The expression of heat shock protein in human skeletal muscle: effects of muscle fibre phenotype and training background. (15th June 2013)
- Record Type:
- Journal Article
- Title:
- The expression of heat shock protein in human skeletal muscle: effects of muscle fibre phenotype and training background. (15th June 2013)
- Main Title:
- The expression of heat shock protein in human skeletal muscle: effects of muscle fibre phenotype and training background
- Authors:
- Folkesson, M.
Mackey, A. L.
Langberg, H.
Oskarsson, E.
Piehl‐Aulin, K.
Henriksson, J.
Kadi, F. - Abstract:
- <abstract abstract-type="main" id="apha12124-abs-0001"> <title>Abstract</title> <sec id="apha12124-sec-0001" sec-type="section"> <title>Aim</title> <p>Exercise‐induced adaptations of skeletal muscle are related to training mode and can be muscle fibre type specific. This study aimed to investigate heat shock protein expression in type I and type II muscle fibres in resting skeletal muscle of subjects with different training backgrounds.</p> </sec> <sec id="apha12124-sec-0002" sec-type="section"> <title>Methods</title> <p>Three groups of subjects were included: healthy active not engaged in any training programme (ACT, <italic> n </italic>= 12), resistance trained (RES, <italic> n </italic>= 6) and endurance trained (END, <italic> n </italic>= 8). Biopsies were obtained from vastus lateralis, and immunohistochemistry was performed using monoclonal antibodies against myosin heavy chain I and IIA, αB‐crystallin, HSP27, HSP60 and HSP70.</p> </sec> <sec id="apha12124-sec-0003" sec-type="section"> <title>Results</title> <p>In ACT and RES, but not in END, a fibre type–specific expression with higher staining intensity in type I than type II fibres was seen for αB‐crystallin. The opposite (II &gt; I) was found for HSP27 in subjects from ACT (6 of 12 subjects) and RES (3 of 6), whereas all subjects from END displayed uniform staining. HSP60 showed no fibre‐specific expression. HSP70 displayed a fibre‐specific expression pattern (I &gt; II) in ACT (4 of 12), but not in END or RES.</p><abstract abstract-type="main" id="apha12124-abs-0001"> <title>Abstract</title> <sec id="apha12124-sec-0001" sec-type="section"> <title>Aim</title> <p>Exercise‐induced adaptations of skeletal muscle are related to training mode and can be muscle fibre type specific. This study aimed to investigate heat shock protein expression in type I and type II muscle fibres in resting skeletal muscle of subjects with different training backgrounds.</p> </sec> <sec id="apha12124-sec-0002" sec-type="section"> <title>Methods</title> <p>Three groups of subjects were included: healthy active not engaged in any training programme (ACT, <italic> n </italic>= 12), resistance trained (RES, <italic> n </italic>= 6) and endurance trained (END, <italic> n </italic>= 8). Biopsies were obtained from vastus lateralis, and immunohistochemistry was performed using monoclonal antibodies against myosin heavy chain I and IIA, αB‐crystallin, HSP27, HSP60 and HSP70.</p> </sec> <sec id="apha12124-sec-0003" sec-type="section"> <title>Results</title> <p>In ACT and RES, but not in END, a fibre type–specific expression with higher staining intensity in type I than type II fibres was seen for αB‐crystallin. The opposite (II &gt; I) was found for HSP27 in subjects from ACT (6 of 12 subjects) and RES (3 of 6), whereas all subjects from END displayed uniform staining. HSP60 showed no fibre‐specific expression. HSP70 displayed a fibre‐specific expression pattern (I &gt; II) in ACT (4 of 12), but not in END or RES.</p> </sec> <sec id="apha12124-sec-0004" sec-type="section"> <title>Conclusion</title> <p>This study shows that the level of expression of the different HSPs in human skeletal muscle is influenced by muscle fibre phenotype. The fibre type–specific expression of HSP70 is influenced by resistance and endurance training, whereas those of αB‐crystallin and HSP27 is influenced only by endurance training, suggesting the existence of a training‐modality‐specific action on the adaptive processes including heat shock proteins in human skeletal muscle.</p> </sec> </abstract> … (more)
- Is Part Of:
- Acta physiologica. Volume 209:Number 1(2013:Sep.)
- Journal:
- Acta physiologica
- Issue:
- Volume 209:Number 1(2013:Sep.)
- Issue Display:
- Volume 209, Issue 1 (2013)
- Year:
- 2013
- Volume:
- 209
- Issue:
- 1
- Issue Sort Value:
- 2013-0209-0001-0000
- Page Start:
- 26
- Page End:
- 33
- Publication Date:
- 2013-06-15
- Subjects:
- Physiology -- Periodicals
Physiology -- Research -- Periodicals
612 - Journal URLs:
- http://www.blackwell-synergy.com/loi/aps ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1748-1716 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/apha.12124 ↗
- Languages:
- English
- ISSNs:
- 1748-1708
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0650.750000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3956.xml