliographically approved

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Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=17522120&dopt=Citation

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Kadi, Fawzi

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Kadi, Fawzi
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School of Health and Medical Sciences, Örebro University, Sweden
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